{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,11,3]],"date-time":"2026-11-03T19:57:37Z","timestamp":1793735857030,"version":"4.6.1"},"reference-count":321,"publisher":"Springer Science and Business Media LLC","issue":"5","license":[{"start":{"date-parts":[[2025,3,26]],"date-time":"2025-03-26T00:00:00Z","timestamp":1742947200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0"},{"start":{"date-parts":[[2025,3,26]],"date-time":"2025-03-26T00:00:00Z","timestamp":1742947200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0"}],"funder":[{"DOI":"10.13039\/501100001659","name":"Deutsche Forschungsgemeinschaft","doi-asserted-by":"publisher","award":["517204983"],"award-info":[{"award-number":["517204983"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Leukemia"],"published-print":{"date-parts":[[2025,5]]},"abstract":"<jats:title>Abstract<\/jats:title>\n          <jats:p>The JAK pathway is central to mammalian cell communication, characterized by rapid responses, receptor versatility, and fine-tuned regulation. It involves Janus kinases (JAK1, JAK2, JAK3, TYK2), which are activated when natural ligands bind to receptors, leading to autophosphorylation and activation of STAT transcription factors [1, 2]. JAK-dependent signaling plays a pivotal role in coordinating cell communication networks across a broad spectrum of biological systems including development, immune responses, cell growth, and differentiation. JAKs are frequently mutated in the aging hematopoietic system [3, 4] and in hematopoietic cancers [5]. Thus, dysregulation of the pathway results in various diseases, including cancers and immune disorders. The binding of extracellular ligands to class I and II cytokine receptors initiates a critical signaling cascade through the activation of Janus kinases (JAKs). Upon ligand engagement, JAKs become activated and phosphorylate specific tyrosine residues on the receptor, creating docking sites for signal transducer and activator of transcription (STAT) proteins. Subsequent JAK-mediated phosphorylation of STATs enables their dimerization and nuclear translocation, where they function as transcription factors to modulate gene expression. Under physiological conditions, JAK-signaling is a tightly regulated mechanism that governs cellular responses to external cues, such as cytokines and growth factors, ensuring homeostasis and maintaining the functional integrity of tissues and organs. Highly defined regulation of JAK-signaling is essential for balancing cellular responses to inflammatory stimuli and growth signals, thus safeguarding tissue health. In contrast, dysregulated JAK-signaling results in chronic inflammation and unrestrained cellular proliferation associated with various diseases. Understanding the qualitative and quantitative differences at the interface of physiologic JAK-signaling and its aberrant activation in disease is crucial for the development of targeted therapies that precisely tune this pathway to target pathologic activation patterns while leaving homeostatic processes largely unaffected. Consequently, pharmaceutical research has targeted this pathway for drug development leading to the approval of several substances with different selectivity profiles towards individual JAKs. Yet, the precise impact of inhibitor selectivity and the complex interplay of different functional modules within normal and malignant cells remains incompletely understood. In this review, we summarize the current knowledge on JAK-signaling in health and disease and highlight recent advances and future directions in the field.<\/jats:p>","DOI":"10.1038\/s41375-025-02569-8","type":"journal-article","created":{"date-parts":[[2025,3,26]],"date-time":"2025-03-26T16:46:16Z","timestamp":1743007576000},"page":"1011-1030","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":67,"title":["Malignant JAK-signaling: at the interface of inflammation and malignant transformation"],"prefix":"10.1038","volume":"39","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-1010-3321","authenticated-orcid":false,"given":"Florian","family":"Perner","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Heike L.","family":"Pahl","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6565-3393","authenticated-orcid":false,"given":"Robert","family":"Zeiser","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2438-1955","authenticated-orcid":false,"given":"Florian H.","family":"Heidel","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2025,3,26]]},"reference":[{"key":"2569_CR1","doi-asserted-by":"crossref","first-page":"3857","DOI":"10.1016\/j.cell.2022.09.023","volume":"185","author":"RL Philips","year":"2022","unstructured":"Philips RL, Wang Y, Cheon H, Kanno Y, Gadina M, Sartorelli V, et al. The JAK-STAT pathway at 30: much learned, much more to do. Cell. 2022;185:3857\u20133876.","journal-title":"Cell"},{"key":"2569_CR2","doi-asserted-by":"crossref","first-page":"643","DOI":"10.1126\/science.aaw3242","volume":"367","author":"S Wilmes","year":"2020","unstructured":"Wilmes S, Hafer M, Vuorio J, Tucker JA, Winkelmann H, Lochte S, et al. Mechanism of homodimeric cytokine receptor activation and dysregulation by oncogenic mutations. Science. 2020;367:643\u2013652.","journal-title":"Science"},{"key":"2569_CR3","doi-asserted-by":"crossref","first-page":"2477","DOI":"10.1056\/NEJMoa1409405","volume":"371","author":"G Genovese","year":"2014","unstructured":"Genovese G, Kahler AK, Handsaker RE, Lindberg J, Rose SA, Bakhoum SF, et al. Clonal hematopoiesis and blood-cancer risk inferred from blood DNA sequence. N Engl J Med. 2014;371:2477\u201387.","journal-title":"N Engl J Med"},{"key":"2569_CR4","doi-asserted-by":"crossref","first-page":"2488","DOI":"10.1056\/NEJMoa1408617","volume":"371","author":"S Jaiswal","year":"2014","unstructured":"Jaiswal S, Fontanillas P, Flannick J, Manning A, Grauman PV, Mar BG, et al. Age-related clonal hematopoiesis associated with adverse outcomes. N Engl J Med. 2014;371:2488\u201398.","journal-title":"N Engl J Med"},{"key":"2569_CR5","doi-asserted-by":"crossref","first-page":"D777","DOI":"10.1093\/nar\/gkw1121","volume":"45","author":"SA Forbes","year":"2017","unstructured":"Forbes SA, Beare D, Boutselakis H, Bamford S, Bindal N, Tate J, et al. COSMIC: somatic cancer genetics at high-resolution. Nucleic Acids Res. 2017;45:D777\u2013D783.","journal-title":"Nucleic Acids Res"},{"key":"2569_CR6","doi-asserted-by":"crossref","first-page":"99","DOI":"10.2144\/btn-2022-0034","volume":"75","author":"R Sule","year":"2023","unstructured":"Sule R, Rivera G, Gomes AV. Western blotting (immunoblotting): history, theory, uses, protocol and problems. Biotechniques. 2023;75:99\u2013114.","journal-title":"Biotechniques"},{"key":"2569_CR7","doi-asserted-by":"crossref","first-page":"2335","DOI":"10.1016\/j.molcel.2022.05.022","volume":"82","author":"A Mund","year":"2022","unstructured":"Mund A, Brunner AD, Mann M. Unbiased spatial proteomics with single-cell resolution in tissues. Mol Cell. 2022;82:2335\u201349.","journal-title":"Mol Cell"},{"key":"2569_CR8","doi-asserted-by":"crossref","first-page":"427","DOI":"10.1038\/nrm2900","volume":"11","author":"C Choudhary","year":"2010","unstructured":"Choudhary C, Mann M. Decoding signalling networks by mass spectrometry-based proteomics. Nat Rev Mol Cell Biol. 2010;11:427\u201339.","journal-title":"Nat Rev Mol Cell Biol"},{"key":"2569_CR9","doi-asserted-by":"crossref","first-page":"255","DOI":"10.1038\/nbt0303-255","volume":"21","author":"M Mann","year":"2003","unstructured":"Mann M, Jensen ON. Proteomic analysis of post-translational modifications. Nat Biotechnol. 2003;21:255\u201361.","journal-title":"Nat Biotechnol"},{"key":"2569_CR10","doi-asserted-by":"crossref","first-page":"e1800113","DOI":"10.1002\/prca.201800113","volume":"13","author":"S Doll","year":"2019","unstructured":"Doll S, Gnad F, Mann M. The case for proteomics and phospho-proteomics in personalized cancer medicine. Proteomics Clin Appl. 2019;13:e1800113.","journal-title":"Proteomics Clin Appl"},{"key":"2569_CR11","doi-asserted-by":"crossref","first-page":"347","DOI":"10.1038\/nature19949","volume":"537","author":"R Aebersold","year":"2016","unstructured":"Aebersold R, Mann M. Mass-spectrometric exploration of proteome structure and function. Nature. 2016;537:347\u201355.","journal-title":"Nature"},{"key":"2569_CR12","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1038\/s41586-020-2968-3","volume":"588","author":"AK Jayavelu","year":"2020","unstructured":"Jayavelu AK, Schnoder TM, Perner F, Herzog C, Meiler A, Krishnamoorthy G, et al. Splicing factor YBX1 mediates persistence of JAK2-mutated neoplasms. Nature. 2020;588:157\u201363.","journal-title":"Nature"},{"key":"2569_CR13","doi-asserted-by":"crossref","first-page":"1871172","DOI":"10.1080\/23723556.2020.1871172","volume":"8","author":"TM Schnoeder","year":"2021","unstructured":"Schnoeder TM, Perner F, Heidel FHA. JAK of all trades: how global phosphoproteomics reveal the Achilles heel of MPNs. Mol Cell Oncol. 2021;8:1871172.","journal-title":"Mol Cell Oncol"},{"key":"2569_CR14","doi-asserted-by":"crossref","first-page":"205","DOI":"10.1038\/s41577-019-0131-x","volume":"19","author":"G Altan-Bonnet","year":"2019","unstructured":"Altan-Bonnet G, Mukherjee R. Cytokine-mediated communication: a quantitative appraisal of immune complexity. Nat Rev Immunol. 2019;19:205\u201317.","journal-title":"Nat Rev Immunol"},{"key":"2569_CR15","doi-asserted-by":"crossref","first-page":"159","DOI":"10.1016\/S1074-7613(03)00211-5","volume":"19","author":"JL Boulay","year":"2003","unstructured":"Boulay JL, O'Shea JJ, Paul WE. Molecular phylogeny within type I cytokines and their cognate receptors. Immunity. 2003;19:159\u201363.","journal-title":"Immunity"},{"key":"2569_CR16","doi-asserted-by":"crossref","first-page":"667","DOI":"10.1038\/nri1153","volume":"3","author":"JC Renauld","year":"2003","unstructured":"Renauld JC. Class II cytokine receptors and their ligands: key antiviral and inflammatory modulators. Nat Rev Immunol. 2003;3:667\u201376.","journal-title":"Nat Rev Immunol"},{"key":"2569_CR17","doi-asserted-by":"crossref","first-page":"92","DOI":"10.1126\/science.8272873","volume":"263","author":"N Stahl","year":"1994","unstructured":"Stahl N, Boulton TG, Farruggella T, Ip NY, Davis S, Witthuhn BA, et al. Association and activation of Jak-Tyk kinases by CNTF-LIF-OSM-IL-6 beta receptor components. Science. 1994;263:92\u201395.","journal-title":"Science"},{"key":"2569_CR18","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1038\/ni875","volume":"4","author":"SV Kotenko","year":"2003","unstructured":"Kotenko SV, Gallagher G, Baurin VV, Lewis-Antes A, Shen M, Shah NK, et al. IFN-lambdas mediate antiviral protection through a distinct class II cytokine receptor complex. Nat Immunol. 2003;4:69\u201377.","journal-title":"Nat Immunol"},{"key":"2569_CR19","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1038\/375247a0","volume":"375","author":"MB Marrero","year":"1995","unstructured":"Marrero MB, Schieffer B, Paxton WG, Heerdt L, Berk BC, Delafontaine P, et al. Direct stimulation of Jak\/STAT pathway by the angiotensin II AT1 receptor. Nature. 1995;375:247\u201350.","journal-title":"Nature"},{"key":"2569_CR20","doi-asserted-by":"crossref","first-page":"153","DOI":"10.1038\/370153a0","volume":"370","author":"BA Witthuhn","year":"1994","unstructured":"Witthuhn BA, Silvennoinen O, Miura O, Lai KS, Cwik C, Liu ET, et al. Involvement of the Jak-3 Janus kinase in signalling by interleukins 2 and 4 in lymphoid and myeloid cells. Nature. 1994;370:153\u20137.","journal-title":"Nature"},{"key":"2569_CR21","doi-asserted-by":"crossref","first-page":"1042","DOI":"10.1126\/science.7973658","volume":"266","author":"SM Russell","year":"1994","unstructured":"Russell SM, Johnston JA, Noguchi M, Kawamura M, Bacon CM, Friedmann M, et al. Interaction of IL-2R beta and gamma c chains with Jak1 and Jak3: implications for XSCID and XCID. Science. 1994;266:1042\u20135.","journal-title":"Science"},{"key":"2569_CR22","doi-asserted-by":"crossref","first-page":"227","DOI":"10.1016\/0092-8674(93)90414-L","volume":"74","author":"BA Witthuhn","year":"1993","unstructured":"Witthuhn BA, Quelle FW, Silvennoinen O, Yi T, Tang B, Miura O, et al. JAK2 associates with the erythropoietin receptor and is tyrosine phosphorylated and activated following stimulation with erythropoietin. Cell. 1993;74:227\u201336.","journal-title":"Cell"},{"key":"2569_CR23","doi-asserted-by":"crossref","first-page":"1070","DOI":"10.1126\/science.abi5200","volume":"374","author":"R Medzhitov","year":"2021","unstructured":"Medzhitov R. The spectrum of inflammatory responses. Science. 2021;374:1070\u20135.","journal-title":"Science"},{"key":"2569_CR24","doi-asserted-by":"crossref","first-page":"555","DOI":"10.1038\/s41586-020-2938-9","volume":"587","author":"NC Henderson","year":"2020","unstructured":"Henderson NC, Rieder F, Wynn TA. Fibrosis: from mechanisms to medicines. Nature. 2020;587:555\u201366.","journal-title":"Nature"},{"key":"2569_CR25","doi-asserted-by":"crossref","first-page":"177","DOI":"10.1038\/nature21363","volume":"542","author":"GS Hotamisligil","year":"2017","unstructured":"Hotamisligil GS. Inflammation, metaflammation and immunometabolic disorders. Nature. 2017;542:177\u201385.","journal-title":"Nature"},{"key":"2569_CR26","doi-asserted-by":"crossref","first-page":"307","DOI":"10.1038\/nature17039","volume":"529","author":"M Karin","year":"2016","unstructured":"Karin M, Clevers H. Reparative inflammation takes charge of tissue regeneration. Nature. 2016;529:307\u201315.","journal-title":"Nature"},{"key":"2569_CR27","doi-asserted-by":"crossref","first-page":"526","DOI":"10.1038\/s41577-021-00508-z","volume":"21","author":"AF Salvador","year":"2021","unstructured":"Salvador AF, de Lima KA, Kipnis J. Neuromodulation by the immune system: a focus on cytokines. Nat Rev Immunol. 2021;21:526\u201341.","journal-title":"Nat Rev Immunol"},{"key":"2569_CR28","doi-asserted-by":"crossref","first-page":"1290","DOI":"10.1038\/s41423-023-01043-8","volume":"20","author":"T Mamuladze","year":"2023","unstructured":"Mamuladze T, Kipnis J. Type 2 immunity in the brain and brain borders. Cell Mol Immunol. 2023;20:1290\u20139.","journal-title":"Cell Mol Immunol"},{"key":"2569_CR29","doi-asserted-by":"crossref","first-page":"454","DOI":"10.1038\/s41577-020-00487-7","volume":"21","author":"KE Zengeler","year":"2021","unstructured":"Zengeler KE, Lukens JR. Innate immunity at the crossroads of healthy brain maturation and neurodevelopmental disorders. Nat Rev Immunol. 2021;21:454\u201368.","journal-title":"Nat Rev Immunol"},{"key":"2569_CR30","doi-asserted-by":"crossref","first-page":"309","DOI":"10.1038\/s41577-021-00624-w","volume":"22","author":"H Baazim","year":"2022","unstructured":"Baazim H, Antonio-Herrera L, Bergthaler A. The interplay of immunology and cachexia in infection and cancer. Nat Rev Immunol. 2022;22:309\u201321.","journal-title":"Nat Rev Immunol"},{"key":"2569_CR31","doi-asserted-by":"crossref","first-page":"471","DOI":"10.1038\/s41577-021-00633-9","volume":"22","author":"YJ Crow","year":"2022","unstructured":"Crow YJ, Stetson DB. The type I interferonopathies: 10 years on. Nat Rev Immunol. 2022;22:471\u201383.","journal-title":"Nat Rev Immunol"},{"key":"2569_CR32","doi-asserted-by":"crossref","first-page":"250","DOI":"10.1038\/cmi.2010.5","volume":"7","author":"F Lafdil","year":"2010","unstructured":"Lafdil F, Miller AM, Ki SH, Gao B. Th17 cells and their associated cytokines in liver diseases. Cell Mol Immunol. 2010;7:250\u20134.","journal-title":"Cell Mol Immunol"},{"key":"2569_CR33","doi-asserted-by":"crossref","DOI":"10.1038\/s41598-021-92888-4","volume":"11","author":"A Murtha-Lemekhova","year":"2021","unstructured":"Murtha-Lemekhova A, Fuchs J, Ghamarnejad O, Nikdad M, Probst P, Hoffmann K. Influence of cytokines, circulating markers and growth factors on liver regeneration and post-hepatectomy liver failure: a systematic review and meta-analysis. Sci Rep. 2021;11:13739.","journal-title":"Sci Rep"},{"key":"2569_CR34","doi-asserted-by":"crossref","first-page":"453","DOI":"10.1038\/s41577-022-00816-y","volume":"23","author":"HJ Anders","year":"2023","unstructured":"Anders HJ, Kitching AR, Leung N, Romagnani P. Glomerulonephritis: immunopathogenesis and immunotherapy. Nat Rev Immunol. 2023;23:453\u201371.","journal-title":"Nat Rev Immunol"},{"key":"2569_CR35","doi-asserted-by":"crossref","first-page":"589","DOI":"10.1038\/s41385-019-0158-0","volume":"12","author":"WJ Branchett","year":"2019","unstructured":"Branchett WJ, Lloyd CM. Regulatory cytokine function in the respiratory tract. Mucosal Immunol. 2019;12:589\u2013600.","journal-title":"Mucosal Immunol"},{"key":"2569_CR36","doi-asserted-by":"crossref","first-page":"402","DOI":"10.1038\/s41392-021-00791-1","volume":"6","author":"X Hu","year":"2021","unstructured":"Hu X, Li J, Fu M, Zhao X, Wang W. The JAK\/STAT signaling pathway: from bench to clinic. Signal Transduct Target Ther. 2021;6:402.","journal-title":"Signal Transduct Target Ther"},{"key":"2569_CR37","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1126\/science.abn8933","volume":"376","author":"CR Glassman","year":"2022","unstructured":"Glassman CR, Tsutsumi N, Saxton RA, Lupardus PJ, Jude KM, Garcia KC. Structure of a Janus kinase cytokine receptor complex reveals the basis for dimeric activation. Science. 2022;376:163\u20139.","journal-title":"Science"},{"key":"2569_CR38","doi-asserted-by":"crossref","unstructured":"Herrera SC, Bach EA. JAK\/STAT signaling in stem cells and regeneration: from Drosophila to vertebrates. Development 2019;146:dev167643.","DOI":"10.1242\/dev.167643"},{"key":"2569_CR39","doi-asserted-by":"crossref","first-page":"1630","DOI":"10.1126\/science.277.5332.1630","volume":"277","author":"JE Darnell Jr","year":"1997","unstructured":"Darnell JE Jr. STATs and gene regulation. Science. 1997;277:1630\u20135.","journal-title":"Science"},{"key":"2569_CR40","doi-asserted-by":"crossref","first-page":"1415","DOI":"10.1126\/science.8197455","volume":"264","author":"JE Darnell Jr.","year":"1994","unstructured":"Darnell JE Jr., Kerr IM, Stark GR. Jak-STAT pathways and transcriptional activation in response to IFNs and other extracellular signaling proteins. Science (N. Y, NY). 1994;264:1415\u201321.","journal-title":"Science (N. Y, NY)"},{"key":"2569_CR41","doi-asserted-by":"crossref","first-page":"1347","DOI":"10.1126\/science.7871432","volume":"267","author":"MH Heim","year":"1995","unstructured":"Heim MH, Kerr IM, Stark GR, Darnell JE Jr. Contribution of STAT SH2 groups to specific interferon signaling by the Jak-STAT pathway. Science (N. Y, NY). 1995;267:1347\u20139.","journal-title":"Science (N. Y, NY)"},{"key":"2569_CR42","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1002\/(SICI)1521-1878(199901)21:1<47::AID-BIES6>3.0.CO;2-N","volume":"21","author":"R Starr","year":"1999","unstructured":"Starr R, Hilton DJ. Negative regulation of the JAK\/STAT pathway. Bioessays. 1999;21:47\u201352.","journal-title":"Bioessays"},{"key":"2569_CR43","doi-asserted-by":"crossref","first-page":"6985","DOI":"10.1128\/MCB.16.12.6985","volume":"16","author":"H Jiao","year":"1996","unstructured":"Jiao H, Berrada K, Yang W, Tabrizi M, Platanias LC, Yi T. Direct association with and dephosphorylation of Jak2 kinase by the SH2-domain-containing protein tyrosine phosphatase SHP-1. Mol Cell Biol. 1996;16:6985\u201392.","journal-title":"Mol Cell Biol"},{"key":"2569_CR44","doi-asserted-by":"crossref","first-page":"3845","DOI":"10.1073\/pnas.95.7.3845","volume":"95","author":"TS Migone","year":"1998","unstructured":"Migone TS, Cacalano NA, Taylor N, Yi T, Waldmann TA, Johnston JA. Recruitment of SH2-containing protein tyrosine phosphatase SHP-1 to the interleukin 2 receptor; loss of SHP-1 expression in human T-lymphotropic virus type I-transformed T cells. Proc Natl Acad Sci USA. 1998;95:3845\u201350.","journal-title":"Proc Natl Acad Sci USA"},{"key":"2569_CR45","doi-asserted-by":"crossref","first-page":"4925","DOI":"10.2741\/3051","volume":"13","author":"D Xu","year":"2008","unstructured":"Xu D, Qu CK. Protein tyrosine phosphatases in the JAK\/STAT pathway. Front Biosci. 2008;13:4925\u201332.","journal-title":"Front Biosci"},{"key":"2569_CR46","doi-asserted-by":"crossref","first-page":"307","DOI":"10.1038\/nrc1837","volume":"6","author":"A Ostman","year":"2006","unstructured":"Ostman A, Hellberg C, Bohmer FD. Protein-tyrosine phosphatases and cancer. Nat Rev Cancer. 2006;6:307\u201320.","journal-title":"Nat Rev Cancer"},{"key":"2569_CR47","doi-asserted-by":"crossref","first-page":"6396","DOI":"10.1128\/MCB.19.9.6396","volume":"19","author":"A Matsumoto","year":"1999","unstructured":"Matsumoto A, Seki Y, Kubo M, Ohtsuka S, Suzuki A, Hayashi I, et al. Suppression of STAT5 functions in liver, mammary glands, and T cells in cytokine-inducible SH2-containing protein 1 transgenic mice. Mol Cell Biol. 1999;19:6396\u2013407.","journal-title":"Mol Cell Biol"},{"key":"2569_CR48","doi-asserted-by":"crossref","first-page":"273","DOI":"10.1038\/s41573-022-00618-w","volume":"22","author":"SM Stanford","year":"2023","unstructured":"Stanford SM, Bottini N. Targeting protein phosphatases in cancer immunotherapy and autoimmune disorders. Nat Rev Drug Discov. 2023;22:273\u201394.","journal-title":"Nat Rev Drug Discov"},{"key":"2569_CR49","doi-asserted-by":"crossref","first-page":"410","DOI":"10.1038\/nri818","volume":"2","author":"WS Alexander","year":"2002","unstructured":"Alexander WS. Suppressors of cytokine signalling (SOCS) in the immune system. Nat Rev Immunol. 2002;2:410\u20136.","journal-title":"Nat Rev Immunol"},{"key":"2569_CR50","doi-asserted-by":"crossref","first-page":"2071","DOI":"10.1073\/pnas.96.5.2071","volume":"96","author":"JG Zhang","year":"1999","unstructured":"Zhang JG, Farley A, Nicholson SE, Willson TA, Zugaro LM, Simpson RJ, et al. The conserved SOCS box motif in suppressors of cytokine signaling binds to elongins B and C and may couple bound proteins to proteasomal degradation. Proc Natl Acad Sci USA. 1999;96:2071\u20136.","journal-title":"Proc Natl Acad Sci USA"},{"key":"2569_CR51","doi-asserted-by":"crossref","first-page":"114","DOI":"10.1073\/pnas.95.1.114","volume":"95","author":"DJ Hilton","year":"1998","unstructured":"Hilton DJ, Richardson RT, Alexander WS, Viney EM, Willson TA, Sprigg NS, et al. Twenty proteins containing a C-terminal SOCS box form five structural classes. Proc Natl Acad Sci USA. 1998;95:114\u20139.","journal-title":"Proc Natl Acad Sci USA"},{"key":"2569_CR52","doi-asserted-by":"crossref","first-page":"924","DOI":"10.1038\/43219","volume":"387","author":"T Naka","year":"1997","unstructured":"Naka T, Narazaki M, Hirata M, Matsumoto T, Minamoto S, Aono A, et al. Structure and function of a new STAT-induced STAT inhibitor. Nature. 1997;387:924\u20139.","journal-title":"Nature"},{"key":"2569_CR53","doi-asserted-by":"crossref","first-page":"917","DOI":"10.1038\/43206","volume":"387","author":"R Starr","year":"1997","unstructured":"Starr R, Willson TA, Viney EM, Murray LJ, Rayner JR, Jenkins BJ, et al. A family of cytokine-inducible inhibitors of signalling. Nature. 1997;387:917\u201321.","journal-title":"Nature"},{"key":"2569_CR54","doi-asserted-by":"crossref","first-page":"1309","DOI":"10.1093\/emboj\/18.5.1309","volume":"18","author":"H Yasukawa","year":"1999","unstructured":"Yasukawa H, Misawa H, Sakamoto H, Masuhara M, Sasaki A, Wakioka T, et al. The JAK-binding protein JAB inhibits Janus tyrosine kinase activity through binding in the activation loop. EMBO J. 1999;18:1309\u201320.","journal-title":"EMBO J"},{"key":"2569_CR55","doi-asserted-by":"crossref","first-page":"6493","DOI":"10.1073\/pnas.100135197","volume":"97","author":"SE Nicholson","year":"2000","unstructured":"Nicholson SE, De Souza D, Fabri LJ, Corbin J, Willson TA, Zhang JG, et al. Suppressor of cytokine signaling-3 preferentially binds to the SHP-2-binding site on the shared cytokine receptor subunit gp130. Proc Natl Acad Sci USA. 2000;97:6493\u20138.","journal-title":"Proc Natl Acad Sci USA"},{"key":"2569_CR56","doi-asserted-by":"crossref","first-page":"29338","DOI":"10.1074\/jbc.M003456200","volume":"275","author":"A Sasaki","year":"2000","unstructured":"Sasaki A, Yasukawa H, Shouda T, Kitamura T, Dikic I, Yoshimura A. CIS3\/SOCS-3 suppresses erythropoietin (EPO) signaling by binding the EPO receptor and JAK2. J Biol Chem. 2000;275:29338\u201347.","journal-title":"J Biol Chem"},{"key":"2569_CR57","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1093\/jb\/mvg004","volume":"133","author":"T Endo","year":"2003","unstructured":"Endo T, Sasaki A, Minoguchi M, Joo A, Yoshimura A. CIS1 interacts with the Y532 of the prolactin receptor and suppresses prolactin-dependent STAT5 activation. J Biochem. 2003;133:109\u201313.","journal-title":"J Biochem"},{"key":"2569_CR58","doi-asserted-by":"crossref","first-page":"14017","DOI":"10.1074\/jbc.272.22.14017","volume":"272","author":"CL Yu","year":"1997","unstructured":"Yu CL, Burakoff SJ. Involvement of proteasomes in regulating Jak-STAT pathways upon interleukin-2 stimulation. J Biol Chem. 1997;272:14017\u201320.","journal-title":"J Biol Chem"},{"key":"2569_CR59","doi-asserted-by":"crossref","first-page":"28185","DOI":"10.1074\/jbc.273.43.28185","volume":"273","author":"F Verdier","year":"1998","unstructured":"Verdier F, Chretien S, Muller O, Varlet P, Yoshimura A, Gisselbrecht S, et al. Proteasomes regulate erythropoietin receptor and signal transducer and activator of transcription 5 (STAT5) activation. Possible involvement of the ubiquitinated Cis protein. J Biol Chem. 1998;273:28185\u201390.","journal-title":"J Biol Chem"},{"key":"2569_CR60","doi-asserted-by":"crossref","first-page":"593","DOI":"10.1038\/nri1667","volume":"5","author":"K Shuai","year":"2005","unstructured":"Shuai K, Liu B. Regulation of gene-activation pathways by PIAS proteins in the immune system. Nat Rev Immunol. 2005;5:593\u2013605.","journal-title":"Nat Rev Immunol"},{"key":"2569_CR61","doi-asserted-by":"crossref","first-page":"1803","DOI":"10.1126\/science.278.5344.1803","volume":"278","author":"CD Chung","year":"1997","unstructured":"Chung CD, Liao J, Liu B, Rao X, Jay P, Berta P, et al. Specific inhibition of Stat3 signal transduction by PIAS3. Science. 1997;278:1803\u20135.","journal-title":"Science"},{"key":"2569_CR62","doi-asserted-by":"crossref","first-page":"10626","DOI":"10.1073\/pnas.95.18.10626","volume":"95","author":"B Liu","year":"1998","unstructured":"Liu B, Liao J, Rao X, Kushner SA, Chung CD, Chang DD, et al. Inhibition of Stat1-mediated gene activation by PIAS1. Proc Natl Acad Sci USA. 1998;95:10626\u201331.","journal-title":"Proc Natl Acad Sci USA"},{"key":"2569_CR63","doi-asserted-by":"crossref","unstructured":"Perner F, Perner C, Ernst T, Heidel FH. Roles of JAK2 in aging, inflammation, hematopoiesis and malignant transformation. Cells. 2019;8:854.","DOI":"10.3390\/cells8080854"},{"key":"2569_CR64","doi-asserted-by":"crossref","first-page":"673","DOI":"10.1038\/nrc2210","volume":"7","author":"RL Levine","year":"2007","unstructured":"Levine RL, Pardanani A, Tefferi A, Gilliland DG. Role of JAK2 in the pathogenesis and therapy of myeloproliferative disorders. Nat Rev Cancer. 2007;7:673\u201383.","journal-title":"Nat Rev Cancer"},{"key":"2569_CR65","doi-asserted-by":"crossref","first-page":"1144","DOI":"10.1038\/nature03546","volume":"434","author":"C James","year":"2005","unstructured":"James C, Ugo V, Le Couedic JP, Staerk J, Delhommeau F, Lacout C, et al. A unique clonal JAK2 mutation leading to constitutive signalling causes polycythaemia vera. Nature. 2005;434:1144\u20138.","journal-title":"Nature"},{"key":"2569_CR66","doi-asserted-by":"crossref","first-page":"387","DOI":"10.1016\/j.ccr.2005.03.023","volume":"7","author":"RL Levine","year":"2005","unstructured":"Levine RL, Wadleigh M, Cools J, Ebert BL, Wernig G, Huntly BJ, et al. Activating mutation in the tyrosine kinase JAK2 in polycythemia vera, essential thrombocythemia, and myeloid metaplasia with myelofibrosis. Cancer Cell. 2005;7:387\u201397.","journal-title":"Cancer Cell"},{"key":"2569_CR67","doi-asserted-by":"crossref","first-page":"4642","DOI":"10.1073\/pnas.1423201112","volume":"112","author":"HM Hammaren","year":"2015","unstructured":"Hammaren HM, Ungureanu D, Grisouard J, Skoda RC, Hubbard SR, Silvennoinen O. ATP binding to the pseudokinase domain of JAK2 is critical for pathogenic activation. Proc Natl Acad Sci USA. 2015;112:4642\u20137.","journal-title":"Proc Natl Acad Sci USA"},{"key":"2569_CR68","doi-asserted-by":"crossref","first-page":"1909","DOI":"10.1182\/blood.2022017578","volume":"141","author":"D Luque Paz","year":"2023","unstructured":"Luque Paz D, Kralovics R, Skoda RC. Genetic basis and molecular profiling in myeloproliferative neoplasms. Blood. 2023;141:1909\u201321.","journal-title":"Blood"},{"key":"2569_CR69","doi-asserted-by":"crossref","first-page":"459","DOI":"10.1056\/NEJMoa065202","volume":"356","author":"LM Scott","year":"2007","unstructured":"Scott LM, Tong W, Levine RL, Scott MA, Beer PA, Stratton MR, et al. JAK2 exon 12 mutations in polycythemia vera and idiopathic erythrocytosis. N Engl J Med. 2007;356:459\u201368.","journal-title":"N Engl J Med"},{"key":"2569_CR70","doi-asserted-by":"crossref","first-page":"2213","DOI":"10.1084\/jem.20131371","volume":"211","author":"P Lundberg","year":"2014","unstructured":"Lundberg P, Takizawa H, Kubovcakova L, Guo G, Hao-Shen H, Dirnhofer S, et al. Myeloproliferative neoplasms can be initiated from a single hematopoietic stem cell expressing JAK2-V617F. J Exp Med. 2014;211:2213\u201330.","journal-title":"J Exp Med"},{"key":"2569_CR71","doi-asserted-by":"crossref","first-page":"5296","DOI":"10.1074\/jbc.M109.040733","volume":"285","author":"M Funakoshi-Tago","year":"2010","unstructured":"Funakoshi-Tago M, Tago K, Abe M, Sonoda Y, Kasahara T. STAT5 activation is critical for the transformation mediated by myeloproliferative disorder-associated JAK2 V617F mutant. J Biol Chem. 2010;285:5296\u2013307.","journal-title":"J Biol Chem"},{"key":"2569_CR72","doi-asserted-by":"crossref","first-page":"268","DOI":"10.1182\/asheducation-2014.1.268","volume":"2014","author":"E Chen","year":"2014","unstructured":"Chen E, Mullally A. How does JAK2V617F contribute to the pathogenesis of myeloproliferative neoplasms? Hematology Am Soc Hematol Educ Program. 2014;2014:268\u201376.","journal-title":"Hematology Am Soc Hematol Educ Program"},{"key":"2569_CR73","doi-asserted-by":"crossref","first-page":"584","DOI":"10.1016\/j.ccr.2010.05.015","volume":"17","author":"A Mullally","year":"2010","unstructured":"Mullally A, Lane SW, Ball B, Megerdichian C, Okabe R, Al-Shahrour F, et al. Physiological Jak2V617F expression causes a lethal myeloproliferative neoplasm with differential effects on hematopoietic stem and progenitor cells. Cancer Cell. 2010;17:584\u201396.","journal-title":"Cancer Cell"},{"key":"2569_CR74","doi-asserted-by":"crossref","first-page":"2184","DOI":"10.1182\/bloodadvances.2020003291","volume":"5","author":"M Balliu","year":"2021","unstructured":"Balliu M, Calabresi L, Bartalucci N, Romagnoli S, Maggi L, Manfredini R, et al. Activated IL-6 signaling contributes to the pathogenesis of, and is a novel therapeutic target for, CALR-mutated MPNs. Blood Adv. 2021;5:2184\u201395.","journal-title":"Blood Adv"},{"key":"2569_CR75","doi-asserted-by":"crossref","first-page":"589048","DOI":"10.3389\/fimmu.2020.589048","volume":"11","author":"R Li","year":"2020","unstructured":"Li R, Sun N, Chen X, Li X, Zhao J, Cheng W, et al. JAK2(V617F) Mutation promoted IL-6 production and glycolysis via mediating PKM1 stabilization in macrophages. Front Immunol. 2020;11:589048.","journal-title":"Front Immunol"},{"key":"2569_CR76","doi-asserted-by":"crossref","first-page":"3943","DOI":"10.1182\/blood-2013-07-514208","volume":"123","author":"A Duek","year":"2014","unstructured":"Duek A, Lundberg P, Shimizu T, Grisouard J, Karow A, Kubovcakova L, et al. Loss of Stat1 decreases megakaryopoiesis and favors erythropoiesis in a JAK2-V617F-driven mouse model of MPNs. Blood. 2014;123:3943\u201350.","journal-title":"Blood"},{"key":"2569_CR77","doi-asserted-by":"crossref","unstructured":"Torres DG, Paes J, da Costa AG, Malheiro A, Silva GV, Mourao LPS, et al. JAK2 variant signaling: genetic, hematologic and immune implication in chronic myeloproliferative neoplasms. Biomolecules. 2022;12:291.","DOI":"10.3390\/biom12020291"},{"key":"2569_CR78","doi-asserted-by":"crossref","first-page":"e79478","DOI":"10.1371\/journal.pone.0079478","volume":"8","author":"T Kurosu","year":"2013","unstructured":"Kurosu T, Nagao T, Wu N, Oshikawa G, Miura O. Inhibition of the PI3K\/Akt\/GSK3 pathway downstream of BCR\/ABL, Jak2-V617F, or FLT3-ITD downregulates DNA damage-induced Chk1 activation as well as G2\/M arrest and prominently enhances induction of apoptosis. PLoS ONE. 2013;8:e79478.","journal-title":"PLoS ONE"},{"key":"2569_CR79","doi-asserted-by":"crossref","first-page":"667","DOI":"10.1111\/bjh.12308","volume":"161","author":"S Barrio","year":"2013","unstructured":"Barrio S, Gallardo M, Arenas A, Ayala R, Rapado I, Rueda D, et al. Inhibition of related JAK\/STAT pathways with molecular targeted drugs shows strong synergy with ruxolitinib in chronic myeloproliferative neoplasm. Br J Haematol. 2013;161:667\u201376.","journal-title":"Br J Haematol"},{"key":"2569_CR80","doi-asserted-by":"crossref","first-page":"334","DOI":"10.1111\/j.1365-2141.2010.08249.x","volume":"150","author":"S Oku","year":"2010","unstructured":"Oku S, Takenaka K, Kuriyama T, Shide K, Kumano T, Kikushige Y, et al. JAK2 V617F uses distinct signalling pathways to induce cell proliferation and neutrophil activation. Br J Haematol. 2010;150:334\u201344.","journal-title":"Br J Haematol"},{"key":"2569_CR81","first-page":"e24574","volume":"2","author":"A Wolf","year":"2013","unstructured":"Wolf A, Eulenfeld R, Gabler K, Rolvering C, Haan S, Behrmann I, et al. JAK2-V617F-induced MAPK activity is regulated by PI3K and acts synergistically with PI3K on the proliferation of JAK2-V617F-positive cells. JAKSTAT. 2013;2:e24574.","journal-title":"JAKSTAT"},{"key":"2569_CR82","doi-asserted-by":"crossref","first-page":"1596","DOI":"10.1172\/JCI98785","volume":"129","author":"S Stivala","year":"2019","unstructured":"Stivala S, Codilupi T, Brkic S, Baerenwaldt A, Ghosh N, Hao-Shen H, et al. Targeting compensatory MEK\/ERK activation increases JAK inhibitor efficacy in myeloproliferative neoplasms. J Clin Investig. 2019;129:1596\u2013611.","journal-title":"J Clin Investig"},{"key":"2569_CR83","doi-asserted-by":"crossref","first-page":"708","DOI":"10.1038\/leu.2008.27","volume":"22","author":"JA McCubrey","year":"2008","unstructured":"McCubrey JA, Steelman LS, Abrams SL, Bertrand FE, Ludwig DE, Basecke J, et al. Targeting survival cascades induced by activation of Ras\/Raf\/MEK\/ERK, PI3K\/PTEN\/Akt\/mTOR and Jak\/STAT pathways for effective leukemia therapy. Leukemia. 2008;22:708\u201322.","journal-title":"Leukemia"},{"key":"2569_CR84","first-page":"108","volume":"4","author":"T Kong","year":"2023","unstructured":"Kong T, Laranjeira ABA, Yang K, Fisher DAC, Yu L, Poittevin De La Fregonniere L, et al. DUSP6 mediates resistance to JAK2 inhibition and drives leukemic progression. Nat Cancer. 2023;4:108\u201327.","journal-title":"Nat Cancer"},{"key":"2569_CR85","doi-asserted-by":"crossref","first-page":"737","DOI":"10.1158\/2159-8290.CD-22-0952","volume":"14","author":"AJ Dunbar","year":"2024","unstructured":"Dunbar AJ, Bowman RL, Park YC, O'Connor K, Izzo F, Myers RM, et al. Jak2V617F reversible activation shows its essential requirement in myeloproliferative neoplasms. Cancer Discov. 2024;14:737\u201351.","journal-title":"Cancer Discov"},{"key":"2569_CR86","doi-asserted-by":"crossref","first-page":"1412","DOI":"10.1002\/j.1460-2075.1995.tb07127.x","volume":"14","author":"H Luo","year":"1995","unstructured":"Luo H, Hanratty WP, Dearolf CR. An amino acid substitution in the Drosophila hopTum-l Jak kinase causes leukemia-like hematopoietic defects. EMBO J. 1995;14:1412\u201320.","journal-title":"EMBO J"},{"key":"2569_CR87","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1007\/BF00279527","volume":"238","author":"WP Hanratty","year":"1993","unstructured":"Hanratty WP, Dearolf CR. The Drosophila Tumorous-lethal hematopoietic oncogene is a dominant mutation in the hopscotch locus. Mol Gen Genet. 1993;238:33\u201337.","journal-title":"Mol Gen Genet"},{"key":"2569_CR88","doi-asserted-by":"crossref","first-page":"2857","DOI":"10.1002\/j.1460-2075.1995.tb07285.x","volume":"14","author":"DA Harrison","year":"1995","unstructured":"Harrison DA, Binari R, Nahreini TS, Gilman M, Perrimon N. Activation of a Drosophila Janus kinase (JAK) causes hematopoietic neoplasia and developmental defects. EMBO J. 1995;14:2857\u201365.","journal-title":"EMBO J"},{"key":"2569_CR89","doi-asserted-by":"crossref","first-page":"381","DOI":"10.1038\/sj.leu.2404060","volume":"20","author":"CP Kratz","year":"2006","unstructured":"Kratz CP, Boll S, Kontny U, Schrappe M, Niemeyer CM, Stanulla M. Mutational screen reveals a novel JAK2 mutation, L611S, in a child with acute lymphoblastic leukemia. Leukemia. 2006;20:381\u20133.","journal-title":"Leukemia"},{"key":"2569_CR90","doi-asserted-by":"crossref","first-page":"94","DOI":"10.1038\/leu.2015.202","volume":"30","author":"AM Roncero","year":"2016","unstructured":"Roncero AM, Lopez-Nieva P, Cobos-Fernandez MA, Villa-Morales M, Gonzalez-Sanchez L, Lopez-Lorenzo JL, et al. Contribution of JAK2 mutations to T-cell lymphoblastic lymphoma development. Leukemia. 2016;30:94\u2013103.","journal-title":"Leukemia"},{"key":"2569_CR91","doi-asserted-by":"crossref","first-page":"186","DOI":"10.1016\/j.ijbiomac.2013.05.029","volume":"60","author":"F Li","year":"2013","unstructured":"Li F, Guo HY, Wang M, Geng HL, Bian MR, Cao J, et al. The effects of R683S (G) genetic mutations on the JAK2 activity, structure and stability. Int J Biol Macromol. 2013;60:186\u201395.","journal-title":"Int J Biol Macromol"},{"key":"2569_CR92","doi-asserted-by":"crossref","first-page":"3295","DOI":"10.1038\/s41375-021-01239-9","volume":"35","author":"G Carreno-Tarragona","year":"2021","unstructured":"Carreno-Tarragona G, Varghese LN, Sebastian E, Galvez E, Marin-Sanchez A, Lopez-Munoz N, et al. A typical acute lymphoblastic leukemia JAK2 variant, R683G, causes an aggressive form of familial thrombocytosis when germline. Leukemia. 2021;35:3295\u20138.","journal-title":"Leukemia"},{"key":"2569_CR93","doi-asserted-by":"crossref","first-page":"921","DOI":"10.1007\/s00277-021-04657-y","volume":"101","author":"RZ Xu","year":"2022","unstructured":"Xu RZ, Karsan A, Xu Z, Berry BR. A rare de novo pure erythroid leukemia with JAK2 R683S mutation. Annals Hematol. 2022;101:921\u20132.","journal-title":"Annals Hematol"},{"key":"2569_CR94","doi-asserted-by":"crossref","first-page":"574","DOI":"10.1038\/sj.leu.2404527","volume":"21","author":"H Kiyoi","year":"2007","unstructured":"Kiyoi H, Yamaji S, Kojima S, Naoe T. JAK3 mutations occur in acute megakaryoblastic leukemia both in Down syndrome children and non-Down syndrome adults. Leukemia. 2007;21:574\u20136.","journal-title":"Leukemia"},{"key":"2569_CR95","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1016\/j.ccr.2006.06.002","volume":"10","author":"DK Walters","year":"2006","unstructured":"Walters DK, Mercher T, Gu TL, O'Hare T, Tyner JW, Loriaux M, et al. Activating alleles of JAK3 in acute megakaryoblastic leukemia. Cancer Cell. 2006;10:65\u201375.","journal-title":"Cancer Cell"},{"key":"2569_CR96","doi-asserted-by":"crossref","first-page":"3092","DOI":"10.1182\/blood-2014-04-566687","volume":"124","author":"S Degryse","year":"2014","unstructured":"Degryse S, de Bock CE, Cox L, Demeyer S, Gielen O, Mentens N, et al. JAK3 mutants transform hematopoietic cells through JAK1 activation, causing T-cell acute lymphoblastic leukemia in a mouse model. Blood. 2014;124:3092\u2013100.","journal-title":"Blood"},{"key":"2569_CR97","doi-asserted-by":"crossref","first-page":"591","DOI":"10.1158\/2159-8290.CD-12-0028","volume":"2","author":"GC Koo","year":"2012","unstructured":"Koo GC, Tan SY, Tang T, Poon SL, Allen GE, Tan L, et al. Janus kinase 3-activating mutations identified in natural killer\/T-cell lymphoma. Cancer Discov. 2012;2:591\u20137.","journal-title":"Cancer Discov"},{"key":"2569_CR98","doi-asserted-by":"crossref","first-page":"515","DOI":"10.1016\/j.immuni.2012.03.016","volume":"36","author":"JL Casanova","year":"2012","unstructured":"Casanova JL, Holland SM, Notarangelo LD. Inborn errors of human JAKs and STATs. Immunity. 2012;36:515\u201328.","journal-title":"Immunity"},{"key":"2569_CR99","doi-asserted-by":"crossref","first-page":"255","DOI":"10.1002\/humu.1188","volume":"18","author":"LD Notarangelo","year":"2001","unstructured":"Notarangelo LD, Mella P, Jones A, de Saint Basile G, Savoldi G, Cranston T, et al. Mutations in severe combined immune deficiency (SCID) due to JAK3 deficiency. Hum Mutat. 2001;18:255\u201363.","journal-title":"Hum Mutat"},{"key":"2569_CR100","doi-asserted-by":"crossref","first-page":"727","DOI":"10.1016\/j.molimm.2004.04.014","volume":"41","author":"JJ O'Shea","year":"2004","unstructured":"O'Shea JJ, Husa M, Li D, Hofmann SR, Watford W, Roberts JL, et al. Jak3 and the pathogenesis of severe combined immunodeficiency. Mol Immunol. 2004;41:727\u201337.","journal-title":"Mol Immunol"},{"key":"2569_CR101","doi-asserted-by":"crossref","first-page":"238","DOI":"10.1182\/blood.2024024626","volume":"144","author":"Q Wei","year":"2024","unstructured":"Wei Q, Xu J. Chronic eosinophilic leukemia with a novel JAK1 mutation responds well to the JAK1\/2 inhibitor ruxolitinib. Blood. 2024;144:238.","journal-title":"Blood"},{"key":"2569_CR102","doi-asserted-by":"crossref","first-page":"751","DOI":"10.1084\/jem.20072182","volume":"205","author":"E Flex","year":"2008","unstructured":"Flex E, Petrangeli V, Stella L, Chiaretti S, Hornakova T, Knoops L, et al. Somatically acquired JAK1 mutations in adult acute lymphoblastic leukemia. J Exp Med. 2008;205:751\u20138.","journal-title":"J Exp Med"},{"key":"2569_CR103","doi-asserted-by":"crossref","first-page":"6773","DOI":"10.1074\/jbc.M807531200","volume":"284","author":"T Hornakova","year":"2009","unstructured":"Hornakova T, Staerk J, Royer Y, Flex E, Tartaglia M, Constantinescu SN, et al. Acute lymphoblastic leukemia-associated JAK1 mutants activate the Janus kinase\/STAT pathway via interleukin-9 receptor alpha homodimers. J Biol Chem. 2009;284:6773\u201381.","journal-title":"J Biol Chem"},{"key":"2569_CR104","doi-asserted-by":"crossref","unstructured":"Biggs CM, Cordeiro-Santanach A, Prykhozhij SV, Deveau AP, Lin Y, Del Bel KL, et al. Human JAK1 gain of function causes dysregulated myelopoeisis and severe allergic inflammation. JCI Insight. 2022;7:e150849.","DOI":"10.1172\/jci.insight.150849"},{"key":"2569_CR105","doi-asserted-by":"crossref","first-page":"e0176181","DOI":"10.1371\/journal.pone.0176181","volume":"12","author":"LA Albacker","year":"2017","unstructured":"Albacker LA, Wu J, Smith P, Warmuth M, Stephens PJ, Zhu P, et al. Loss of function JAK1 mutations occur at high frequency in cancers with microsatellite instability and are suggestive of immune evasion. PLoS ONE. 2017;12:e0176181.","journal-title":"PLoS ONE"},{"key":"2569_CR106","doi-asserted-by":"crossref","first-page":"188","DOI":"10.1158\/2159-8290.CD-16-1223","volume":"7","author":"DS Shin","year":"2017","unstructured":"Shin DS, Zaretsky JM, Escuin-Ordinas H, Garcia-Diaz A, Hu-Lieskovan S, Kalbasi A, et al. Primary resistance to PD-1 blockade mediated by JAK1\/2 mutations. Cancer Discov. 2017;7:188\u2013201.","journal-title":"Cancer Discov"},{"key":"2569_CR107","volume":"3","author":"Y Ren","year":"2013","unstructured":"Ren Y, Zhang Y, Liu RZ, Fenstermacher DA, Wright KL, Teer JK, et al. JAK1 truncating mutations in gynecologic cancer define new role of cancer-associated protein tyrosine kinase aberrations. Sci Rep. 2013;3:3042.","journal-title":"Sci Rep"},{"key":"2569_CR108","doi-asserted-by":"crossref","first-page":"819","DOI":"10.1056\/NEJMoa1604958","volume":"375","author":"JM Zaretsky","year":"2016","unstructured":"Zaretsky JM, Garcia-Diaz A, Shin DS, Escuin-Ordinas H, Hugo W, Hu-Lieskovan S, et al. Mutations associated with acquired resistance to PD-1 blockade in melanoma. N Engl J Med. 2016;375:819\u201329.","journal-title":"N Engl J Med"},{"key":"2569_CR109","doi-asserted-by":"crossref","first-page":"564","DOI":"10.1158\/2159-8290.CD-12-0504","volume":"3","author":"T Sanda","year":"2013","unstructured":"Sanda T, Tyner JW, Gutierrez A, Ngo VN, Glover J, Chang BH, et al. TYK2-STAT1-BCL2 pathway dependence in T-cell acute lymphoblastic leukemia. Cancer Discov. 2013;3:564\u201377.","journal-title":"Cancer Discov"},{"key":"2569_CR110","doi-asserted-by":"crossref","first-page":"821","DOI":"10.1038\/leu.2016.277","volume":"31","author":"E Waanders","year":"2017","unstructured":"Waanders E, Scheijen B, Jongmans MC, Venselaar H, van Reijmersdal SV, van Dijk AH, et al. Germline activating TYK2 mutations in pediatric patients with two primary acute lymphoblastic leukemia occurrences. Leukemia. 2017;31:821\u20138.","journal-title":"Leukemia"},{"key":"2569_CR111","doi-asserted-by":"crossref","unstructured":"Woss K, Simonovic N, Strobl B, Macho-Maschler S, Muller M. TYK2: an upstream kinase of STATs in cancer. Cancers. 2019;11:1728.","DOI":"10.3390\/cancers11111728"},{"key":"2569_CR112","unstructured":"Boisson-Dupuis S, Ramirez-Alejo N, Li Z, Patin E, Rao G, Kerner G, et al. Tuberculosis and impaired IL-23-dependent IFN-gamma immunity in humans homozygous for a common TYK2 missense variant. Sci Immunol. 2018;3:eaau8714."},{"key":"2569_CR113","doi-asserted-by":"crossref","first-page":"1309","DOI":"10.1126\/science.278.5341.1309","volume":"278","author":"V Lacronique","year":"1997","unstructured":"Lacronique V, Boureux A, Valle VD, Poirel H, Quang CT, Mauchauffe M, et al. A TEL-JAK2 fusion protein with constitutive kinase activity in human leukemia. Science. 1997;278:1309\u201312.","journal-title":"Science"},{"key":"2569_CR114","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1080\/10428194.2019.1658105","volume":"61","author":"JR Cook","year":"2020","unstructured":"Cook JR, Rogers HJ, Chandra PK, Prescott JL, Mukherjee S. Myeloid neoplasm with eosinophilia and ETV6-JAK2 fusion. Leuk Lymphoma. 2020;61:213\u20136.","journal-title":"Leuk Lymphoma"},{"key":"2569_CR115","doi-asserted-by":"crossref","first-page":"3891","DOI":"10.1182\/blood.V95.12.3891","volume":"95","author":"C Carron","year":"2000","unstructured":"Carron C, Cormier F, Janin A, Lacronique V, Giovannini M, Daniel MT, et al. TEL-JAK2 transgenic mice develop T-cell leukemia. Blood. 2000;95:3891\u20139.","journal-title":"Blood"},{"key":"2569_CR116","doi-asserted-by":"crossref","first-page":"1668","DOI":"10.1016\/j.exphem.2007.08.025","volume":"35","author":"V Najfeld","year":"2007","unstructured":"Najfeld V, Cozza A, Berkofsy-Fessler W, Prchal J, Scalise A. Numerical gain and structural rearrangements of JAK2, identified by FISH, characterize both JAK2617V\u2009>\u2009F-positive and -negative patients with Ph-negative MPD, myelodysplasia, and B-lymphoid neoplasms. Exp Hematol. 2007;35:1668\u201376.","journal-title":"Exp Hematol"},{"key":"2569_CR117","doi-asserted-by":"crossref","unstructured":"Reiter A, Walz C, Watmore A, Schoch C, Blau I, Schlegelberger B, et al. The t(8;9)(p22;p24) is a recurrent abnormality in chronic and acute leukemia that fuses PCM1 to JAK2. Cancer Res. 2005;65:2662\u20137.","DOI":"10.1158\/0008-5472.CAN-04-4263"},{"key":"2569_CR118","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1002\/ajh.26352","volume":"97","author":"W Shomali","year":"2022","unstructured":"Shomali W, Gotlib J. World Health Organization-defined eosinophilic disorders: 2022 update on diagnosis, risk stratification, and management. Am J Hematol. 2022;97:129\u201348.","journal-title":"Am J Hematol"},{"key":"2569_CR119","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1016\/j.cancergen.2016.03.002","volume":"209","author":"R He","year":"2016","unstructured":"He R, Greipp PT, Rangan A, Mai M, Chen D, Reichard KK, et al. BCR-JAK2 fusion in a myeloproliferative neoplasm with associated eosinophilia. Cancer Genet. 2016;209:223\u20138.","journal-title":"Cancer Genet"},{"key":"2569_CR120","doi-asserted-by":"crossref","first-page":"89923","DOI":"10.18632\/oncotarget.21027","volume":"8","author":"EMP Steeghs","year":"2017","unstructured":"Steeghs EMP, Jerchel IS, de Goffau-Nobel W, Hoogkamer AQ, Boer JM, Boeree A, et al. JAK2 aberrations in childhood B-cell precursor acute lymphoblastic leukemia. Oncotarget. 2017;8:89923\u201338.","journal-title":"Oncotarget"},{"key":"2569_CR121","doi-asserted-by":"crossref","first-page":"700","DOI":"10.1111\/bjh.17910","volume":"196","author":"CEJ Downes","year":"2022","unstructured":"Downes CEJ, Rehn J, Heatley SL, Yeung D, McClure BJ, White DL. Identification of a novel GOLGA4-JAK2 fusion gene in B-cell acute lymphoblastic leukaemia. Br J Haematol. 2022;196:700\u20135.","journal-title":"Br J Haematol"},{"key":"2569_CR122","doi-asserted-by":"crossref","first-page":"4056","DOI":"10.1182\/blood-2010-06-291310","volume":"117","author":"K Van Roosbroeck","year":"2011","unstructured":"Van Roosbroeck K, Cox L, Tousseyn T, Lahortiga I, Gielen O, Cauwelier B, et al. JAK2 rearrangements, including the novel SEC31A-JAK2 fusion, are recurrent in classical Hodgkin lymphoma. Blood. 2011;117:4056\u201364.","journal-title":"Blood"},{"key":"2569_CR123","doi-asserted-by":"crossref","first-page":"e108397","DOI":"10.15252\/embj.2021108397","volume":"41","author":"S Jurado","year":"2022","unstructured":"Jurado S, Fedl AS, Jaritz M, Kostanova-Poliakova D, Malin SG, Mullighan CG, et al. The PAX5-JAK2 translocation acts as dual-hit mutation that promotes aggressive B-cell leukemia via nuclear STAT5 activation. EMBO J. 2022;41:e108397.","journal-title":"EMBO J"},{"key":"2569_CR124","doi-asserted-by":"crossref","first-page":"1002140","DOI":"10.3389\/fcimb.2022.1002140","volume":"12","author":"F Ye","year":"2022","unstructured":"Ye F, Zhang W, Dong J, Peng M, Fan C, Deng W, et al. A novel STAT1 loss-of-function mutation associated with Mendelian susceptibility to mycobacterial disease. Front Cell Infect Microbiol. 2022;12:1002140.","journal-title":"Front Cell Infect Microbiol"},{"key":"2569_CR125","doi-asserted-by":"crossref","first-page":"1446","DOI":"10.1007\/s10875-021-01118-z","volume":"41","author":"CJA Duncan","year":"2021","unstructured":"Duncan CJA, Hambleton S. Human disease phenotypes associated with loss and gain of function mutations in STAT2: viral susceptibility and type I interferonopathy. J Clin Immunol. 2021;41:1446\u201356.","journal-title":"J Clin Immunol"},{"key":"2569_CR126","doi-asserted-by":"crossref","first-page":"654406","DOI":"10.3389\/fimmu.2021.654406","volume":"12","author":"W Zhang","year":"2021","unstructured":"Zhang W, Chen X, Gao G, Xing S, Zhou L, Tang X, et al. Clinical relevance of gain- and loss-of-function germline mutations in STAT1: a systematic review. Front Immunol. 2021;12:654406.","journal-title":"Front Immunol"},{"key":"2569_CR127","doi-asserted-by":"crossref","unstructured":"Gruber C, Martin-Fernandez M, Ailal F, Qiu X, Taft J, Altman J, et al. Homozygous STAT2 gain-of-function mutation by loss of USP18 activity in a patient with type I interferonopathy. J Exp Med. 2020;217:e20192319.","DOI":"10.1084\/jem.20192319"},{"key":"2569_CR128","doi-asserted-by":"crossref","first-page":"808","DOI":"10.1007\/s10875-023-01445-3","volume":"43","author":"G Zhu","year":"2023","unstructured":"Zhu G, Badonyi M, Franklin L, Seabra L, Rice GI, Anne Boland A, et al. Type I interferonopathy due to a homozygous loss-of-inhibitory function mutation in STAT2. J Clin Immunol. 2023;43:808\u201318.","journal-title":"J Clin Immunol"},{"key":"2569_CR129","doi-asserted-by":"crossref","unstructured":"Yadav PS, Feng S, Cong Q, Kim H, Liu Y, Yang Y. Stat3 loss in mesenchymal progenitors causes Job syndrome-like skeletal defects by reducing Wnt\/beta-catenin signaling. Proc Natl Acad Sci USA. 2021;118:e2020100118.","DOI":"10.1073\/pnas.2020100118"},{"key":"2569_CR130","doi-asserted-by":"crossref","first-page":"864","DOI":"10.1007\/s10875-021-01051-1","volume":"41","author":"C Tsilifis","year":"2021","unstructured":"Tsilifis C, Freeman AF, Gennery AR. STAT3 hyper-IgE syndrome-an update and unanswered questions. J Clin Immunol. 2021;41:864\u201380.","journal-title":"J Clin Immunol"},{"key":"2569_CR131","doi-asserted-by":"crossref","first-page":"977","DOI":"10.1056\/NEJMoa073003","volume":"357","author":"EF Remmers","year":"2007","unstructured":"Remmers EF, Plenge RM, Lee AT, Graham RR, Hom G, Behrens TW, et al. STAT4 and the risk of rheumatoid arthritis and systemic lupus erythematosus. N Engl J Med. 2007;357:977\u201386.","journal-title":"N Engl J Med"},{"key":"2569_CR132","doi-asserted-by":"crossref","first-page":"8873","DOI":"10.1007\/s11033-012-1754-1","volume":"39","author":"YL Liang","year":"2012","unstructured":"Liang YL, Wu H, Shen X, Li PQ, Yang XQ, Liang L, et al. Association of STAT4 rs7574865 polymorphism with autoimmune diseases: a meta-analysis. Mol Biol Rep. 2012;39:8873\u201382.","journal-title":"Mol Biol Rep"},{"key":"2569_CR133","doi-asserted-by":"crossref","first-page":"1016","DOI":"10.3899\/jrheum.091007","volume":"37","author":"RJ Palomino-Morales","year":"2010","unstructured":"Palomino-Morales RJ, Diaz-Gallo LM, Witte T, Anaya JM, Martin J. Influence of STAT4 polymorphism in primary Sjogren's syndrome. J Rheumatol. 2010;37:1016\u20139.","journal-title":"J Rheumatol"},{"key":"2569_CR134","doi-asserted-by":"crossref","DOI":"10.1038\/s41467-018-04521-0","volume":"9","author":"J Klammt","year":"2018","unstructured":"Klammt J, Neumann D, Gevers EF, Andrew SF, Schwartz ID, Rockstroh D, et al. Dominant-negative STAT5B mutations cause growth hormone insensitivity with short stature and mild immune dysregulation. Nat Commun. 2018;9:2105.","journal-title":"Nat Commun"},{"key":"2569_CR135","doi-asserted-by":"crossref","first-page":"16","DOI":"10.1016\/j.ghir.2015.12.006","volume":"28","author":"V Hwa","year":"2016","unstructured":"Hwa V. STAT5B deficiency: Impacts on human growth and immunity. Growth Horm IGF Res. 2016;28:16\u201320.","journal-title":"Growth Horm IGF Res"},{"key":"2569_CR136","doi-asserted-by":"crossref","first-page":"2347","DOI":"10.1182\/blood.2021010980","volume":"138","author":"S Kollmann","year":"2021","unstructured":"Kollmann S, Grausenburger R, Klampfl T, Prchal-Murphy M, Bastl K, Pisa H, et al. A STAT5B-CD9 axis determines self-renewal in hematopoietic and leukemic stem cells. Blood. 2021;138:2347\u201359.","journal-title":"Blood"},{"key":"2569_CR137","doi-asserted-by":"crossref","DOI":"10.1038\/s41467-019-10422-7","volume":"10","author":"ED de Araujo","year":"2019","unstructured":"de Araujo ED, Erdogan F, Neubauer HA, Meneksedag-Erol D, Manaswiyoungkul P, Eram MS, et al. Structural and functional consequences of the STAT5B(N642H) driver mutation. Nat Commun. 2019;10:2517.","journal-title":"Nat Commun"},{"key":"2569_CR138","doi-asserted-by":"crossref","unstructured":"Consortium SG-o-FI. Human germline gain-of-function in STAT6: from severe allergic disease to lymphoma and beyond. Trends Immunol. 2024;45:138\u201353.","DOI":"10.1016\/j.it.2023.12.003"},{"key":"2569_CR139","doi-asserted-by":"crossref","first-page":"787","DOI":"10.1056\/NEJMoa1110556","volume":"366","author":"C Harrison","year":"2012","unstructured":"Harrison C, Kiladjian JJ, Al-Ali HK, Gisslinger H, Waltzman R, Stalbovskaya V, et al. JAK inhibition with ruxolitinib versus best available therapy for myelofibrosis. N Engl J Med. 2012;366:787\u201398.","journal-title":"N Engl J Med"},{"key":"2569_CR140","doi-asserted-by":"crossref","first-page":"799","DOI":"10.1056\/NEJMoa1110557","volume":"366","author":"S Verstovsek","year":"2012","unstructured":"Verstovsek S, Mesa RA, Gotlib J, Levy RS, Gupta V, DiPersio JF, et al. A double-blind, placebo-controlled trial of ruxolitinib for myelofibrosis. N Engl J Med. 2012;366:799\u2013807.","journal-title":"N Engl J Med"},{"key":"2569_CR141","doi-asserted-by":"crossref","first-page":"e301","DOI":"10.1016\/S2352-3026(22)00046-1","volume":"9","author":"M Marchetti","year":"2022","unstructured":"Marchetti M, Vannucchi AM, Griesshammer M, Harrison C, Koschmieder S, Gisslinger H, et al. Appropriate management of polycythaemia vera with cytoreductive drug therapy: European LeukemiaNet 2021 recommendations. Lancet Haematol. 2022;9:e301\u2013e311.","journal-title":"Lancet Haematol"},{"key":"2569_CR142","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1186\/s13045-017-0417-z","volume":"10","author":"S Verstovsek","year":"2017","unstructured":"Verstovsek S, Mesa RA, Gotlib J, Gupta V, DiPersio JF, Catalano JV, et al. Long-term treatment with ruxolitinib for patients with myelofibrosis: 5-year update from the randomized, double-blind, placebo-controlled, phase 3 COMFORT-I trial. J Hematol Oncol. 2017;10:55.","journal-title":"J Hematol Oncol"},{"key":"2569_CR143","doi-asserted-by":"crossref","first-page":"1929","DOI":"10.1080\/14656566.2017.1404574","volume":"18","author":"M Griesshammer","year":"2017","unstructured":"Griesshammer M, Sadjadian P. The BCR-ABL1-negative myeloproliferative neoplasms: a review of JAK inhibitors in the therapeutic armamentarium. Expert Opin Pharmacother. 2017;18:1929\u201338.","journal-title":"Expert Opin Pharmacother"},{"key":"2569_CR144","doi-asserted-by":"crossref","unstructured":"Swaminathan M, Jain A, Choi SD, Pemmaraju N. Janus kinase inhibitor monotherapy and combination therapies for myelofibrosis: what's the current standard of care? Expert Rev. Hematol. 2024;17:1\u201312.","DOI":"10.1080\/17474086.2024.2409438"},{"key":"2569_CR145","doi-asserted-by":"crossref","first-page":"1954","DOI":"10.1182\/blood.2022017423","volume":"141","author":"F Passamonti","year":"2023","unstructured":"Passamonti F, Mora BMyelofibrosis. Blood. 2023;141:1954\u201370.","journal-title":"Blood"},{"key":"2569_CR146","doi-asserted-by":"crossref","DOI":"10.1007\/s11864-019-0604-y","volume":"20","author":"P Bose","year":"2019","unstructured":"Bose P, Alfayez M, Verstovsek S. New concepts of treatment for patients with myelofibrosis. Curr Treat Opt Oncol. 2019;20:5.","journal-title":"Curr Treat Opt Oncol"},{"key":"2569_CR147","doi-asserted-by":"crossref","first-page":"e317","DOI":"10.1016\/S2352-3026(17)30088-1","volume":"4","author":"CN Harrison","year":"2017","unstructured":"Harrison CN, Schaap N, Vannucchi AM, Kiladjian JJ, Tiu RV, Zachee P, et al. Janus kinase-2 inhibitor fedratinib in patients with myelofibrosis previously treated with ruxolitinib (JAKARTA-2): a single-arm, open-label, non-randomised, phase 2, multicentre study. Lancet Haematol. 2017;4:e317\u2013e324.","journal-title":"Lancet Haematol"},{"key":"2569_CR148","volume":"5","author":"A Pardanani","year":"2015","unstructured":"Pardanani A, Tefferi A, Jamieson C, Gabrail NY, Lebedinsky C, Gao G, et al. A phase 2 randomized dose-ranging study of the JAK2-selective inhibitor fedratinib (SAR302503) in patients with myelofibrosis. Blood Cancer J. 2015;5:e335.","journal-title":"Blood Cancer J"},{"key":"2569_CR149","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/s41375-020-0954-2","volume":"35","author":"M Talpaz","year":"2021","unstructured":"Talpaz M, Kiladjian JJFedratinib. A newly approved treatment for patients with myeloproliferative neoplasm-associated myelofibrosis. Leukemia. 2021;35:1\u201317.","journal-title":"Leukemia"},{"key":"2569_CR150","doi-asserted-by":"crossref","first-page":"3832","DOI":"10.1182\/blood-2013-12-543736","volume":"123","author":"S Spoerl","year":"2014","unstructured":"Spoerl S, Mathew NR, Bscheider M, Schmitt-Graeff A, Chen S, Mueller T, et al. Activity of therapeutic JAK 1\/2 blockade in graft-versus-host disease. Blood. 2014;123:3832\u201342.","journal-title":"Blood"},{"key":"2569_CR151","doi-asserted-by":"crossref","first-page":"1800","DOI":"10.1056\/NEJMoa1917635","volume":"382","author":"R Zeiser","year":"2020","unstructured":"Zeiser R, von Bubnoff N, Butler J, Mohty M, Niederwieser D, Or R, et al. For the REACH2 trial group. ruxolitinib for glucocorticoid-refractory acute graft-versus-host disease. N Eng J Med. 2020;382:1800\u201310.","journal-title":"N Eng J Med"},{"key":"2569_CR152","doi-asserted-by":"crossref","first-page":"228","DOI":"10.1056\/NEJMoa2033122","volume":"385","author":"R Zeiser","year":"2021","unstructured":"Zeiser R, Polverelli N, Ram R, Hashmi SK, Chakraverty R, Middeke JM, et al. For the REACH3 investigators. ruxolitinib for glucocorticoid-refractory chronic graft-versus-host disease. N Eng J Med. 2021;385:228\u201338.","journal-title":"N Eng J Med"},{"key":"2569_CR153","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1038\/s41584-021-00726-8","volume":"18","author":"Y Tanaka","year":"2022","unstructured":"Tanaka Y, Luo Y, O'Shea JJ, Nakayamada S. Janus kinase-targeting therapies in rheumatology: a mechanisms-based approach. Nature Rev Rheumatol. 2022;18:133\u201345.","journal-title":"Nature Rev Rheumatol"},{"key":"2569_CR154","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1186\/s41927-018-0031-x","volume":"2","author":"JM Parmentier","year":"2018","unstructured":"Parmentier JM, Voss J, Graff C, Schwartz A, Argiriadi M, Friedman M, et al. In vitro and in vivo characterization of the JAK1 selectivity of upadacitinib (ABT-494). BMC Rheumatol. 2018;2:23.","journal-title":"BMC Rheumatol"},{"key":"2569_CR155","doi-asserted-by":"crossref","first-page":"9323","DOI":"10.1021\/jm501262q","volume":"57","author":"CJ Menet","year":"2014","unstructured":"Menet CJ, Fletcher SR, Van Lommen G, Geney R, Blanc J, Smits K, et al. Triazolopyridines as selective JAK1 inhibitors: from hit identification to GLPG0634. J Med Chem. 2014;57:9323\u201342.","journal-title":"J Med Chem"},{"key":"2569_CR156","doi-asserted-by":"crossref","first-page":"3442","DOI":"10.1021\/acschembio.6b00677","volume":"11","author":"JB Telliez","year":"2016","unstructured":"Telliez JB, Dowty ME, Wang L, Jussif J, Lin T, Li L, et al. Discovery of a JAK3-selective inhibitor: functional differentiation of JAK3-selective inhibition over pan-JAK or JAK1-selective inhibition. ACS Chem Biol. 2016;11:3442\u201351.","journal-title":"ACS Chem Biol"},{"key":"2569_CR157","doi-asserted-by":"crossref","first-page":"8973","DOI":"10.1021\/acs.jmedchem.9b00444","volume":"62","author":"ST Wrobleski","year":"2019","unstructured":"Wrobleski ST, Moslin R, Lin S, Zhang Y, Spergel S, Kempson J, et al. Highly selective inhibition of tyrosine kinase 2 (TYK2) for the treatment of autoimmune diseases: discovery of the allosteric inhibitor BMS-986165. J Med Chem. 2019;62:8973\u201395.","journal-title":"J Med Chem"},{"key":"2569_CR158","doi-asserted-by":"crossref","first-page":"1018","DOI":"10.1038\/leu.2016.12","volume":"30","author":"S Koschmieder","year":"2016","unstructured":"Koschmieder S, Mughal TI, Hasselbalch HC, Barosi G, Valent P, Kiladjian JJ, et al. Myeloproliferative neoplasms and inflammation: whether to target the malignant clone or the inflammatory process or both. Leukemia. 2016;30:1018\u201324.","journal-title":"Leukemia"},{"key":"2569_CR159","doi-asserted-by":"crossref","first-page":"E5401","DOI":"10.1073\/pnas.1407792111","volume":"111","author":"R Rampal","year":"2014","unstructured":"Rampal R, Ahn J, Abdel-Wahab O, Nahas M, Wang K, Lipson D, et al. Genomic and functional analysis of leukemic transformation of myeloproliferative neoplasms. Proc Natl Acad Sci USA. 2014;111:E5401\u20135410.","journal-title":"Proc Natl Acad Sci USA"},{"key":"2569_CR160","doi-asserted-by":"crossref","first-page":"807","DOI":"10.1007\/s00432-017-2354-1","volume":"143","author":"TM Schnoder","year":"2017","unstructured":"Schnoder TM, Eberhardt J, Koehler M, Bierhoff HB, Weinert S, Pandey AD, et al. Cell autonomous expression of CXCL-10 in JAK2V617F-mutated MPN. J Cancer Res Clin Oncol. 2017;143:807\u201320.","journal-title":"J Cancer Res Clin Oncol"},{"key":"2569_CR161","doi-asserted-by":"crossref","first-page":"1356","DOI":"10.1200\/JCO.2010.32.9490","volume":"29","author":"A Tefferi","year":"2011","unstructured":"Tefferi A, Vaidya R, Caramazza D, Finke C, Lasho T, Pardanani A. Circulating interleukin (IL)-8, IL-2R, IL-12, and IL-15 levels are independently prognostic in primary myelofibrosis: a comprehensive cytokine profiling study. J Clin Oncol. 2011;29:1356\u201363.","journal-title":"J Clin Oncol"},{"key":"2569_CR162","doi-asserted-by":"crossref","first-page":"1117","DOI":"10.1056\/NEJMoa1002028","volume":"363","author":"S Verstovsek","year":"2010","unstructured":"Verstovsek S, Kantarjian H, Mesa RA, Pardanani AD, Cortes-Franco J, Thomas DA, et al. Safety and efficacy of INCB018424, a JAK1 and JAK2 inhibitor, in myelofibrosis. N Engl J Med. 2010;363:1117\u201327.","journal-title":"N Engl J Med"},{"key":"2569_CR163","doi-asserted-by":"crossref","first-page":"9321","DOI":"10.1093\/nar\/gky787","volume":"46","author":"S Carrasco Pro","year":"2018","unstructured":"Carrasco Pro S, Dafonte Imedio A, Santoso CS, Gan KA, Sewell JA, Martinez M, et al. Global landscape of mouse and human cytokine transcriptional regulation. Nucleic Acids Res. 2018;46:9321\u201337.","journal-title":"Nucleic Acids Res"},{"key":"2569_CR164","doi-asserted-by":"crossref","first-page":"754","DOI":"10.1093\/nar\/gks1085","volume":"41","author":"AJ Bonham","year":"2013","unstructured":"Bonham AJ, Wenta N, Osslund LM, Prussin AJ 2nd, Vinkemeier U, Reich NO. STAT1:DNA sequence-dependent binding modulation by phosphorylation, protein:protein interactions and small-molecule inhibition. Nucleic Acids Res. 2013;41:754\u201363.","journal-title":"Nucleic Acids Res"},{"key":"2569_CR165","doi-asserted-by":"crossref","first-page":"1713","DOI":"10.1038\/s41375-018-0117-x","volume":"32","author":"B Wingelhofer","year":"2018","unstructured":"Wingelhofer B, Neubauer HA, Valent P, Han X, Constantinescu SN, Gunning PT, et al. Implications of STAT3 and STAT5 signaling on gene regulation and chromatin remodeling in hematopoietic cancer. Leukemia. 2018;32:1713\u201326.","journal-title":"Leukemia"},{"key":"2569_CR166","doi-asserted-by":"crossref","first-page":"586","DOI":"10.1016\/j.immuni.2012.02.017","volume":"36","author":"JX Lin","year":"2012","unstructured":"Lin JX, Li P, Liu D, Jin HT, He J, Ata Ur Rasheed M, et al. Critical Role of STAT5 transcription factor tetramerization for cytokine responses and normal immune function. Immunity. 2012;36:586\u201399.","journal-title":"Immunity"},{"key":"2569_CR167","doi-asserted-by":"crossref","first-page":"651","DOI":"10.1038\/nrm909","volume":"3","author":"DE Levy","year":"2002","unstructured":"Levy DE, Darnell JE Jr. Stats: transcriptional control and biological impact. Nat Rev Mol Cell Biol. 2002;3:651\u201362.","journal-title":"Nat Rev Mol Cell Biol"},{"key":"2569_CR168","doi-asserted-by":"crossref","first-page":"4339","DOI":"10.1158\/1078-0432.CCR-10-1092","volume":"16","author":"W Berkofsky-Fessler","year":"2010","unstructured":"Berkofsky-Fessler W, Buzzai M, Kim MK, Fruchtman S, Najfeld V, Min DJ, et al. Transcriptional profiling of polycythemia vera identifies gene expression patterns both dependent and independent from the action of JAK2V617F. Clin Cancer Res Off J Am Assoc Cancer Res. 2010;16:4339\u201352.","journal-title":"Clin Cancer Res Off J Am Assoc Cancer Res"},{"key":"2569_CR169","doi-asserted-by":"crossref","first-page":"14","DOI":"10.1016\/j.exphem.2021.12.364","volume":"107","author":"D Van Egeren","year":"2022","unstructured":"Van Egeren D, Kamaz B, Liu S, Nguyen M, Reilly CR, Kalyva M, et al. Transcriptional differences between JAK2-V617F and wild-type bone marrow cells in patients with myeloproliferative neoplasms. Exp Hematol. 2022;107:14\u201319.","journal-title":"Exp Hematol"},{"key":"2569_CR170","doi-asserted-by":"crossref","first-page":"6392","DOI":"10.1182\/blood-2011-04-348144","volume":"118","author":"AG Fleischman","year":"2011","unstructured":"Fleischman AG, Aichberger KJ, Luty SB, Bumm TG, Petersen CL, Doratotaj S, et al. TNFalpha facilitates clonal expansion of JAK2V617F positive cells in myeloproliferative neoplasms. Blood. 2011;118:6392\u20138.","journal-title":"Blood"},{"key":"2569_CR171","doi-asserted-by":"crossref","first-page":"100280","DOI":"10.1016\/j.eclinm.2020.100280","volume":"21","author":"KM Pedersen","year":"2020","unstructured":"Pedersen KM, Colak Y, Ellervik C, Hasselbalch HC, Bojesen SE, Nordestgaard BG. Loss-of-function polymorphism in IL6R reduces risk of JAK2V617F somatic mutation and myeloproliferative neoplasm: A Mendelian randomization study. EClinicalMedicine. 2020;21:100280.","journal-title":"EClinicalMedicine"},{"key":"2569_CR172","doi-asserted-by":"crossref","first-page":"709","DOI":"10.1111\/j.1365-2141.2005.05674.x","volume":"130","author":"KE Panteli","year":"2005","unstructured":"Panteli KE, Hatzimichael EC, Bouranta PK, Katsaraki A, Seferiadis K, Stebbing J, et al. Serum interleukin (IL)-1, IL-2, sIL-2Ra, IL-6 and thrombopoietin levels in patients with chronic myeloproliferative diseases. Br J Haematol. 2005;130:709\u201315.","journal-title":"Br J Haematol"},{"key":"2569_CR173","doi-asserted-by":"crossref","first-page":"1416","DOI":"10.1056\/NEJMoa1716614","volume":"379","author":"J Grinfeld","year":"2018","unstructured":"Grinfeld J, Nangalia J, Baxter EJ, Wedge DC, Angelopoulos N, Cantrill R, et al. Classification and Personalized Prognosis in Myeloproliferative Neoplasms. N Engl J Med. 2018;379:1416\u201330.","journal-title":"N Engl J Med"},{"key":"2569_CR174","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1182\/bloodadvances.2018026658","volume":"3","author":"H Ali","year":"2019","unstructured":"Ali H, Aldoss I, Yang D, Mokhtari S, Khaled S, Aribi A, et al. MIPSS70\u2009+\u2009v2.0 predicts long-term survival in myelofibrosis after allogeneic HCT with the Flu\/Mel conditioning regimen. Blood Adv. 2019;3:83\u201395.","journal-title":"Blood Adv"},{"key":"2569_CR175","doi-asserted-by":"crossref","first-page":"672","DOI":"10.1038\/nm.4097","volume":"22","author":"SC Lee","year":"2016","unstructured":"Lee SC, Dvinge H, Kim E, Cho H, Micol JB, Chung YR, et al. Modulation of splicing catalysis for therapeutic targeting of leukemia with mutations in genes encoding spliceosomal proteins. Nat Med. 2016;22:672\u20138.","journal-title":"Nat Med"},{"key":"2569_CR176","doi-asserted-by":"crossref","unstructured":"Flavahan WA, Gaskell E, Bernstein BE. Epigenetic plasticity and the hallmarks of cancer. Science. 2017;357:6348.","DOI":"10.1126\/science.aal2380"},{"key":"2569_CR177","unstructured":"Rodrigues CP, Shvedunova M, Akhtar A. Epigenetic regulators as the gatekeepers of hematopoiesis. Trends Genet. 2020;S0168-9525:30251\u20131."},{"key":"2569_CR178","doi-asserted-by":"crossref","first-page":"6987","DOI":"10.1182\/blood-2011-10-385278","volume":"118","author":"MA Dawson","year":"2011","unstructured":"Dawson MA, Bannister AJ, Saunders L, Wahab OA, Liu F, Nimer SD, et al. Nuclear JAK2. Blood. 2011;118:6987\u20138.","journal-title":"Blood"},{"key":"2569_CR179","doi-asserted-by":"crossref","first-page":"231","DOI":"10.1093\/jmcb\/mjp054","volume":"2","author":"J He","year":"2010","unstructured":"He J, Zhang Y. Janus kinase 2: an epigenetic 'writer' that activates leukemogenic genes. J Mol Cell Biol. 2010;2:231\u20133.","journal-title":"J Mol Cell Biol"},{"key":"2569_CR180","doi-asserted-by":"crossref","first-page":"819","DOI":"10.1038\/nature08448","volume":"461","author":"MA Dawson","year":"2009","unstructured":"Dawson MA, Bannister AJ, Gottgens B, Foster SD, Bartke T, Green AR, et al. JAK2 phosphorylates histone H3Y41 and excludes HP1alpha from chromatin. Nature. 2009;461:819\u201322.","journal-title":"Nature"},{"key":"2569_CR181","doi-asserted-by":"crossref","unstructured":"Strom AR, Biggs RJ, Banigan EJ, Wang X, Chiu K, Herman C, et al. HP1alpha is a chromatin crosslinker that controls nuclear and mitotic chromosome mechanics. Elife. 2021;10:e63972.","DOI":"10.7554\/eLife.63972"},{"key":"2569_CR182","doi-asserted-by":"crossref","first-page":"470","DOI":"10.1016\/j.celrep.2012.08.016","volume":"2","author":"MA Dawson","year":"2012","unstructured":"Dawson MA, Foster SD, Bannister AJ, Robson SC, Hannah R, Wang X, et al. Three distinct patterns of histone H3Y41 phosphorylation mark active genes. Cell Rep. 2012;2:470\u20137.","journal-title":"Cell Rep"},{"key":"2569_CR183","doi-asserted-by":"crossref","first-page":"2065","DOI":"10.1182\/blood-2017-10-810622","volume":"131","author":"JC Peeken","year":"2018","unstructured":"Peeken JC, Jutzi JS, Wehrle J, Koellerer C, Staehle HF, Becker H, et al. Epigenetic regulation of NFE2 overexpression in myeloproliferative neoplasms. Blood. 2018;131:2065\u201373.","journal-title":"Blood"},{"key":"2569_CR184","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1038\/ncb2135","volume":"13","author":"DS Griffiths","year":"2011","unstructured":"Griffiths DS, Li J, Dawson MA, Trotter MW, Cheng YH, Smith AM, et al. LIF-independent JAK signalling to chromatin in embryonic stem cells uncovered from an adult stem cell disease. Nat Cell Biol. 2011;13:13\u201321.","journal-title":"Nat Cell Biol"},{"key":"2569_CR185","doi-asserted-by":"crossref","first-page":"11766","DOI":"10.1073\/pnas.1805662115","volume":"115","author":"H Kim","year":"2018","unstructured":"Kim H, Kim D, Choi SA, Kim CR, Oh SK, Pyo KE, et al. KDM3A histone demethylase functions as an essential factor for activation of JAK2-STAT3 signaling pathway. Proc Natl Acad Sci USA. 2018;115:11766\u201371.","journal-title":"Proc Natl Acad Sci USA"},{"key":"2569_CR186","doi-asserted-by":"crossref","first-page":"919","DOI":"10.1038\/s41375-023-01826-y","volume":"37","author":"AM Staehle","year":"2023","unstructured":"Staehle AM, Peeken JC, Vladimirov G, Hoeness ME, Bojtine Kovacs S, Karantzelis N, et al. The histone demethylase JMJD2C constitutes a novel NFE2 target gene that is required for the survival of JAK2(V617F) mutated cells. Leukemia. 2023;37:919\u201323.","journal-title":"Leukemia"},{"key":"2569_CR187","doi-asserted-by":"crossref","first-page":"1843","DOI":"10.1038\/s41375-022-01611-3","volume":"36","author":"P Ernst","year":"2022","unstructured":"Ernst P, Schnoder TM, Huber N, Perner F, Jayavelu AK, Eifert T, et al. Histone demethylase KDM4C is a functional dependency in JAK2-mutated neoplasms. Leukemia. 2022;36:1843\u20139.","journal-title":"Leukemia"},{"key":"2569_CR188","doi-asserted-by":"crossref","first-page":"25343","DOI":"10.1074\/jbc.274.36.25343","volume":"274","author":"M Paulson","year":"1999","unstructured":"Paulson M, Pisharody S, Pan L, Guadagno S, Mui AL, Levy DE. Stat protein transactivation domains recruit p300\/CBP through widely divergent sequences. J Biol Chem. 1999;274:25343\u20139.","journal-title":"J Biol Chem"},{"key":"2569_CR189","doi-asserted-by":"crossref","first-page":"344","DOI":"10.1038\/383344a0","volume":"383","author":"S Bhattacharya","year":"1996","unstructured":"Bhattacharya S, Eckner R, Grossman S, Oldread E, Arany Z, D'Andrea A, et al. Cooperation of Stat2 and p300\/CBP in signalling induced by interferon-alpha. Nature. 1996;383:344\u20137.","journal-title":"Nature"},{"key":"2569_CR190","doi-asserted-by":"crossref","first-page":"948","DOI":"10.1038\/emboj.2009.30","volume":"28","author":"JM Wojciak","year":"2009","unstructured":"Wojciak JM, Martinez-Yamout MA, Dyson HJ, Wright PE. Structural basis for recruitment of CBP\/p300 coactivators by STAT1 and STAT2 transactivation domains. EMBO J. 2009;28:948\u201358.","journal-title":"EMBO J"},{"key":"2569_CR191","doi-asserted-by":"crossref","first-page":"3817","DOI":"10.1128\/MCB.01562-12","volume":"33","author":"L Gnatovskiy","year":"2013","unstructured":"Gnatovskiy L, Mita P, Levy DE. The human RVB complex is required for efficient transcription of type I interferon-stimulated genes. Mol Cell Biol. 2013;33:3817\u201325.","journal-title":"Mol Cell Biol"},{"key":"2569_CR192","doi-asserted-by":"crossref","first-page":"217","DOI":"10.1126\/science.1108164","volume":"3077","author":"JJ O'Shea","year":"2005","unstructured":"O'Shea JJ, Kanno Y, Chen X, Levy DE. Cell signaling. Stat acetylation-a key facet of cytokine signaling? Science. 2005;3077:217\u20138.","journal-title":"Science"},{"key":"2569_CR193","doi-asserted-by":"crossref","first-page":"269","DOI":"10.1126\/science.1105166","volume":"307","author":"ZL Yuan","year":"2005","unstructured":"Yuan ZL, Guan YJ, Chatterjee D, Chin YE. Stat3 dimerization regulated by reversible acetylation of a single lysine residue. Science (N. Y, NY). 2005;307:269\u201373.","journal-title":"Science (N. Y, NY)"},{"key":"2569_CR194","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1016\/j.cell.2007.07.034","volume":"131","author":"X Tang","year":"2007","unstructured":"Tang X, Gao JS, Guan YJ, McLane KE, Yuan ZL, Ramratnam B, et al. Acetylation-dependent signal transduction for type I interferon receptor. Cell. 2007;131:93\u2013105.","journal-title":"Cell"},{"key":"2569_CR195","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1016\/j.ccell.2017.11.009","volume":"33","author":"M Kleppe","year":"2018","unstructured":"Kleppe M, Koche R, Zou L, van Galen P, Hill CE, Dong L, et al. Dual targeting of oncogenic activation and inflammatory signaling increases therapeutic efficacy in myeloproliferative neoplasms. Cancer Cell. 2018;33:29\u201343.e27.","journal-title":"Cancer Cell"},{"key":"2569_CR196","doi-asserted-by":"crossref","first-page":"88","DOI":"10.1038\/leu.2013.234","volume":"28","author":"BS Wyspianska","year":"2014","unstructured":"Wyspianska BS, Bannister AJ, Barbieri I, Nangalia J, Godfrey A, Calero-Nieto FJ, et al. BET protein inhibition shows efficacy against JAK2V617F-driven neoplasms. Leukemia. 2014;28:88\u201397.","journal-title":"Leukemia"},{"key":"2569_CR197","doi-asserted-by":"crossref","first-page":"3194","DOI":"10.1084\/jem.20180520","volume":"215","author":"IJ Marie","year":"2018","unstructured":"Marie IJ, Chang HM, Levy DE. HDAC stimulates gene expression through BRD4 availability in response to IFN and in interferonopathies. J Exp Med. 2018;215:3194\u2013212.","journal-title":"J Exp Med"},{"key":"2569_CR198","doi-asserted-by":"crossref","first-page":"4993","DOI":"10.1200\/JCO.22.01972","volume":"41","author":"J Mascarenhas","year":"2023","unstructured":"Mascarenhas J, Kremyanskaya M, Patriarca A, Palandri F, Devos T, Passamonti F, et al. MANIFEST: pelabresib in combination with ruxolitinib for Janus kinase inhibitor treatment-naive myelofibrosis. J Clin Oncol Off J Am Soc Clin Oncol. 2023;41:4993\u20135004.","journal-title":"J Clin Oncol Off J Am Soc Clin Oncol"},{"key":"2569_CR199","doi-asserted-by":"crossref","first-page":"6502","DOI":"10.1200\/JCO.2024.42.16_suppl.6502","volume":"42","author":"R Rampal","year":"2024","unstructured":"Rampal R, Grosicki S, Chraniuk D, Abruzzese E, Bose P, Gerds AT, et al. Updated safety and efficacy data from the phase 3 MANIFEST-2 study of pelabresib in combination with ruxolitinib for JAK inhibitor treatment-na\u00efve patients with myelofibrosis. J Clin Oncol. 2024;42:6502.","journal-title":"J Clin Oncol"},{"key":"2569_CR200","volume":"14","author":"MHE Wildschut","year":"2023","unstructured":"Wildschut MHE, Mena J, Dordelmann C, van Oostrum M, Hale BD, Settelmeier J, et al. Proteogenetic drug response profiling elucidates targetable vulnerabilities of myelofibrosis. Nat Commun. 2023;14:6414.","journal-title":"Nat Commun"},{"key":"2569_CR201","doi-asserted-by":"crossref","first-page":"879","DOI":"10.1080\/13543784.2023.2267980","volume":"32","author":"HY Rienhoff Jr","year":"2023","unstructured":"Rienhoff HY Jr, Gill H. Bomedemstat as an investigative treatment for myeloproliferative neoplasms. Expert Opin Investig drugs. 2023;32:879\u201386.","journal-title":"Expert Opin Investig drugs"},{"key":"2569_CR202","doi-asserted-by":"crossref","first-page":"e54","DOI":"10.1097\/HS9.0000000000000054","volume":"2","author":"JS Jutzi","year":"2018","unstructured":"Jutzi JS, Kleppe M, Dias J, Staehle HF, Shank K, Teruya-Feldstein J, et al. LSD1 inhibition prolongs survival in mouse models of MPN by selectively targeting the disease clone. Hemasphere. 2018;2:e54.","journal-title":"Hemasphere"},{"key":"2569_CR203","doi-asserted-by":"crossref","first-page":"747","DOI":"10.1182\/blood-2023-179329","volume":"142","author":"JR Goethert","year":"2023","unstructured":"Goethert JR, Gill H, Palandri F, Ross DM, Cochrane T, Larsen SR, et al. Bomedemstat (IMG-7289), an LSD1 inhibitor, manages the signs and symptoms of essential thrombocythemia (ET) while reducing the burden of cells homozygous for driver mutations. Blood. 2023;142:747.","journal-title":"Blood"},{"key":"2569_CR204","doi-asserted-by":"crossref","first-page":"9717","DOI":"10.1182\/blood-2022-167122","volume":"140","author":"KM Pettit","year":"2022","unstructured":"Pettit KM, Gill H, Yacoub A, Bradley T, Gerds AT, Tatarczuch M, et al. A phase 2 study of the LSD1 inhibitor bomedemstat (IMG-7289) for the treatment of advanced myelofibrosis (MF): updated results and genomic analyses. Blood. 2022;140:9717\u201320.","journal-title":"Blood"},{"key":"2569_CR205","doi-asserted-by":"crossref","first-page":"1784","DOI":"10.1182\/blood-2022-159047","volume":"140","author":"H Gill","year":"2022","unstructured":"Gill H, Palandri F, Ross DM, Cochrane T, Tate C, Lane SW, et al. A phase 2 study of the LSD1 inhibitor bomedemstat (IMG-7289) for the treatment of essential thrombocythemia (ET). Blood. 2022;140:1784\u20137.","journal-title":"Blood"},{"key":"2569_CR206","doi-asserted-by":"crossref","first-page":"556","DOI":"10.1182\/blood-2019-123244","volume":"134","author":"K Pettit","year":"2019","unstructured":"Pettit K, Gerds AT, Yacoub A, Watts JM, Tartaczuch M, Bradley TJ, et al. A phase 2a study of the LSD1 inhibitor img-7289 (bomedemstat) for the treatment of myelofibrosis. Blood. 2019;134:556.","journal-title":"Blood"},{"key":"2569_CR207","doi-asserted-by":"crossref","first-page":"778","DOI":"10.1158\/2159-8290.CD-18-1138","volume":"9","author":"JJ Jeong","year":"2019","unstructured":"Jeong JJ, Gu X, Nie J, Sundaravel S, Liu H, Kuo WL, et al. Cytokine-regulated phosphorylation and activation of TET2 by JAK2 in hematopoiesis. Cancer Discov. 2019;9:778\u201395.","journal-title":"Cancer Discov"},{"key":"2569_CR208","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1016\/j.tem.2017.11.001","volume":"29","author":"DW Dodington","year":"2018","unstructured":"Dodington DW, Desai HR, Woo M. JAK\/STAT - emerging players in metabolism. Trends Endocrinol Metab. 2018;29:55\u201365.","journal-title":"Trends Endocrinol Metab"},{"key":"2569_CR209","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1016\/j.cmet.2017.05.018","volume":"26","author":"S Theurich","year":"2017","unstructured":"Theurich S, Tsaousidou E, Hanssen R, Lempradl AM, Mauer J, Timper K, et al. IL-6\/Stat3-dependent induction of a distinct, obesity-associated NK cell subpopulation deteriorates energy and glucose homeostasis. Cell Metab. 2017;26:171\u201384 e176.","journal-title":"Cell Metab"},{"key":"2569_CR210","doi-asserted-by":"crossref","first-page":"860","DOI":"10.1038\/nature05485","volume":"444","author":"GS Hotamisligil","year":"2006","unstructured":"Hotamisligil GS. Inflammation and metabolic disorders. Nature. 2006;444:860\u20137.","journal-title":"Nature"},{"key":"2569_CR211","doi-asserted-by":"crossref","DOI":"10.1186\/1471-2350-12-166","volume":"12","author":"A Penas-Steinhardt","year":"2011","unstructured":"Penas-Steinhardt A, Tellechea ML, Gomez-Rosso L, Brites F, Frechtel GD, Poskus E. Association of common variants in JAK2 gene with reduced risk of metabolic syndrome and related disorders. BMC Med Genet. 2011;12:166.","journal-title":"BMC Med Genet"},{"key":"2569_CR212","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1007\/s00125-015-3786-2","volume":"59","author":"SY Shi","year":"2016","unstructured":"Shi SY, Zhang W, Luk CT, Sivasubramaniyam T, Brunt JJ, Schroer SA, et al. JAK2 promotes brown adipose tissue function and is required for diet- and cold-induced thermogenesis in mice. Diabetologia. 2016;59:187\u201396.","journal-title":"Diabetologia"},{"key":"2569_CR213","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1038\/ncb3075","volume":"17","author":"A Moisan","year":"2015","unstructured":"Moisan A, Lee YK, Zhang JD, Hudak CS, Meyer CA, Prummer M, et al. White-to-brown metabolic conversion of human adipocytes by JAK inhibition. Nat Cell Biol. 2015;17:57\u201367.","journal-title":"Nat Cell Biol"},{"key":"2569_CR214","doi-asserted-by":"crossref","first-page":"2831","DOI":"10.1084\/jem.20100665","volume":"207","author":"D Choi","year":"2010","unstructured":"Choi D, Schroer SA, Lu SY, Wang L, Wu X, Liu Y, et al. Erythropoietin protects against diabetes through direct effects on pancreatic beta cells. J Exp Med. 2010;207:2831\u201342.","journal-title":"J Exp Med"},{"key":"2569_CR215","doi-asserted-by":"crossref","first-page":"10277","DOI":"10.1074\/jbc.M111.317453","volume":"287","author":"SY Shi","year":"2012","unstructured":"Shi SY, Martin RG, Duncan RE, Choi D, Lu SY, Schroer SA, et al. Hepatocyte-specific deletion of Janus kinase 2 (JAK2) protects against diet-induced steatohepatitis and glucose intolerance. J Biol Chem. 2012;287:10277\u201388.","journal-title":"J Biol Chem"},{"key":"2569_CR216","volume":"7","author":"HR Desai","year":"2017","unstructured":"Desai HR, Sivasubramaniyam T, Revelo XS, Schroer SA, Luk CT, Rikkala PR, et al. Macrophage JAK2 deficiency protects against high-fat diet-induced inflammation. Sci Rep. 2017;7:7653.","journal-title":"Sci Rep."},{"key":"2569_CR217","doi-asserted-by":"crossref","first-page":"1292","DOI":"10.1016\/j.cell.2014.03.066","volume":"157","author":"Y Qiu","year":"2014","unstructured":"Qiu Y, Nguyen KD, Odegaard JI, Cui X, Tian X, Locksley RM, et al. Eosinophils and type 2 cytokine signaling in macrophages orchestrate development of functional beige fat. Cell. 2014;157:1292\u2013308.","journal-title":"Cell"},{"key":"2569_CR218","first-page":"1832","volume":"134","author":"TN Rao","year":"2019","unstructured":"Rao TN, Hansen N, Hilfiker J, Rai S, Majewska JM, Lekovic D, et al. JAK2-mutant hematopoietic cells display metabolic alterations that can be targeted to treat myeloproliferative neoplasms. Blood. 2019;134:1832\u201346.","journal-title":"Blood"},{"key":"2569_CR219","volume":"13","author":"R Al-Rifai","year":"2022","unstructured":"Al-Rifai R, Vandestienne M, Lavillegrand JR, Mirault T, Cornebise J, Poisson J, et al. JAK2V617F mutation drives vascular resident macrophages toward a pathogenic phenotype and promotes dissecting aortic aneurysm. Nat Commun. 2022;13:6592.","journal-title":"Nat Commun"},{"key":"2569_CR220","first-page":"3","volume":"134","author":"F He","year":"2024","unstructured":"He F, Laranjeira AB, Kong T, Lin S, Ashworth KJ, Liu A, et al. Multiomic profiling reveals metabolic alterations mediating aberrant platelet activity and inflammation in myeloproliferative neoplasms. J Clin Investig. 2024;134:3.","journal-title":"J Clin Investig"},{"key":"2569_CR221","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1038\/s41556-018-0234-9","volume":"21","author":"Z Sun","year":"2019","unstructured":"Sun Z, Costell M, Fassler R. Integrin activation by talin, kindlin and mechanical forces. Nat Cell Biol. 2019;21:25\u201331.","journal-title":"Nat Cell Biol"},{"key":"2569_CR222","doi-asserted-by":"crossref","first-page":"1003","DOI":"10.1083\/jcb.201303067","volume":"203","author":"A Montresor","year":"2013","unstructured":"Montresor A, Bolomini-Vittori M, Toffali L, Rossi B, Constantin G, Laudanna C. JAK tyrosine kinases promote hierarchical activation of Rho and Rap modules of integrin activation. J Cell Biol. 2013;203:1003\u201319.","journal-title":"J Cell Biol"},{"key":"2569_CR223","doi-asserted-by":"crossref","first-page":"2969","DOI":"10.1182\/bloodadvances.2020003032","volume":"5","author":"N Eaton","year":"2021","unstructured":"Eaton N, Subramaniam S, Schulte ML, Drew C, Jakab D, Haberichter SL, et al. Bleeding diathesis in mice lacking JAK2 in platelets. Blood Adv. 2021;5:2969\u201381.","journal-title":"Blood Adv"},{"key":"2569_CR224","doi-asserted-by":"crossref","first-page":"1739","DOI":"10.1182\/bloodadvances.2022008498","volume":"7","author":"D Szpak","year":"2023","unstructured":"Szpak D, Turpin C, Goreke U, Bialkowska K, Bledzka KM, Verbovetskiy D, et al. Kindlin-3 deficiency leads to impaired erythropoiesis and erythrocyte cytoskeleton. Blood Adv. 2023;7:1739\u201353.","journal-title":"Blood Adv"},{"key":"2569_CR225","doi-asserted-by":"crossref","first-page":"24326","DOI":"10.1073\/pnas.2009078117","volume":"117","author":"PW Krenn","year":"2020","unstructured":"Krenn PW, Koschmieder S, Fassler R. Kindlin-3 loss curbs chronic myeloid leukemia in mice by mobilizing leukemic stem cells from protective bone marrow niches. Proc Natl Acad Sci USA. 2020;117:24326\u201335.","journal-title":"Proc Natl Acad Sci USA"},{"key":"2569_CR226","doi-asserted-by":"crossref","first-page":"1223","DOI":"10.1038\/leu.2017.26","volume":"31","author":"N Gupta","year":"2017","unstructured":"Gupta N, Edelmann B, Schnoeder TM, Saalfeld FC, Wolleschak D, Kliche S, et al. JAK2-V617F activates beta1-integrin-mediated adhesion of granulocytes to vascular cell adhesion molecule 1. Leukemia. 2017;31:1223\u20136.","journal-title":"Leukemia"},{"key":"2569_CR227","doi-asserted-by":"crossref","first-page":"4359","DOI":"10.1172\/JCI90312","volume":"128","author":"B Edelmann","year":"2018","unstructured":"Edelmann B, Gupta N, Schnoeder TM, Oelschlegel AM, Shahzad K, Goldschmidt J, et al. JAK2-V617F promotes venous thrombosis through beta1\/beta2 integrin activation. J Clin Investig. 2018;128:4359\u201371.","journal-title":"J Clin Investig"},{"key":"2569_CR228","doi-asserted-by":"crossref","first-page":"1047","DOI":"10.1016\/j.celrep.2013.10.038","volume":"5","author":"M Waibel","year":"2013","unstructured":"Waibel M, Solomon VS, Knight DA, Ralli RA, Kim SK, Banks KM, et al. Combined targeting of JAK2 and Bcl-2\/Bcl-xL to cure mutant JAK2-driven malignancies and overcome acquired resistance to JAK2 inhibitors. Cell Rep. 2013;5:1047\u201359.","journal-title":"Cell Rep"},{"key":"2569_CR229","doi-asserted-by":"crossref","first-page":"12350","DOI":"10.1074\/jbc.272.19.12350","volume":"272","author":"I Sakai","year":"1997","unstructured":"Sakai I, Kraft AS. The kinase domain of Jak2 mediates induction of bcl-2 and delays cell death in hematopoietic cells. J Biol Chem. 1997;272:12350\u20138.","journal-title":"J Biol Chem"},{"key":"2569_CR230","doi-asserted-by":"crossref","first-page":"e0114363","DOI":"10.1371\/journal.pone.0114363","volume":"10","author":"J Guo","year":"2015","unstructured":"Guo J, Roberts L, Chen Z, Merta PJ, Glaser KB, Shah OJ. JAK2V617F drives Mcl-1 expression and sensitizes hematologic cell lines to dual inhibition of JAK2 and Bcl-xL. PLoS One. 2015;10:e0114363.","journal-title":"PLoS One"},{"key":"2569_CR231","doi-asserted-by":"crossref","first-page":"732","DOI":"10.1038\/s41580-023-00629-4","volume":"24","author":"PE Czabotar","year":"2023","unstructured":"Czabotar PE, Garcia-Saez AJ. Mechanisms of BCL-2 family proteins in mitochondrial apoptosis. Nat Rev Mol Cell Biol. 2023;24:732\u201348.","journal-title":"Nat Rev Mol Cell Biol"},{"key":"2569_CR232","doi-asserted-by":"crossref","first-page":"678","DOI":"10.1128\/MCB.21.2.678-689.2001","volume":"21","author":"R Wen","year":"2001","unstructured":"Wen R, Wang D, McKay C, Bunting KD, Marine JC, Vanin EF, et al. Jak3 selectively regulates Bax and Bcl-2 expression to promote T-cell development. Mol Cell Biol. 2001;21:678\u201389.","journal-title":"Mol Cell Biol"},{"key":"2569_CR233","doi-asserted-by":"crossref","first-page":"ra122","DOI":"10.1126\/scisignal.2005301","volume":"7","author":"PS Winter","year":"2014","unstructured":"Winter PS, Sarosiek KA, Lin KH, Meggendorfer M, Schnittger S, Letai A, et al. RAS signaling promotes resistance to JAK inhibitors by suppressing BAD-mediated apoptosis. Sci Signal. 2014;7:ra122.","journal-title":"Sci Signal"},{"key":"2569_CR234","doi-asserted-by":"crossref","unstructured":"Igelmann S, Neubauer HA, Ferbeyre G. STAT3 and STAT5 activation in solid cancers. Cancers. 2019;11:1428.","DOI":"10.3390\/cancers11101428"},{"key":"2569_CR235","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1016\/S1074-7613(00)80011-4","volume":"10","author":"R Catlett-Falcone","year":"1999","unstructured":"Catlett-Falcone R, Landowski TH, Oshiro MM, Turkson J, Levitzki A, Savino R, et al. Constitutive activation of Stat3 signaling confers resistance to apoptosis in human U266 myeloma cells. Immunity. 1999;10:105\u201315.","journal-title":"Immunity"},{"key":"2569_CR236","doi-asserted-by":"crossref","first-page":"18490","DOI":"10.1073\/pnas.0809242105","volume":"105","author":"RR Weichselbaum","year":"2008","unstructured":"Weichselbaum RR, Ishwaran H, Yoon T, Nuyten DS, Baker SW, Khodarev N, et al. An interferon-related gene signature for DNA damage resistance is a predictive marker for chemotherapy and radiation for breast cancer. Proc Natl Acad Sci USA. 2008;105:18490\u20135.","journal-title":"Proc Natl Acad Sci USA"},{"key":"2569_CR237","doi-asserted-by":"crossref","first-page":"2901","DOI":"10.1182\/blood-2009-03-209544","volume":"115","author":"B Will","year":"2010","unstructured":"Will B, Siddiqi T, Jorda MA, Shimamura T, Luptakova K, Staber PB, et al. Apoptosis induced by JAK2 inhibition is mediated by Bim and enhanced by the BH3 mimetic ABT-737 in JAK2 mutant human erythroid cells. Blood. 2010;115:2901\u20139.","journal-title":"Blood"},{"key":"2569_CR238","doi-asserted-by":"crossref","first-page":"2235","DOI":"10.1038\/onc.2015.285","volume":"35","author":"JS Ahn","year":"2016","unstructured":"Ahn JS, Li J, Chen E, Kent DG, Park HJ, Green AR. JAK2V617F mediates resistance to DNA damage-induced apoptosis by modulating FOXO3A localization and Bcl-xL deamidation. Oncogene. 2016;35:2235\u201346.","journal-title":"Oncogene"},{"key":"2569_CR239","doi-asserted-by":"crossref","first-page":"48","DOI":"10.1016\/j.exphem.2023.08.005","volume":"128","author":"DAC Fisher","year":"2023","unstructured":"Fisher DAC, Laranjeira ABA, Kong T, Snyder SC, Shim K, Fulbright MC, et al. Complementary and countervailing actions of Jak2 and Ikk2 in hematopoiesis in mice. Exp Hematol. 2023;128:48\u201366.","journal-title":"Exp Hematol"},{"key":"2569_CR240","doi-asserted-by":"crossref","first-page":"785","DOI":"10.1016\/j.stem.2017.03.008","volume":"20","author":"RK Schneider","year":"2017","unstructured":"Schneider RK, Mullally A, Dugourd A, Peisker F, Hoogenboezem R, Van Strien PMH, et al. Gli1(+) mesenchymal stromal cells are a key driver of bone marrow fibrosis and an important cellular therapeutic target. Cell Stem cell. 2017;20:785\u2013800.e788.","journal-title":"Cell Stem cell"},{"key":"2569_CR241","doi-asserted-by":"crossref","first-page":"3495","DOI":"10.1182\/blood-2002-04-1133","volume":"100","author":"H Chagraoui","year":"2002","unstructured":"Chagraoui H, Komura E, Tulliez M, Giraudier S, Vainchenker W, Wendling F. Prominent role of TGF-beta 1 in thrombopoietin-induced myelofibrosis in mice. Blood. 2002;100:3495\u2013503.","journal-title":"Blood"},{"key":"2569_CR242","doi-asserted-by":"crossref","first-page":"3493","DOI":"10.1182\/blood-2004-04-1320","volume":"105","author":"AM Vannucchi","year":"2005","unstructured":"Vannucchi AM, Bianchi L, Paoletti F, Pancrazzi A, Torre E, Nishikawa M, et al. A pathobiologic pathway linking thrombopoietin, GATA-1, and TGF-beta1 in the development of myelofibrosis. Blood. 2005;105:3493\u2013501.","journal-title":"Blood"},{"key":"2569_CR243","doi-asserted-by":"crossref","first-page":"3345","DOI":"10.1182\/blood-2012-06-439661","volume":"121","author":"M Zingariello","year":"2013","unstructured":"Zingariello M, Martelli F, Ciaffoni F, Masiello F, Ghinassi B, D'Amore E, et al. Characterization of the TGF-beta1 signaling abnormalities in the Gata1low mouse model of myelofibrosis. Blood. 2013;121:3345\u201363.","journal-title":"Blood"},{"key":"2569_CR244","doi-asserted-by":"crossref","unstructured":"Yao JC, Oetjen KA, Wang T, Xu H, Abou-Ezzi G, Krambs JR, et al. TGF-beta signaling in myeloproliferative neoplasms contributes to myelofibrosis without disrupting the hematopoietic niche. J Clin Investig. 2022;132:e154092.","DOI":"10.1172\/JCI154092"},{"key":"2569_CR245","doi-asserted-by":"crossref","first-page":"5901","DOI":"10.1158\/1078-0432.CCR-18-4089","volume":"25","author":"B Woods","year":"2019","unstructured":"Woods B, Chen W, Chiu S, Marinaccio C, Fu C, Gu L, et al. Activation of JAK\/STAT signaling in megakaryocytes sustains myeloproliferation In Vivo. Clin Cancer Res Off J Am Assoc Cancer Res. 2019;25:5901\u201312.","journal-title":"Clin Cancer Res Off J Am Assoc Cancer Res"},{"key":"2569_CR246","doi-asserted-by":"crossref","first-page":"920","DOI":"10.1182\/blood-2016-12-757344","volume":"130","author":"A Dutta","year":"2017","unstructured":"Dutta A, Hutchison RE, Mohi G. Hmga2 promotes the development of myelofibrosis in Jak2(V617F) knockin mice by enhancing TGF-beta1 and Cxcl12 pathways. Blood. 2017;130:920\u201332.","journal-title":"Blood"},{"key":"2569_CR247","doi-asserted-by":"crossref","first-page":"2332","DOI":"10.1038\/leu.2016.114","volume":"30","author":"H Zhan","year":"2016","unstructured":"Zhan H, Ma Y, Lin CH, Kaushansky K. JAK2(V617F)-mutant megakaryocytes contribute to hematopoietic stem\/progenitor cell expansion in a model of murine myeloproliferation. Leukemia. 2016;30:2332\u201341.","journal-title":"Leukemia"},{"key":"2569_CR248","doi-asserted-by":"crossref","first-page":"2805","DOI":"10.1182\/blood.2022017326","volume":"140","author":"J Melo-Cardenas","year":"2022","unstructured":"Melo-Cardenas J, Bezavada L, Crawford JC, Gurbuxani S, Cotton A, Kang G, et al. IL-13\/IL-4 signaling contributes to fibrotic progression of the myeloproliferative neoplasms. Blood. 2022;140:2805\u201317.","journal-title":"Blood"},{"key":"2569_CR249","doi-asserted-by":"crossref","first-page":"180","DOI":"10.1016\/j.humpath.2017.01.007","volume":"62","author":"S Nakayama","year":"2017","unstructured":"Nakayama S, Yokote T, Hiraoka N, Akioka T, Nishiwaki U, Miyoshi T, et al. Transforming growth factor beta- and interleukin 13-producing mast cells are associated with fibrosis in bone marrow. Hum Pathol. 2017;62:180\u20136.","journal-title":"Hum Pathol"},{"key":"2569_CR250","doi-asserted-by":"crossref","first-page":"2985","DOI":"10.1158\/0008-5472.CAN-23-3553","volume":"84","author":"D Schmidt","year":"2024","unstructured":"Schmidt D, Endres C, Hoefflin R, Andrieux G, Zwick M, Karantzelis N, et al. Oncogenic calreticulin induces immune escape by stimulating TGF-beta expression and regulatory T cell expansion in the bone marrow microenvironment. Cancer Res. 2024;84:2985\u20133003.","journal-title":"Cancer Res"},{"key":"2569_CR251","doi-asserted-by":"crossref","first-page":"2051","DOI":"10.1182\/blood.2019004095","volume":"136","author":"HFE Gleitz","year":"2020","unstructured":"Gleitz HFE, Dugourd AJF, Leimkuhler NB, Snoeren IAM, Fuchs SNR, Menzel S, et al. Increased CXCL4 expression in hematopoietic cells links inflammation and progression of bone marrow fibrosis in MPN. Blood. 2020;136:2051\u201364.","journal-title":"Blood"},{"key":"2569_CR252","doi-asserted-by":"crossref","first-page":"1971","DOI":"10.1038\/s41375-024-02354-z","volume":"38","author":"D Capitanio","year":"2024","unstructured":"Capitanio D, Calledda FR, Abbonante V, Cattaneo D, Moriggi M, Niccolo B, et al. Proteomic screening identifies PF4\/Cxcl4 as a critical driver of myelofibrosis. Leukemia. 2024;38:1971\u201384.","journal-title":"Leukemia"},{"key":"2569_CR253","doi-asserted-by":"crossref","first-page":"112131","DOI":"10.1016\/j.celrep.2023.112131","volume":"42","author":"K Hoeft","year":"2023","unstructured":"Hoeft K, Schaefer GJL, Kim H, Schumacher D, Bleckwehl T, Long Q, et al. Platelet-instructed SPP1(+) macrophages drive myofibroblast activation in fibrosis in a CXCL4-dependent manner. Cell Rep. 2023;42:112131.","journal-title":"Cell Rep"},{"key":"2569_CR254","volume":"13","author":"S Rai","year":"2022","unstructured":"Rai S, Grockowiak E, Hansen N, Luque Paz D, Stoll CB, Hao-Shen H, et al. Inhibition of interleukin-1beta reduces myelofibrosis and osteosclerosis in mice with JAK2-V617F driven myeloproliferative neoplasm. Nat Commun. 2022;13:5346.","journal-title":"Nat Commun"},{"key":"2569_CR255","doi-asserted-by":"crossref","DOI":"10.1038\/s41467-022-32928-3","volume":"13","author":"MF Rahman","year":"2022","unstructured":"Rahman MF, Yang Y, Le BT, Dutta A, Posyniak J, Faughnan P, et al. Interleukin-1 contributes to clonal expansion and progression of bone marrow fibrosis in JAK2V617F-induced myeloproliferative neoplasm. Nat Commun. 2022;13:5347.","journal-title":"Nat Commun"},{"key":"2569_CR256","doi-asserted-by":"crossref","first-page":"1287","DOI":"10.1038\/s41375-023-01878-0","volume":"37","author":"C Willekens","year":"2023","unstructured":"Willekens C, Laplane L, Dagher T, Benlabiod C, Papadopoulos N, Lacout C, et al. SRSF2-P95H decreases JAK\/STAT signaling in hematopoietic cells and delays myelofibrosis development in mice. Leukemia. 2023;37:1287\u201397.","journal-title":"Leukemia"},{"key":"2569_CR257","doi-asserted-by":"crossref","first-page":"3831","DOI":"10.1158\/0008-5472.CAN-10-4002","volume":"71","author":"T Manshouri","year":"2011","unstructured":"Manshouri T, Estrov Z, Quintas-Cardama A, Burger J, Zhang Y, Livun A, et al. Bone marrow stroma-secreted cytokines protect JAK2(V617F)-mutated cells from the effects of a JAK2 inhibitor. Cancer Res. 2011;71:3831\u201340.","journal-title":"Cancer Res"},{"key":"2569_CR258","doi-asserted-by":"crossref","first-page":"316","DOI":"10.1158\/2159-8290.CD-14-0736","volume":"5","author":"M Kleppe","year":"2015","unstructured":"Kleppe M, Kwak M, Koppikar P, Riester M, Keller M, Bastian L, et al. JAK-STAT pathway activation in malignant and nonmalignant cells contributes to MPN pathogenesis and therapeutic response. Cancer Discov. 2015;5:316\u201331.","journal-title":"Cancer Discov"},{"key":"2569_CR259","doi-asserted-by":"crossref","first-page":"637","DOI":"10.1016\/j.stem.2020.11.004","volume":"28","author":"NB Leimkuhler","year":"2021","unstructured":"Leimkuhler NB, Gleitz HFE, Ronghui L, Snoeren IAM, Fuchs SNR, Nagai JS, et al. Heterogeneous bone-marrow stromal progenitors drive myelofibrosis via a druggable alarmin axis. Cell Stem Cell. 2021;28:637\u201352.e638.","journal-title":"Cell Stem Cell"},{"key":"2569_CR260","doi-asserted-by":"crossref","first-page":"3219","DOI":"10.1182\/blood-2011-11-394775","volume":"119","author":"HC Hasselbalch","year":"2012","unstructured":"Hasselbalch HC. Perspectives on chronic inflammation in essential thrombocythemia, polycythemia vera, and myelofibrosis: is chronic inflammation a trigger and driver of clonal evolution and development of accelerated atherosclerosis and second cancer? Blood. 2012;119:3219\u201325.","journal-title":"Blood"},{"key":"2569_CR261","doi-asserted-by":"crossref","first-page":"683401","DOI":"10.3389\/fimmu.2021.683401","volume":"12","author":"DAC Fisher","year":"2021","unstructured":"Fisher DAC, Fowles JS, Zhou A, Oh ST. Inflammatory pathophysiology as a contributor to myeloproliferative neoplasms. Front Immunol. 2021;12:683401.","journal-title":"Front Immunol"},{"key":"2569_CR262","doi-asserted-by":"crossref","first-page":"2252","DOI":"10.1182\/blood.V99.6.2252","volume":"99","author":"DP Steensma","year":"2002","unstructured":"Steensma DP, Mesa RA, Li CY, Gray L, Tefferi A. Etanercept, a soluble tumor necrosis factor receptor, palliates constitutional symptoms in patients with myelofibrosis with myeloid metaplasia: results of a pilot study. Blood. 2002;99:2252\u20134.","journal-title":"Blood"},{"key":"2569_CR263","doi-asserted-by":"crossref","first-page":"e90932","DOI":"10.1172\/jci.insight.90932","volume":"2","author":"L Yue","year":"2017","unstructured":"Yue L, Bartenstein M, Zhao W, Ho WT, Han Y, Murdun C, et al. Efficacy of ALK5 inhibition in myelofibrosis. JCI Insight. 2017;2:e90932.","journal-title":"JCI Insight"},{"key":"2569_CR264","doi-asserted-by":"crossref","unstructured":"Jaiswal S, Ebert BL. Clonal hematopoiesis in human aging and disease. Science 2019;366:eaan4673.","DOI":"10.1126\/science.aan4673"},{"key":"2569_CR265","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1056\/NEJMoa1701719","volume":"377","author":"S Jaiswal","year":"2017","unstructured":"Jaiswal S, Natarajan P, Silver AJ, Gibson CJ, Bick AG, Shvartz E, et al. Clonal hematopoiesis and risk of atherosclerotic cardiovascular disease. N Engl J Med. 2017;377:111\u201321.","journal-title":"N Engl J Med"},{"key":"2569_CR266","doi-asserted-by":"crossref","first-page":"833","DOI":"10.1016\/j.stem.2018.10.013","volume":"23","author":"Z Cai","year":"2018","unstructured":"Cai Z, Kotzin JJ, Ramdas B, Chen S, Nelanuthala S, Palam LR, et al. Inhibition of inflammatory signaling in Tet2 mutant preleukemic cells mitigates stress-induced abnormalities and clonal hematopoiesis. Cell Stem cell. 2018;23:833\u2013e835.","journal-title":"Cell Stem cell"},{"key":"2569_CR267","doi-asserted-by":"crossref","first-page":"572","DOI":"10.1038\/s44161-023-00281-3","volume":"2","author":"W Liu","year":"2023","unstructured":"Liu W, Yalcinkaya M, Maestre IF, Olszewska M, Ampomah PB, Heimlich JB, et al. Blockade of IL-6 signaling alleviates atherosclerosis in Tet2-deficient clonal hematopoiesis. Nat Cardiovasc Res. 2023;2:572\u201386.","journal-title":"Nat Cardiovasc Res"},{"key":"2569_CR268","doi-asserted-by":"crossref","first-page":"791","DOI":"10.1093\/eurheartj\/ehad670","volume":"45","author":"A Schuermans","year":"2024","unstructured":"Schuermans A, Vlasschaert C, Nauffal V, Cho SMJ, Uddin MM, Nakao T, et al. Clonal haematopoiesis of indeterminate potential predicts incident cardiac arrhythmias. Eur Heart J. 2024;45:791\u2013805.","journal-title":"Eur Heart J"},{"key":"2569_CR269","doi-asserted-by":"crossref","first-page":"810","DOI":"10.1038\/s41591-024-02854-6","volume":"30","author":"C Vlasschaert","year":"2024","unstructured":"Vlasschaert C, Robinson-Cohen C, Chen J, Akwo E, Parker AC, Silver SA, et al. Clonal hematopoiesis of indeterminate potential is associated with acute kidney injury. Nat Med. 2024;30:810\u20137.","journal-title":"Nat Med"},{"key":"2569_CR270","doi-asserted-by":"crossref","first-page":"576","DOI":"10.1111\/ejh.13845","volume":"109","author":"MK Larsen","year":"2022","unstructured":"Larsen MK, Skov V, Kjaer L, Moller-Palacino NA, Pedersen RK, Andersen M, et al. Clonal haematopoiesis of indeterminate potential and impaired kidney function-A Danish general population study with 11 years follow-up. Eur J Haematol. 2022;109:576\u201385.","journal-title":"Eur J Haematol"},{"key":"2569_CR271","doi-asserted-by":"crossref","unstructured":"Siegerist F, Schnoeder T, Jayavelu A, Perner F, Jost7 P, Hammer E, et al. Chronic kidney dysfunction induced by Jak2V617F-mediated mesangiolysis. ASH Ann Meeting Abstracts. 2024;144:3147.","DOI":"10.1182\/blood-2024-205670"},{"key":"2569_CR272","doi-asserted-by":"crossref","first-page":"747","DOI":"10.1038\/s41586-023-05857-4","volume":"616","author":"WJ Wong","year":"2023","unstructured":"Wong WJ, Emdin C, Bick AG, Zekavat SM, Niroula A, Pirruccello JP, et al. Clonal haematopoiesis and risk of chronic liver disease. Nature. 2023;616:747\u201354.","journal-title":"Nature"},{"key":"2569_CR273","doi-asserted-by":"crossref","unstructured":"Hamarsheh S, Osswald L, Saller BS, Unger S, De Feo D, Vinnakota JM, et al. Oncogenic KrasG12D causes myeloproliferation via NLRP3 inflammasome activation. Nat Commun. 2020;11:1659.","DOI":"10.1038\/s41467-020-15497-1"},{"key":"2569_CR274","doi-asserted-by":"crossref","first-page":"339","DOI":"10.1002\/ajh.24976","volume":"93","author":"F Lussana","year":"2018","unstructured":"Lussana F, Cattaneo M, Rambaldi A, Squizzato A. Ruxolitinib-associated infections: a systematic review and meta-analysis. Am J Hematol. 2018;93:339\u201347.","journal-title":"Am J Hematol"},{"key":"2569_CR275","doi-asserted-by":"crossref","first-page":"426","DOI":"10.1056\/NEJMoa1409002","volume":"372","author":"AM Vannucchi","year":"2015","unstructured":"Vannucchi AM, Kiladjian JJ, Griesshammer M, Masszi T, Durrant S, Passamonti F, et al. Ruxolitinib versus standard therapy for the treatment of polycythemia vera. N Engl J Med. 2015;372:426\u201335.","journal-title":"N Engl J Med"},{"key":"2569_CR276","doi-asserted-by":"crossref","first-page":"60","DOI":"10.1111\/bjh.13519","volume":"171","author":"C Keohane","year":"2015","unstructured":"Keohane C, Kordasti S, Seidl T, Perez Abellan P, Thomas NS, Harrison CN, et al. JAK inhibition induces silencing of T Helper cytokine secretion and a profound reduction in T regulatory cells. Br J Haematol. 2015;171:60\u201373.","journal-title":"Br J Haematol"},{"key":"2569_CR277","doi-asserted-by":"crossref","first-page":"824","DOI":"10.1111\/bjh.13373","volume":"169","author":"S Parampalli Yajnanarayana","year":"2015","unstructured":"Parampalli Yajnanarayana S, Stubig T, Cornez I, Alchalby H, Schonberg K, Rudolph J, et al. JAK1\/2 inhibition impairs T cell function in vitro and in patients with myeloproliferative neoplasms. Br J Haematol. 2015;169:824\u201333.","journal-title":"Br J Haematol"},{"key":"2569_CR278","doi-asserted-by":"crossref","first-page":"449","DOI":"10.1038\/leu.2013.296","volume":"28","author":"M Massa","year":"2014","unstructured":"Massa M, Rosti V, Campanelli R, Fois G, Barosi G. Rapid and long-lasting decrease of T-regulatory cells in patients with myelofibrosis treated with ruxolitinib. Leukemia. 2014;28:449\u201351.","journal-title":"Leukemia"},{"key":"2569_CR279","doi-asserted-by":"crossref","first-page":"1043","DOI":"10.1038\/nm.3645","volume":"20","author":"L Xing","year":"2014","unstructured":"Xing L, Dai Z, Jabbari A, Cerise JE, Higgins CA, Gong W, et al. Alopecia areata is driven by cytotoxic T lymphocytes and is reversed by JAK inhibition. Nat Med. 2014;20:1043\u20139.","journal-title":"Nat Med"},{"key":"2569_CR280","doi-asserted-by":"crossref","first-page":"1192","DOI":"10.1182\/blood-2013-03-484642","volume":"122","author":"A Heine","year":"2013","unstructured":"Heine A, Held SA, Daecke SN, Wallner S, Yajnanarayana SP, Kurts C, et al. The JAK-inhibitor ruxolitinib impairs dendritic cell function in vitro and in vivo. Blood. 2013;122:1192\u2013202.","journal-title":"Blood"},{"key":"2569_CR281","doi-asserted-by":"crossref","first-page":"2213","DOI":"10.1136\/annrheumdis-2014-205615","volume":"73","author":"SP Wang","year":"2014","unstructured":"Wang SP, Iwata S, Nakayamada S, Sakata K, Yamaoka K. Tanaka Y. Tofacitinib, a JAK inhibitor, inhibits human B cell activation in vitro. Ann Rheum Dis. 2014;73:2213\u20135.","journal-title":"Ann Rheum Dis"},{"key":"2569_CR282","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1016\/j.jaut.2016.10.005","volume":"77","author":"M Rizzi","year":"2017","unstructured":"Rizzi M, Lorenzetti R, Fischer K, Staniek J, Janowska I, Troilo A, et al. Impact of tofacitinib treatment on human B-cells in vitro and in vivo. J Autoimmun. 2017;77:55\u201366.","journal-title":"J Autoimmun"},{"key":"2569_CR283","doi-asserted-by":"crossref","first-page":"1865","DOI":"10.3324\/haematol.2013.092155","volume":"98","author":"S Verstovsek","year":"2013","unstructured":"Verstovsek S, Mesa RA, Gotlib J, Levy RS, Gupta V, DiPersio JF, et al. Efficacy, safety and survival with ruxolitinib in patients with myelofibrosis: results of a median 2-year follow-up of COMFORT-I. Haematologica. 2013;98:1865\u201371.","journal-title":"Haematologica"},{"key":"2569_CR284","doi-asserted-by":"crossref","first-page":"1739","DOI":"10.1182\/blood.2020004823","volume":"135","author":"M Jagasia","year":"2020","unstructured":"Jagasia M, Perales MA, Schroeder MA, Ali H, Shah NN, Chen YB, et al. Ruxolitinib for the treatment of steroid-refractory acute GVHD (REACH1): a multicenter, open-label phase 2 trial. Blood. 2020;135:1739\u201349.","journal-title":"Blood"},{"key":"2569_CR285","doi-asserted-by":"crossref","first-page":"e109799","DOI":"10.1371\/journal.pone.0109799","volume":"9","author":"J Choi","year":"2014","unstructured":"Choi J, Cooper ML, Alahmari B, Ritchey J, Collins L, Holt M, et al. Pharmacologic blockade of JAK1\/JAK2 reduces GvHD and preserves the graft-versus-leukemia effect. PLoS ONE. 2014;9:e109799.","journal-title":"PLoS ONE"},{"key":"2569_CR286","doi-asserted-by":"crossref","first-page":"991","DOI":"10.1038\/leu.2015.218","volume":"30","author":"F Perner","year":"2016","unstructured":"Perner F, Schnoder TM, Ranjan S, Wolleschak D, Ebert C, Pils MC, et al. Specificity of JAK-kinase inhibition determines impact on human and murine T-cell function. Leukemia. 2016;30:991\u20135.","journal-title":"Leukemia"},{"key":"2569_CR287","doi-asserted-by":"crossref","first-page":"327","DOI":"10.3324\/haematol.2016.151126","volume":"102","author":"JO Mascarenhas","year":"2017","unstructured":"Mascarenhas JO, Talpaz M, Gupta V, Foltz LM, Savona MR, Paquette R, et al. Primary analysis of a phase II open-label trial of INCB039110, a selective JAK1 inhibitor, in patients with myelofibrosis. Haematologica. 2017;102:327\u201335.","journal-title":"Haematologica"},{"key":"2569_CR288","doi-asserted-by":"crossref","unstructured":"De Vries LCS, Ludbrook VJ, Hicks KJ, D'Haens GR. GSK2586184, a JAK1 selective inhibitor, in two patients with ulcerative colitis. BMJ Case Rep. 2017;2017:bcr2017221078.","DOI":"10.1136\/bcr-2017-221078"},{"key":"2569_CR289","doi-asserted-by":"crossref","first-page":"1009","DOI":"10.1136\/annrheumdis-2016-210105","volume":"76","author":"A Kavanaugh","year":"2017","unstructured":"Kavanaugh A, Kremer J, Ponce L, Cseuz R, Reshetko OV, Stanislavchuk M, et al. Filgotinib (GLPG0634\/GS-6034), an oral selective JAK1 inhibitor, is effective as monotherapy in patients with active rheumatoid arthritis: results from a randomised, dose-finding study (DARWIN 2). Ann Rheum Dis. 2017;76:1009\u201319.","journal-title":"Ann Rheum Dis"},{"key":"2569_CR290","doi-asserted-by":"crossref","first-page":"2857","DOI":"10.1002\/art.39808","volume":"68","author":"MC Genovese","year":"2016","unstructured":"Genovese MC, Smolen JS, Weinblatt ME, Burmester GR, Meerwein S, Camp HS, et al. Efficacy and safety of ABT-494, a selective JAK-1 inhibitor, in a phase IIb study in patients with rheumatoid arthritis and an inadequate response to methotrexate. Arthritis Rheumatol. 2016;68:2857\u201366.","journal-title":"Arthritis Rheumatol"},{"key":"2569_CR291","doi-asserted-by":"crossref","first-page":"1420","DOI":"10.1177\/0961203316640910","volume":"25","author":"L Kahl","year":"2016","unstructured":"Kahl L, Patel J, Layton M, Binks M, Hicks K, Leon G, et al. Safety, tolerability, efficacy and pharmacodynamics of the selective JAK1 inhibitor GSK2586184 in patients with systemic lupus erythematosus. Lupus. 2016;25:1420\u201330.","journal-title":"Lupus"},{"key":"2569_CR292","doi-asserted-by":"crossref","first-page":"985","DOI":"10.1111\/bjd.14399","volume":"174","author":"VJ Ludbrook","year":"2016","unstructured":"Ludbrook VJ, Hicks KJ, Hanrott KE, Patel JS, Binks MH, Wyres MR, et al. Investigation of selective JAK1 inhibitor GSK2586184 for the treatment of psoriasis in a randomized placebo-controlled phase IIa study. British J Dermatol. 2016;174:985\u201395.","journal-title":"British J Dermatol"},{"key":"2569_CR293","doi-asserted-by":"crossref","first-page":"2367","DOI":"10.1016\/S0140-6736(18)32483-8","volume":"392","author":"P Mease","year":"2018","unstructured":"Mease P, Coates LC, Helliwell PS, Stanislavchuk M, Rychlewska-Hanczewska A, Dudek A, et al. Efficacy and safety of filgotinib, a selective Janus kinase 1 inhibitor, in patients with active psoriatic arthritis (EQUATOR): results from a randomised, placebo-controlled, phase 2 trial. Lancet. 2018;392:2367\u201377.","journal-title":"Lancet"},{"key":"2569_CR294","doi-asserted-by":"crossref","first-page":"2378","DOI":"10.1016\/S0140-6736(18)32463-2","volume":"392","author":"D van der Heijde","year":"2018","unstructured":"van der Heijde D, Baraliakos X, Gensler LS, Maksymowych WP, Tseluyko V, Nadashkevich O, et al. Efficacy and safety of filgotinib, a selective Janus kinase 1 inhibitor, in patients with active ankylosing spondylitis (TORTUGA): results from a randomised, placebo-controlled, phase 2 trial. Lancet. 2018;392:2378\u201387.","journal-title":"Lancet"},{"key":"2569_CR295","doi-asserted-by":"crossref","first-page":"266","DOI":"10.1016\/S0140-6736(16)32537-5","volume":"389","author":"S Vermeire","year":"2017","unstructured":"Vermeire S, Schreiber S, Petryka R, Kuehbacher T, Hebuterne X, Roblin X, et al. Clinical remission in patients with moderate-to-severe Crohn's disease treated with filgotinib (the FITZROY study): results from a phase 2, double-blind, randomised, placebo-controlled trial. Lancet. 2017;389:266\u201375.","journal-title":"Lancet"},{"key":"2569_CR296","doi-asserted-by":"crossref","first-page":"46","DOI":"10.1002\/art.39473","volume":"68","author":"MC Genovese","year":"2016","unstructured":"Genovese MC, van Vollenhoven RF, Pacheco-Tena C, Zhang Y, Kinnman N. VX-509 (Decernotinib), an oral selective JAK-3 inhibitor, in combination with methotrexate in patients with rheumatoid arthritis. Arthritis Rheumatol. 2016;68:46\u201355.","journal-title":"Arthritis Rheumatol"},{"key":"2569_CR297","doi-asserted-by":"crossref","first-page":"334","DOI":"10.1002\/art.38949","volume":"67","author":"RM Fleischmann","year":"2015","unstructured":"Fleischmann RM, Damjanov NS, Kivitz AJ, Legedza A, Hoock T, Kinnman N. A randomized, double-blind, placebo-controlled, twelve-week, dose-ranging study of decernotinib, an oral selective JAK-3 inhibitor, as monotherapy in patients with active rheumatoid arthritis. Arthritis Rheumatol. 2015;67:334\u201343.","journal-title":"Arthritis Rheumatol"},{"key":"2569_CR298","doi-asserted-by":"crossref","first-page":"1313","DOI":"10.1056\/NEJMoa1806382","volume":"379","author":"K Papp","year":"2018","unstructured":"Papp K, Gordon K, Thaci D, Morita A, Gooderham M, Foley P, et al. Phase 2 trial of selective tyrosine kinase 2 inhibition in psoriasis. Np Engl J Med. 2018;379:1313\u201321.","journal-title":"Np Engl J Med"},{"key":"2569_CR299","doi-asserted-by":"crossref","first-page":"429","DOI":"10.1126\/scitranslmed.aam7729","volume":"10","author":"A Prestipino","year":"2018","unstructured":"Prestipino A, Emhardt AJ, Aumann K, O'Sullivan D, Gorantla SP, Duquesne S, et al. Oncogenic JAK2(V617F) causes PD-L1 expression, mediating immune escape in myeloproliferative neoplasms. Sci Transl Med. 2018;10:429.","journal-title":"Sci Transl Med"},{"key":"2569_CR300","doi-asserted-by":"crossref","first-page":"2775","DOI":"10.1007\/s00277-024-05867-w","volume":"103","author":"S Isfort","year":"2024","unstructured":"Isfort S, von Bubnoff N, Al-Ali HK, Becker H, Gotze T, le Coutre P, et al. FRACTION: protocol of a phase II study of Fedratinib and Nivolumab combination in patients with myelofibrosis and resistance or suboptimal response to JAK-inhibitor treatment of the German MPN study group (GSG-MPN). Ann Hematol. 2024;103:2775\u201385.","journal-title":"Ann Hematol"},{"key":"2569_CR301","doi-asserted-by":"crossref","first-page":"214","DOI":"10.1016\/j.clml.2014.12.008","volume":"15","author":"RA Mesa","year":"2015","unstructured":"Mesa RA, Verstovsek S, Gupta V, Mascarenhas JO, Atallah E, Burn T, et al. Effects of ruxolitinib treatment on metabolic and nutritional parameters in patients with myelofibrosis from COMFORT-I. Clin Lymphoma Myeloma Leuk. 2015;15:214\u201321 e211.","journal-title":"Clin Lymphoma Myeloma Leuk"},{"key":"2569_CR302","doi-asserted-by":"crossref","first-page":"162","DOI":"10.1038\/s41586-021-04312-6","volume":"602","author":"N Williams","year":"2022","unstructured":"Williams N, Lee J, Mitchell E, Moore L, Baxter EJ, Hewinson J, et al. Life histories of myeloproliferative neoplasms inferred from phylogenies. Nature. 2022;602:162\u20138.","journal-title":"Nature"},{"key":"2569_CR303","doi-asserted-by":"crossref","first-page":"601","DOI":"10.1056\/NEJMoa1412098","volume":"372","author":"CA Ortmann","year":"2015","unstructured":"Ortmann CA, Kent DG, Nangalia J, Silber Y, Wedge DC, Grinfeld J, et al. Effect of mutation order on myeloproliferative neoplasms. N Engl J Med. 2015;372:601\u201312.","journal-title":"N Engl J Med"},{"key":"2569_CR304","doi-asserted-by":"crossref","first-page":"1065","DOI":"10.3324\/haematol.2016.143677","volume":"101","author":"HK Al-Ali","year":"2016","unstructured":"Al-Ali HK, Griesshammer M, le Coutre P, Waller CF, Liberati AM, Schafhausen P, et al. Safety and efficacy of ruxolitinib in an open-label, multicenter, single-arm phase 3b expanded-access study in patients with myelofibrosis: a snapshot of 1144 patients in the JUMP trial. Haematologica. 2016;101:1065\u201373.","journal-title":"Haematologica"},{"key":"2569_CR305","doi-asserted-by":"crossref","first-page":"3383","DOI":"10.1007\/s00277-023-05458-1","volume":"102","author":"S Koschmieder","year":"2023","unstructured":"Koschmieder S, Isfort S, Schulte C, Jacobasch L, Geer T, Reiser M, et al. Real-world analysis of ruxolitinib in myelofibrosis: interim results focusing on patients who were naive to JAK inhibitor therapy treated within the JAKoMo non-interventional, phase IV trial. Ann Hematol. 2023;102:3383\u201399.","journal-title":"Ann Hematol"},{"key":"2569_CR306","doi-asserted-by":"crossref","first-page":"3534","DOI":"10.1200\/JCO.22.01935","volume":"41","author":"CN Harrison","year":"2023","unstructured":"Harrison CN, Nangalia J, Boucher R, Jackson A, Yap C, O'Sullivan J, et al. Ruxolitinib versus best available therapy for polycythemia vera intolerant or resistant to hydroxycarbamide in a randomized trial. J Clin Oncol Off J Am Soc Clin Oncol. 2023;41:3534\u201344.","journal-title":"J Clin Oncol Off J Am Soc Clin Oncol"},{"key":"2569_CR307","doi-asserted-by":"crossref","first-page":"796","DOI":"10.1016\/j.clml.2024.06.012","volume":"24","author":"N Gagelmann","year":"2024","unstructured":"Gagelmann N, Bose P, Gupta V, McLornan DP, Vachhani P, Al-Ali HK, et al. Consistency of spleen and symptom reduction regardless of cytopenia in patients with myelofibrosis treated with pacritinib. Clin Lymphoma Myeloma Leuk. 2024;24:796\u2013803.","journal-title":"Clin Lymphoma Myeloma Leuk"},{"key":"2569_CR308","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1007\/s00277-021-04682-x","volume":"101","author":"S Verstovsek","year":"2022","unstructured":"Verstovsek S, Parasuraman S, Yu J, Shah A, Kumar S, Xi A, et al. Real-world survival of US patients with intermediate- to high-risk myelofibrosis: impact of ruxolitinib approval. Ann Hematol. 2022;101:131\u20137.","journal-title":"Ann Hematol"},{"key":"2569_CR309","doi-asserted-by":"crossref","first-page":"244","DOI":"10.1111\/bjh.17727","volume":"195","author":"A Pardanani","year":"2021","unstructured":"Pardanani A, Tefferi A, Masszi T, Mishchenko E, Drummond M, Jourdan E, et al. Updated results of the placebo-controlled, phase III JAKARTA trial of fedratinib in patients with intermediate-2 or high-risk myelofibrosis. Br J Haematol. 2021;195:244\u20138.","journal-title":"Br J Haematol"},{"key":"2569_CR310","doi-asserted-by":"crossref","first-page":"314","DOI":"10.1007\/s12185-024-03822-z","volume":"120","author":"K Shimoda","year":"2024","unstructured":"Shimoda K, Komatsu N, Matsumura I, Ikeda K, Hino M, Hidaka M, et al. Momelotinib versus ruxolitinib in JAK inhibitor-naive patients with myelofibrosis: an efficacy\/safety analysis in the Japanese subgroup of the phase 3 randomized SIMPLIFY-1 trial. Int J Hematol. 2024;120:314\u201324.","journal-title":"Int J Hematol"},{"key":"2569_CR311","doi-asserted-by":"crossref","first-page":"1314","DOI":"10.1080\/10428194.2024.2346733","volume":"65","author":"V Gupta","year":"2024","unstructured":"Gupta V, Yacoub A, Mesa RA, Harrison CN, Vannucchi AM, Kiladjian JJ, et al. Safety and efficacy of fedratinib in patients with myelofibrosis previously treated with ruxolitinib: primary analysis of FREEDOM trial. Leuk Lymphoma. 2024;65:1314\u201324.","journal-title":"Leuk Lymphoma"},{"key":"2569_CR312","doi-asserted-by":"crossref","unstructured":"Gerke MB, Christodoulou I, Karantanos T. Definitions, biology, and current therapeutic landscape of myelodysplastic\/myeloproliferative neoplasms. Cancers. 2023;15:3815.","DOI":"10.3390\/cancers15153815"},{"key":"2569_CR313","doi-asserted-by":"crossref","first-page":"e966","DOI":"10.1097\/HS9.0000000000000966","volume":"7","author":"RA Mesa","year":"2023","unstructured":"Mesa RA, Harrison C, Palmer JM, Gupta V, McLornan DP, McMullin MF, et al. Patient-reported outcomes and quality of Life in anemic and symptomatic patients with myelofibrosis: results from the MOMENTUM study. Hemasphere. 2023;7:e966.","journal-title":"Hemasphere"},{"key":"2569_CR314","doi-asserted-by":"crossref","first-page":"e225","DOI":"10.1016\/S2352-3026(17)30027-3","volume":"4","author":"RA Mesa","year":"2017","unstructured":"Mesa RA, Vannucchi AM, Mead A, Egyed M, Szoke A, Suvorov A, et al. Pacritinib versus best available therapy for the treatment of myelofibrosis irrespective of baseline cytopenias (PERSIST-1): an international, randomised, phase 3 trial. Lancet Haematol. 2017;4:e225\u2013e236.","journal-title":"Lancet Haematol"},{"key":"2569_CR315","doi-asserted-by":"crossref","first-page":"1855","DOI":"10.1002\/cncr.31986","volume":"125","author":"CB Benton","year":"2019","unstructured":"Benton CB, Boddu PC, DiNardo CD, Bose P, Wang F, Assi R, et al. Janus kinase 2 variants associated with the transformation of myeloproliferative neoplasms into acute myeloid leukemia. Cancer. 2019;125:1855\u201366.","journal-title":"Cancer"},{"key":"2569_CR316","doi-asserted-by":"crossref","first-page":"73","DOI":"10.3390\/hematolrep15010008","volume":"15","author":"M Delio","year":"2023","unstructured":"Delio M, Bryke C, Mendez L, Joseph L, Jassim S. JAK2 Mutations are rare and diverse in myelodysplastic syndromes: case series and review of the literature. Hematol Rep. 2023;15:73\u201387.","journal-title":"Hematol Rep"},{"key":"2569_CR317","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1182\/blood-2020-142078","volume":"136","author":"H Lesmana","year":"2020","unstructured":"Lesmana H, Popescu M, Lewis S, Sahoo SS, Goodings-Harris C, Onciu M, et al. Germline gain-of-function JAK3 mutation in familial chronic lymphoproliferative disorder of NK cells. Blood. 2020;136:9\u201310.","journal-title":"Blood"},{"key":"2569_CR318","doi-asserted-by":"crossref","first-page":"411","DOI":"10.1007\/s12185-014-1711-y","volume":"101","author":"S Kawashima-Goto","year":"2015","unstructured":"Kawashima-Goto S, Imamura T, Seki M, Kato M, Yoshida K, Sugimoto A, et al. Identification of a homozygous JAK3 V674A mutation caused by acquired uniparental disomy in a relapsed early T-cell precursor ALL patient. Int J Hematol. 2015;101:411\u20136.","journal-title":"Int J Hematol"},{"key":"2569_CR319","doi-asserted-by":"crossref","first-page":"309","DOI":"10.1002\/gcc.22141","volume":"53","author":"AK Bergmann","year":"2014","unstructured":"Bergmann AK, Schneppenheim S, Seifert M, Betts MJ, Haake A, Lopez C, et al. Recurrent mutation of JAK3 in T-cell prolymphocytic leukemia. Genes Chromosomes Cancer. 2014;53:309\u201316.","journal-title":"Genes Chromosomes Cancer"},{"key":"2569_CR320","doi-asserted-by":"crossref","first-page":"560","DOI":"10.3389\/fonc.2018.00560","volume":"8","author":"J Raivola","year":"2018","unstructured":"Raivola J, Hammaren HM, Virtanen AT, Bulleeraz V, Ward AC, Silvennoinen O. Hyperactivation of oncogenic JAK3 mutants depend on ATP binding to the pseudokinase domain. Front Oncol. 2018;8:560.","journal-title":"Front Oncol"},{"key":"2569_CR321","doi-asserted-by":"crossref","unstructured":"Velatooru LR, Hu CH, Bijani P, Wang X, Bojaxhi P, Chen H, et al. New JAK3-INSL3 fusion transcript-an oncogenic event in cutaneous T-cell lymphoma. Cells. 2023;12:2381.","DOI":"10.3390\/cells12192381"}],"container-title":["Leukemia"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.nature.com\/articles\/s41375-025-02569-8.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/s41375-025-02569-8","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/s41375-025-02569-8.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,5,6]],"date-time":"2025-05-06T11:47:40Z","timestamp":1746532060000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.nature.com\/articles\/s41375-025-02569-8"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,3,26]]},"references-count":321,"journal-issue":{"issue":"5","published-print":{"date-parts":[[2025,5]]}},"alternative-id":["2569"],"URL":"https:\/\/doi.org\/10.1038\/s41375-025-02569-8","relation":{},"ISSN":["0887-6924","1476-5551"],"issn-type":[{"value":"0887-6924","type":"print"},{"value":"1476-5551","type":"electronic"}],"subject":[],"published":{"date-parts":[[2025,3,26]]},"assertion":[{"value":"2 January 2025","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"21 February 2025","order":2,"name":"revised","label":"Revised","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"13 March 2025","order":3,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"26 March 2025","order":4,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"FHH is a consultant for BMS\/Celgene, AOP, Novartis, CTI, Janssen, AbbVie, GSK, Merck, CTI, Kartos, Telios and received research funding from: Novartis, BMS\/Celgene, and CTI. FP received travel support from Syndax Pharmaceuticals and CHARM Therapeutics. RZ has received honoraria from Novartis, Incyte, Sanofi, and Mallinckrodt. HLP has no conflicts of interest to disclose.","order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Competing interests"}}]}}