{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,23]],"date-time":"2026-10-23T19:22:49Z","timestamp":1792783369254,"version":"4.5.0"},"reference-count":100,"publisher":"Springer Science and Business Media LLC","issue":"11","license":[{"start":{"date-parts":[[2023,7,17]],"date-time":"2023-07-17T00:00:00Z","timestamp":1689552000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"},{"start":{"date-parts":[[2023,7,17]],"date-time":"2023-07-17T00:00:00Z","timestamp":1689552000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"}],"funder":[{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["81602327"],"award-info":[{"award-number":["81602327"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Zhishan Scholars Programs of Southeast University","award":["2242021R41070"],"award-info":[{"award-number":["2242021R41070"]}]}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Mol Neurobiol"],"published-print":{"date-parts":[[2023,11]]},"DOI":"10.1007\/s12035-023-03487-5","type":"journal-article","created":{"date-parts":[[2023,7,17]],"date-time":"2023-07-17T06:01:37Z","timestamp":1689573697000},"page":"6530-6541","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":8,"title":["Role of Non-Receptor-Type Tyrosine Phosphatases in Brain-Related Diseases"],"prefix":"10.1007","volume":"60","author":[{"given":"Yatong","family":"He","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ding","family":"Nan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6975-9467","authenticated-orcid":false,"given":"Hongmei","family":"Wang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2023,7,17]]},"reference":[{"issue":"7","key":"3487_CR1","doi-asserted-by":"publisher","first-page":"896","DOI":"10.1093\/neuonc\/nou087","volume":"16","author":"QT Ostrom","year":"2014","unstructured":"Ostrom QT et al (2014) The epidemiology of glioma in adults: a \u201cstate of the science\u201d review. Neuro Oncol 16(7):896\u2013913. https:\/\/doi.org\/10.1093\/neuonc\/nou087","journal-title":"Neuro Oncol"},{"issue":"21","key":"3487_CR2","doi-asserted-by":"publisher","first-page":"2402","DOI":"10.1200\/JCO.2017.73.0119","volume":"35","author":"BM Alexander","year":"2017","unstructured":"Alexander BM, Cloughesy TF (2017) Adult Glioblastoma. J Clin Oncol 35(21):2402\u20132409. https:\/\/doi.org\/10.1200\/JCO.2017.73.0119","journal-title":"J Clin Oncol"},{"issue":"1","key":"3487_CR3","doi-asserted-by":"publisher","first-page":"M19","DOI":"10.1016\/s0304-419x(01)00027-0","volume":"1551","author":"C Dai","year":"2001","unstructured":"Dai C, Holland EC (2001) Glioma models. Biochim Biophys Acta 1551(1):M19-27. https:\/\/doi.org\/10.1016\/s0304-419x(01)00027-0","journal-title":"Biochim Biophys Acta"},{"issue":"7216","key":"3487_CR4","doi-asserted-by":"publisher","first-page":"1061","DOI":"10.1038\/nature07385","volume":"455","author":"Cancer Genome Atlas Research Network","year":"2008","unstructured":"Cancer Genome Atlas Research Network (2008) Comprehensive genomic characterization defines human glioblastoma genes and core pathways. Nature 455(7216):1061\u20131068. https:\/\/doi.org\/10.1038\/nature07385","journal-title":"Nature"},{"issue":"1","key":"3487_CR5","doi-asserted-by":"publisher","first-page":"42","DOI":"10.1016\/j.ccell.2017.06.003","volume":"32","author":"Q Wang","year":"2017","unstructured":"Wang Q et al (2017) Tumor evolution of glioma-intrinsic gene expression subtypes associates with immunological changes in the microenvironment. Cancer Cell 32(1):42-56.e6. https:\/\/doi.org\/10.1016\/j.ccell.2017.06.003","journal-title":"Cancer Cell"},{"issue":"2","key":"3487_CR6","doi-asserted-by":"publisher","first-page":"462","DOI":"10.1016\/j.cell.2013.09.034","volume":"155","author":"CW Brennan","year":"2013","unstructured":"Brennan CW et al (2013) The somatic genomic landscape of glioblastoma. Cell 155(2):462\u2013477. https:\/\/doi.org\/10.1016\/j.cell.2013.09.034","journal-title":"Cell"},{"issue":"3","key":"3487_CR7","doi-asserted-by":"publisher","first-page":"1353","DOI":"10.3390\/ijms23031353","volume":"23","author":"A Barzegar Behrooz","year":"2022","unstructured":"Barzegar Behrooz A, Talaie Z, Jusheghani F, \u0141os MJ, Klonisch T, Ghavami S (2022) Wnt and PI3K\/Akt\/mTOR survival pathways as therapeutic targets in Glioblastoma. Int J Mol Sci 23(3):1353. https:\/\/doi.org\/10.3390\/ijms23031353","journal-title":"Int J Mol Sci"},{"issue":"9","key":"3487_CR8","doi-asserted-by":"publisher","first-page":"827","DOI":"10.1038\/s41419-021-04107-7","volume":"12","author":"C Dong","year":"2021","unstructured":"Dong C et al (2021) PPFIBP1 induces glioma cell migration and invasion through FAK\/Src\/JNK signaling pathway. Cell Death Dis 12(9):827. https:\/\/doi.org\/10.1038\/s41419-021-04107-7","journal-title":"Cell Death Dis"},{"issue":"8","key":"3487_CR9","doi-asserted-by":"publisher","first-page":"1110","DOI":"10.2174\/1871520614666140825110907","volume":"14","author":"C Ma","year":"2014","unstructured":"Ma C, Zhao G, Cruz MH, Siden A, Yakisich JS (2014) Translational gap in glioma research. Anticancer Agents Med Chem 14(8):1110\u20131120. https:\/\/doi.org\/10.2174\/1871520614666140825110907","journal-title":"Anticancer Agents Med Chem"},{"key":"3487_CR10","doi-asserted-by":"publisher","first-page":"28","DOI":"10.1016\/j.jocn.2017.10.001","volume":"47","author":"AF Guishard","year":"2018","unstructured":"Guishard AF, Yakisich JS, Azad N, Iyer AKV (2018) Translational gap in ongoing clinical trials for glioma. J Clin Neurosci 47:28\u201342. https:\/\/doi.org\/10.1016\/j.jocn.2017.10.001","journal-title":"J Clin Neurosci"},{"issue":"24","key":"3487_CR11","doi-asserted-by":"publisher","first-page":"5789","DOI":"10.3390\/molecules25245789","volume":"25","author":"Z Breijyeh","year":"2020","unstructured":"Breijyeh Z, Karaman R (2020) Comprehensive review on Alzheimer\u2019s Disease: causes and treatment. Molecules 25(24):5789. https:\/\/doi.org\/10.3390\/molecules25245789","journal-title":"Molecules"},{"issue":"3","key":"3487_CR12","doi-asserted-by":"publisher","first-page":"270","DOI":"10.1007\/s11102-019-00957-9","volume":"22","author":"D Pavlovic","year":"2019","unstructured":"Pavlovic D, Pekic S, Stojanovic M, Popovic V (2019) Traumatic brain injury: neuropathological, neurocognitive and neurobehavioral sequelae\u2019. Pituitary 22(3):270\u2013282. https:\/\/doi.org\/10.1007\/s11102-019-00957-9","journal-title":"Pituitary"},{"issue":"10","key":"3487_CR13","doi-asserted-by":"publisher","first-page":"1227","DOI":"10.1038\/aps.2014.80","volume":"35","author":"R-J He","year":"2014","unstructured":"He R-J, Yu Z-H, Zhang R-Y, Zhang Z-Y (2014) Protein tyrosine phosphatases as potential therapeutic targets. Acta Pharmacol Sin 35(10):1227\u20131246. https:\/\/doi.org\/10.1038\/aps.2014.80","journal-title":"Acta Pharmacol Sin"},{"issue":"10172","key":"3487_CR14","doi-asserted-by":"publisher","first-page":"689","DOI":"10.1016\/S0140-6736(18)32596-0","volume":"393","author":"RD Thijs","year":"2019","unstructured":"Thijs RD, Surges R, O\u2019Brien TJ, Sander JW (2019) Epilepsy in adults. Lancet 393(10172):689\u2013701. https:\/\/doi.org\/10.1016\/S0140-6736(18)32596-0","journal-title":"Lancet"},{"key":"3487_CR15","unstructured":"Frontiers | Neuroimaging Advances in Parkinson\u2019s Disease and Atypical Parkinsonian Syndromes\u2019 (2020) https:\/\/www.frontiersin.org\/articles\/10.3389\/fneur.572976\/full.\u00a0 Accessed 16 May 2023"},{"issue":"2","key":"3487_CR16","doi-asserted-by":"publisher","first-page":"225","DOI":"10.1016\/0092-8674(95)90405-0","volume":"80","author":"T Hunter","year":"1995","unstructured":"Hunter T (1995) Protein kinases and phosphatases: the yin and yang of protein phosphorylation and signaling. Cell 80(2):225\u2013236. https:\/\/doi.org\/10.1016\/0092-8674(95)90405-0","journal-title":"Cell"},{"issue":"5","key":"3487_CR17","doi-asserted-by":"publisher","first-page":"257","DOI":"10.1159\/000490106","volume":"95","author":"WCM Dempke","year":"2018","unstructured":"Dempke WCM, Uciechowski P, Fenchel K, Chevassut T (2018) Targeting SHP-1, 2 and SHIP pathways: a novel strategy for cancer treatment? Oncology 95(5):257\u2013269. https:\/\/doi.org\/10.1159\/000490106","journal-title":"Oncology"},{"key":"3487_CR18","doi-asserted-by":"publisher","first-page":"104595","DOI":"10.1016\/j.phrs.2019.104595","volume":"152","author":"Q Liu","year":"2020","unstructured":"Liu Q, Qu J, Zhao M, Xu Q, Sun Y (2020) Targeting SHP2 as a promising strategy for cancer immunotherapy. Pharmacol Res 152:104595. https:\/\/doi.org\/10.1016\/j.phrs.2019.104595","journal-title":"Pharmacol Res"},{"issue":"1","key":"3487_CR19","doi-asserted-by":"publisher","first-page":"78","DOI":"10.2174\/187152011794941262","volume":"11","author":"G Freiss","year":"2011","unstructured":"Freiss G, Chalbos D (2011) PTPN13\/PTPL1: an important regulator of tumor aggressiveness. Anticancer Agents Med Chem 11(1):78\u201388. https:\/\/doi.org\/10.2174\/187152011794941262","journal-title":"Anticancer Agents Med Chem"},{"key":"3487_CR20","doi-asserted-by":"publisher","unstructured":"Kostrzewa T, Styszko J, Gorska-Ponikowska M, Sledzinski T, Kuban-Jankowska A (2019) Inhibitors of Protein Tyrosine Phosphatase PTP1B with anticancer potential. Anticancer Res 39(7):3379\u20133384. https:\/\/doi.org\/10.21873\/anticanres.13481","DOI":"10.21873\/anticanres.13481"},{"issue":"1","key":"3487_CR21","doi-asserted-by":"publisher","first-page":"17","DOI":"10.2174\/1874467212666190724150723","volume":"13","author":"A Kumar","year":"2020","unstructured":"Kumar A, Rana D, Rana R, Bhatia R (2020) Protein tyrosine phosphatase (PTP1B): a promising drug target against life-threatening ailments. Curr Mol Pharmacol 13(1):17\u201330. https:\/\/doi.org\/10.2174\/1874467212666190724150723","journal-title":"Curr Mol Pharmacol"},{"issue":"3","key":"3487_CR22","doi-asserted-by":"publisher","first-page":"181","DOI":"10.2174\/1568009622666220128113400","volume":"22","author":"P-J Chen","year":"2022","unstructured":"Chen P-J, Zhang Y-T (2022) Protein tyrosine phosphatase 1B (PTP1B): insights into its new implications in tumorigenesis. Curr Cancer Drug Targets 22(3):181\u2013194. https:\/\/doi.org\/10.2174\/1568009622666220128113400","journal-title":"Curr Cancer Drug Targets"},{"issue":"4","key":"3487_CR23","doi-asserted-by":"publisher","first-page":"246","DOI":"10.2174\/1568026619666190201152153","volume":"19","author":"P Eleftheriou","year":"2019","unstructured":"Eleftheriou P, Geronikaki A, Petrou A (2019) PTP1b inhibition, a promising approach for the treatment of diabetes type II. Curr Top Med Chem 19(4):246\u2013263. https:\/\/doi.org\/10.2174\/1568026619666190201152153","journal-title":"Curr Top Med Chem"},{"key":"3487_CR24","doi-asserted-by":"publisher","first-page":"112376","DOI":"10.1016\/j.ejmech.2020.112376","volume":"199","author":"B Sharma","year":"2020","unstructured":"Sharma B et al (2020) Recent advance on PTP1B inhibitors and their biomedical applications. Eur J Med Chem 199:112376. https:\/\/doi.org\/10.1016\/j.ejmech.2020.112376","journal-title":"Eur J Med Chem"},{"key":"3487_CR25","doi-asserted-by":"publisher","unstructured":"Kamceva M, Benedict J, Nairn AC, Lombroso PJ (2016) Role of striatal-enriched tyrosine phosphatase in neuronal function. Neural Plast :8136925. https:\/\/doi.org\/10.1155\/2016\/8136925","DOI":"10.1155\/2016\/8136925"},{"key":"3487_CR26","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/j.neures.2014.08.018","volume":"89","author":"T Karasawa","year":"2014","unstructured":"Karasawa T, Lombroso PJ (2014) Disruption of striatal-enriched protein tyrosine phosphatase (STEP) function in neuropsychiatric disorders. Neurosci Res 89:1\u20139. https:\/\/doi.org\/10.1016\/j.neures.2014.08.018","journal-title":"Neurosci Res"},{"key":"3487_CR27","doi-asserted-by":"publisher","first-page":"303","DOI":"10.1016\/B978-0-12-394816-8.00009-X","volume":"64","author":"J Xu","year":"2012","unstructured":"Xu J, Kurup P, Nairn AC, Lombroso PJ (2012) Striatal-enriched protein tyrosine phosphatase in Alzheimer\u2019s disease. Adv Pharmacol 64:303\u2013325. https:\/\/doi.org\/10.1016\/B978-0-12-394816-8.00009-X","journal-title":"Adv Pharmacol"},{"issue":"16","key":"3487_CR28","doi-asserted-by":"publisher","first-page":"7242","DOI":"10.1073\/pnas.88.16.7242","volume":"88","author":"PJ Lombroso","year":"1991","unstructured":"Lombroso PJ, Murdoch G, Lerner M (1991) Molecular characterization of a protein-tyrosine-phosphatase enriched in striatum. Proc Natl Acad Sci U S A 88(16):7242\u20137246. https:\/\/doi.org\/10.1073\/pnas.88.16.7242","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"1","key":"3487_CR29","doi-asserted-by":"publisher","first-page":"69","DOI":"10.1002\/syn.20608","volume":"63","author":"DV Venkitaramani","year":"2009","unstructured":"Venkitaramani DV et al (2009) Knockout of striatal enriched protein tyrosine phosphatase in mice results in increased ERK1\/2 phosphorylation. Synapse 63(1):69\u201381. https:\/\/doi.org\/10.1002\/syn.20608","journal-title":"Synapse"},{"issue":"3","key":"3487_CR30","doi-asserted-by":"publisher","first-page":"311","DOI":"10.1016\/j.conb.2004.04.001","volume":"14","author":"JD Sweatt","year":"2004","unstructured":"Sweatt JD (2004) Mitogen-activated protein kinases in synaptic plasticity and memory. Curr Opin Neurobiol 14(3):311\u2013317. https:\/\/doi.org\/10.1016\/j.conb.2004.04.001","journal-title":"Curr Opin Neurobiol"},{"issue":"Suppl 2","key":"3487_CR31","doi-asserted-by":"publisher","first-page":"S12","DOI":"10.1186\/1471-2202-9-S2-S12","volume":"9","author":"AS Borders","year":"2008","unstructured":"Borders AS, de Almeida L, Van Eldik LJ, Watterson DM (2008) The p38alpha mitogen-activated protein kinase as a central nervous system drug discovery target. BMC Neurosci 9(Suppl 2):S12. https:\/\/doi.org\/10.1186\/1471-2202-9-S2-S12","journal-title":"BMC Neurosci"},{"issue":"3","key":"3487_CR32","doi-asserted-by":"publisher","first-page":"529","DOI":"10.1124\/mol.110.068643","volume":"80","author":"PH Wu","year":"2011","unstructured":"Wu PH, Coultrap SJ, Browning MD, Proctor WR (2011) Functional adaptation of the N-methyl-D-aspartate receptor to inhibition by ethanol is modulated by striatal-enriched protein tyrosine phosphatase and p38 mitogen-activated protein kinase. Mol Pharmacol 80(3):529\u2013537. https:\/\/doi.org\/10.1124\/mol.110.068643","journal-title":"Mol Pharmacol"},{"issue":"2","key":"3487_CR33","doi-asserted-by":"publisher","first-page":"443","DOI":"10.1113\/JP278703","volume":"599","author":"S Won","year":"2021","unstructured":"Won S, Roche KW (2021) Regulation of glutamate receptors by striatal-enriched tyrosine phosphatase 61 (STEP61). J Physiol 599(2):443\u2013451. https:\/\/doi.org\/10.1113\/JP278703","journal-title":"J Physiol"},{"issue":"8","key":"3487_CR34","doi-asserted-by":"publisher","first-page":"1051","DOI":"10.1038\/nn1503","volume":"8","author":"EM Snyder","year":"2005","unstructured":"Snyder EM et al (2005) Regulation of NMDA receptor trafficking by amyloid-beta. Nat Neurosci 8(8):1051\u20131058. https:\/\/doi.org\/10.1038\/nn1503","journal-title":"Nat Neurosci"},{"issue":"1","key":"3487_CR35","doi-asserted-by":"publisher","first-page":"306","DOI":"10.1021\/acs.jmedchem.8b00857","volume":"62","author":"CS Tautermann","year":"2019","unstructured":"Tautermann CS et al (2019) Allosteric activation of Striatal-Enriched protein tyrosine phosphatase (STEP, PTPN5) by a fragment-like molecule. J Med Chem 62(1):306\u2013316. https:\/\/doi.org\/10.1021\/acs.jmedchem.8b00857","journal-title":"J Med Chem"},{"issue":"27","key":"3487_CR36","doi-asserted-by":"publisher","first-page":"24274","DOI":"10.1074\/jbc.M111683200","volume":"277","author":"T-H Nguyen","year":"2002","unstructured":"Nguyen T-H, Liu J, Lombroso PJ (2002) Striatal enriched phosphatase 61 dephosphorylates Fyn at phosphotyrosine 420. J Biol Chem 277(27):24274\u201324279. https:\/\/doi.org\/10.1074\/jbc.M111683200","journal-title":"J Biol Chem"},{"issue":"42","key":"3487_CR37","doi-asserted-by":"publisher","first-page":"10561","DOI":"10.1523\/JNEUROSCI.2666-08.2008","volume":"28","author":"Y Zhang","year":"2008","unstructured":"Zhang Y et al (2008) The tyrosine phosphatase STEP mediates AMPA receptor endocytosis after metabotropic glutamate receptor stimulation. J Neurosci 28(42):10561\u201310566. https:\/\/doi.org\/10.1523\/JNEUROSCI.2666-08.2008","journal-title":"J Neurosci"},{"issue":"1","key":"3487_CR38","doi-asserted-by":"publisher","first-page":"217","DOI":"10.1021\/acs.jmedchem.1c01303","volume":"65","author":"HS Szedlacsek","year":"2022","unstructured":"Szedlacsek HS et al (2022) Designed peptide inhibitors of STEP Phosphatase-GluA2 AMPA receptor Interaction enhance the cognitive performance in rats. J Med Chem 65(1):217\u2013233. https:\/\/doi.org\/10.1021\/acs.jmedchem.1c01303","journal-title":"J Med Chem"},{"issue":"10","key":"3487_CR39","doi-asserted-by":"publisher","first-page":"1985","DOI":"10.1158\/1055-9965.EPI-14-0275","volume":"23","author":"JP Thakkar","year":"2014","unstructured":"Thakkar JP et al (2014) Epidemiologic and molecular prognostic review of glioblastoma. Cancer Epidemiol Biomarkers Prev 23(10):1985\u20131996. https:\/\/doi.org\/10.1158\/1055-9965.EPI-14-0275","journal-title":"Cancer Epidemiol Biomarkers Prev"},{"key":"3487_CR40","doi-asserted-by":"publisher","unstructured":"Ostrom QT et al (2014) CBTRUS statistical report: primary brain and central nervous system tumors diagnosed in the United States in 2007\u20132011. Neuro Oncol 16(Suppl 4):iv1-63. https:\/\/doi.org\/10.1093\/neuonc\/nou223","DOI":"10.1093\/neuonc\/nou223"},{"issue":"9","key":"3487_CR41","doi-asserted-by":"publisher","first-page":"121","DOI":"10.3978\/j.issn.2305-5839.2015.05.10","volume":"3","author":"RM Young","year":"2015","unstructured":"Young RM, Jamshidi A, Davis G, Sherman JH (2015) Current trends in the surgical management and treatment of adult glioblastoma. Ann Transl Med 3(9):121. https:\/\/doi.org\/10.3978\/j.issn.2305-5839.2015.05.10","journal-title":"Ann Transl Med"},{"issue":"6","key":"3487_CR42","doi-asserted-by":"publisher","first-page":"803","DOI":"10.1007\/s00401-016-1545-1","volume":"131","author":"DN Louis","year":"2016","unstructured":"Louis DN et al (2016) The 2016 World Health Organization classification of tumors of the Central Nervous System: a summary. Acta Neuropathol 131(6):803\u2013820. https:\/\/doi.org\/10.1007\/s00401-016-1545-1","journal-title":"Acta Neuropathol"},{"issue":"2","key":"3487_CR43","doi-asserted-by":"publisher","first-page":"E241","DOI":"10.3390\/cancers11020241","volume":"11","author":"A Tomiyama","year":"2019","unstructured":"Tomiyama A, Kobayashi T, Mori K, Ichimura K (2019) Protein phosphatases-a touchy enemy in the battle against glioblastomas: a review. Cancers (Basel) 11(2):E241. https:\/\/doi.org\/10.3390\/cancers11020241","journal-title":"Cancers (Basel)"},{"issue":"8","key":"3487_CR44","doi-asserted-by":"publisher","first-page":"2062","DOI":"10.1002\/jcb.23125","volume":"112","author":"W Wang","year":"2011","unstructured":"Wang W et al (2011) Crystal structure of human protein tyrosine phosphatase SHP-1 in the open conformation. J Cell Biochem 112(8):2062\u20132071. https:\/\/doi.org\/10.1002\/jcb.23125","journal-title":"J Cell Biochem"},{"issue":"5","key":"3487_CR45","doi-asserted-by":"publisher","first-page":"4479","DOI":"10.1007\/s13277-013-1590-5","volume":"35","author":"L Sooman","year":"2014","unstructured":"Sooman L et al (2014) PTPN6 expression is epigenetically regulated and influences survival and response to chemotherapy in high-grade gliomas. Tumour Biol 35(5):4479\u20134488. https:\/\/doi.org\/10.1007\/s13277-013-1590-5","journal-title":"Tumour Biol"},{"key":"3487_CR46","doi-asserted-by":"publisher","first-page":"576310","DOI":"10.3389\/fimmu.2020.576310","volume":"11","author":"DR Myers","year":"2020","unstructured":"Myers DR et al (2020) Shp1 loss enhances macrophage effector function and promotes Anti-Tumor Immunity. Front Immunol 11:576310. https:\/\/doi.org\/10.3389\/fimmu.2020.576310","journal-title":"Front Immunol"},{"key":"3487_CR47","doi-asserted-by":"crossref","unstructured":"Banville D, Ahmad S, Stocco R, Shen SH (1994) A novel protein-tyrosine phosphatase with homology to both the cytoskeletal proteins of the band 4.1 family and junction-associated guanylate kinases. J Biol Chem 269(35):22320\u201322327","DOI":"10.1016\/S0021-9258(17)31792-1"},{"issue":"10","key":"3487_CR48","doi-asserted-by":"publisher","first-page":"509","DOI":"10.1016\/j.ejmg.2015.08.005","volume":"58","author":"M Tajan","year":"2015","unstructured":"Tajan M, de Rocca Serra A, Valet P, Edouard T, Yart A (2015) SHP2 sails from physiology to pathology. Eur J Med Genet 58(10):509\u2013525. https:\/\/doi.org\/10.1016\/j.ejmg.2015.08.005","journal-title":"Eur J Med Genet"},{"key":"3487_CR49","doi-asserted-by":"publisher","unstructured":"Zheng H, Yu W-M, Waclaw RR, Kontaridis MI, Neel BG, Qu C-K (2018) Gain-of-function mutations in the gene encoding the tyrosine phosphatase SHP2 induce hydrocephalus in a catalytically dependent manner. Sci Signal 11(522):eaao1591. https:\/\/doi.org\/10.1126\/scisignal.aao1591","DOI":"10.1126\/scisignal.aao1591"},{"issue":"4","key":"3487_CR50","doi-asserted-by":"publisher","first-page":"307","DOI":"10.1038\/nrc1837","volume":"6","author":"A Ostman","year":"2006","unstructured":"Ostman A, Hellberg C, B\u00f6hmer FD (2006) Protein-tyrosine phosphatases and cancer. Nat Rev Cancer 6(4):307\u2013320. https:\/\/doi.org\/10.1038\/nrc1837","journal-title":"Nat Rev Cancer"},{"issue":"28","key":"3487_CR51","doi-asserted-by":"publisher","first-page":"3164","DOI":"10.1038\/sj.onc.1203655","volume":"19","author":"Y Hakak","year":"2000","unstructured":"Hakak Y, Hsu YS, Martin GS (2000) Shp-2 mediates v-Src-induced morphological changes and activation of the anti-apoptotic protein kinase Akt. Oncogene 19(28):3164\u20133171. https:\/\/doi.org\/10.1038\/sj.onc.1203655","journal-title":"Oncogene"},{"issue":"2","key":"3487_CR52","doi-asserted-by":"publisher","first-page":"227","DOI":"10.1002\/jcp.10446","volume":"199","author":"C Ivins Zito","year":"2004","unstructured":"Ivins Zito C, Kontaridis MI, Fornaro M, Feng G-S, Bennett AM (2004) SHP-2 regulates the phosphatidylinositide 3\u2019-kinase\/Akt pathway and suppresses caspase 3-mediated apoptosis. J Cell Physiol 199(2):227\u2013236. https:\/\/doi.org\/10.1002\/jcp.10446","journal-title":"J Cell Physiol"},{"issue":"33","key":"3487_CR53","doi-asserted-by":"publisher","first-page":"22353","DOI":"10.1074\/jbc.M109.020495","volume":"284","author":"W Zhang","year":"2009","unstructured":"Zhang W et al (2009) Negative regulation of Stat3 by activating PTPN11 mutants contributes to the pathogenesis of Noonan syndrome and juvenile myelomonocytic leukemia. J Biol Chem 284(33):22353\u201322363. https:\/\/doi.org\/10.1074\/jbc.M109.020495","journal-title":"J Biol Chem"},{"issue":"2","key":"3487_CR54","doi-asserted-by":"publisher","first-page":"179","DOI":"10.1007\/s10555-008-9126-y","volume":"27","author":"G Chan","year":"2008","unstructured":"Chan G, Kalaitzidis D, Neel BG (2008) The tyrosine phosphatase Shp2 (PTPN11) in cancer. Cancer Metastasis Rev 27(2):179\u2013192. https:\/\/doi.org\/10.1007\/s10555-008-9126-y","journal-title":"Cancer Metastasis Rev"},{"issue":"Pt 16","key":"3487_CR55","doi-asserted-by":"publisher","first-page":"3555","DOI":"10.1242\/jcs.150862","volume":"127","author":"CM Furcht","year":"2014","unstructured":"Furcht CM et al (2014) Multivariate signaling regulation by SHP2 differentially controls proliferation and therapeutic response in glioma cells. J Cell Sci 127(Pt 16):3555\u20133567. https:\/\/doi.org\/10.1242\/jcs.150862","journal-title":"J Cell Sci"},{"key":"3487_CR56","doi-asserted-by":"publisher","first-page":"2343","DOI":"10.1016\/j.yexcr.2009.05.001","volume":"315","author":"Y Zhan","year":"2009","unstructured":"Zhan Y, Counelis GJ, O\u2019Rourke DM (2009) The protein tyrosine phosphatase SHP-2 is required for EGFRvIII oncogenic transformation in human glioblastoma cells. Exp Cell Res 315:2343\u20132357. https:\/\/doi.org\/10.1016\/j.yexcr.2009.05.001","journal-title":"Exp Cell Res"},{"issue":"3","key":"3487_CR57","doi-asserted-by":"publisher","first-page":"750","DOI":"10.1016\/j.apsb.2020.10.021","volume":"11","author":"Y Song","year":"2021","unstructured":"Song Y, Zhao M, Wu Y, Yu B, Liu H-M (2021) A multifunctional cross-validation high-throughput screening protocol enabling the discovery of new SHP2 inhibitors. Acta Pharm Sin B 11(3):750\u2013762. https:\/\/doi.org\/10.1016\/j.apsb.2020.10.021","journal-title":"Acta Pharm Sin B"},{"key":"3487_CR58","doi-asserted-by":"publisher","first-page":"106008","DOI":"10.1016\/j.intimp.2019.106008","volume":"80","author":"K Yu","year":"2020","unstructured":"Yu K et al (2020) Shp2 activation in bone marrow microenvironment mediates the drug resistance of B-cell acute lymphoblastic leukemia through enhancing the role of VCAM-1\/VLA-4. Int Immunopharmacol 80:106008. https:\/\/doi.org\/10.1016\/j.intimp.2019.106008","journal-title":"Int Immunopharmacol"},{"issue":"1","key":"3487_CR59","doi-asserted-by":"publisher","first-page":"13","DOI":"10.1016\/j.apsb.2020.07.010","volume":"11","author":"Z Song","year":"2021","unstructured":"Song Z et al (2021) Tyrosine phosphatase SHP2 inhibitors in tumor-targeted therapies. Acta Pharm Sin B 11(1):13\u201329. https:\/\/doi.org\/10.1016\/j.apsb.2020.07.010","journal-title":"Acta Pharm Sin B"},{"issue":"4","key":"3487_CR60","doi-asserted-by":"publisher","first-page":"491","DOI":"10.1016\/j.bbrc.2009.02.069","volume":"381","author":"M Song","year":"2009","unstructured":"Song M et al (2009) NSC-87877, inhibitor of SHP-1\/2 PTPs, inhibits dual-specificity phosphatase 26 (DUSP26). Biochem Biophys Res Commun 381(4):491\u2013495. https:\/\/doi.org\/10.1016\/j.bbrc.2009.02.069","journal-title":"Biochem Biophys Res Commun"},{"issue":"12","key":"3487_CR61","doi-asserted-by":"publisher","first-page":"1345","DOI":"10.1177\/0091270005282630","volume":"45","author":"L Zhou","year":"2005","unstructured":"Zhou L, Zuo Z, Chow MSS (2005) Danshen: an overview of its chemistry, pharmacology, pharmacokinetics, and clinical use. J Clin Pharmacol 45(12):1345\u20131359. https:\/\/doi.org\/10.1177\/0091270005282630","journal-title":"J Clin Pharmacol"},{"issue":"4","key":"3487_CR62","doi-asserted-by":"publisher","first-page":"365","DOI":"10.2174\/138920007780655441","volume":"8","author":"X-Y Yu","year":"2007","unstructured":"Yu X-Y et al (2007) Transport of cryptotanshinone, a major active triterpenoid in Salvia miltiorrhiza Bunge widely used in the treatment of stroke and Alzheimer\u2019s disease, across the blood-brain barrier. Curr Drug Metab 8(4):365\u2013378. https:\/\/doi.org\/10.2174\/138920007780655441","journal-title":"Curr Drug Metab"},{"issue":"5","key":"3487_CR63","doi-asserted-by":"publisher","first-page":"e2767","DOI":"10.1038\/cddis.2017.174","volume":"8","author":"L Lu","year":"2017","unstructured":"Lu L et al (2017) Cryptotanshinone inhibits human glioma cell proliferation in vitro and in vivo through SHP-2-dependent inhibition of STAT3 activation. Cell Death Dis 8(5):e2767. https:\/\/doi.org\/10.1038\/cddis.2017.174","journal-title":"Cell Death Dis"},{"issue":"14","key":"3487_CR64","doi-asserted-by":"publisher","first-page":"7510","DOI":"10.1021\/acs.jmedchem.0c00471","volume":"63","author":"M Wang","year":"2020","unstructured":"Wang M, Lu J, Wang M, Yang C-Y, Wang S (2020) Discovery of SHP2-D26 as a First, Potent, and Effective PROTAC Degrader of SHP2 Protein. J Med Chem 63(14):7510\u20137528. https:\/\/doi.org\/10.1021\/acs.jmedchem.0c00471","journal-title":"J Med Chem"},{"issue":"3","key":"3487_CR65","doi-asserted-by":"publisher","first-page":"139","DOI":"10.1016\/j.jphs.2020.06.002","volume":"144","author":"W Guo","year":"2020","unstructured":"Guo W, Xu Q (2020) Phosphatase-independent functions of SHP2 and its regulation by small molecule compounds. J Pharmacol Sci 144(3):139\u2013146. https:\/\/doi.org\/10.1016\/j.jphs.2020.06.002","journal-title":"J Pharmacol Sci"},{"key":"3487_CR66","doi-asserted-by":"publisher","unstructured":"Y. X et al (2021)Discovery of thalidomide-based PROTAC small molecules as the highly efficient SHP2 degraders. Eur J Med Chem 218. https:\/\/doi.org\/10.1016\/j.ejmech.2021.113341","DOI":"10.1016\/j.ejmech.2021.113341"},{"key":"3487_CR67","doi-asserted-by":"publisher","unstructured":"Zheng M et al (2021) Novel PROTACs for degradation of SHP2 protein. Bioorg Chem 110:104788. https:\/\/doi.org\/10.1016\/j.bioorg.2021.104788","DOI":"10.1016\/j.bioorg.2021.104788"},{"issue":"16","key":"3487_CR68","doi-asserted-by":"publisher","first-page":"2715","DOI":"10.1038\/sj.onc.1208247","volume":"24","author":"OD Abaan","year":"2005","unstructured":"Abaan OD, Levenson A, Khan O, Furth PA, Uren A, Toretsky JA (2005) PTPL1 is a direct transcriptional target of EWS-FLI1 and modulates Ewing\u2019s Sarcoma tumorigenesis. Oncogene 24(16):2715\u20132722. https:\/\/doi.org\/10.1038\/sj.onc.1208247","journal-title":"Oncogene"},{"issue":"24","key":"3487_CR69","doi-asserted-by":"publisher","first-page":"7170","DOI":"10.1046\/j.1432-1327.2000.01818.x","volume":"267","author":"Y Nakai","year":"2000","unstructured":"Nakai Y, Irie S, Sato TA (2000) Identification of IkappaBalpha as a substrate of Fas-associated phosphatase-1. Eur J Biochem 267(24):7170\u20137175. https:\/\/doi.org\/10.1046\/j.1432-1327.2000.01818.x","journal-title":"Eur J Biochem"},{"issue":"12","key":"3487_CR70","doi-asserted-by":"publisher","first-page":"E1659","DOI":"10.3390\/biom10121659","volume":"10","author":"S Mcheik","year":"2020","unstructured":"Mcheik S, Aptecar L, Coopman P, D\u2019Hondt V, Freiss G (2020) Dual role of the PTPN13 tyrosine phosphatase in cancer. Biomolecules 10(12):E1659. https:\/\/doi.org\/10.3390\/biom10121659","journal-title":"Biomolecules"},{"issue":"1313","key":"3487_CR71","doi-asserted-by":"publisher","first-page":"281","DOI":"10.1098\/rstb.1994.0107","volume":"345","author":"S Nagata","year":"1994","unstructured":"Nagata S (1994) Apoptosis regulated by a death factor and its receptor: Fas ligand and Fas. Philos Trans R Soc Lond B Biol Sci 345(1313):281\u2013287. https:\/\/doi.org\/10.1098\/rstb.1994.0107","journal-title":"Philos Trans R Soc Lond B Biol Sci"},{"issue":"49","key":"3487_CR72","doi-asserted-by":"publisher","first-page":"47861","DOI":"10.1074\/jbc.M208950200","volume":"277","author":"G Bompard","year":"2002","unstructured":"Bompard G, Puech C, Pr\u00e9bois C, Vignon F, Freiss G (2002) Protein-tyrosine phosphatase PTPL1\/FAP-1 triggers apoptosis in human breast cancer cells. J Biol Chem 277(49):47861\u201347869. https:\/\/doi.org\/10.1074\/jbc.M208950200","journal-title":"J Biol Chem"},{"issue":"Pt 15","key":"3487_CR73","doi-asserted-by":"publisher","first-page":"2735","DOI":"10.1242\/jcs.114.15.2735","volume":"114","author":"H Ungefroren","year":"2001","unstructured":"Ungefroren H et al (2001) FAP-1 in pancreatic cancer cells: functional and mechanistic studies on its inhibitory role in CD95-mediated apoptosis. J Cell Sci 114(Pt 15):2735\u20132746. https:\/\/doi.org\/10.1242\/jcs.114.15.2735","journal-title":"J Cell Sci"},{"issue":"3","key":"3487_CR74","doi-asserted-by":"publisher","first-page":"241","DOI":"10.1007\/s11060-004-7202-x","volume":"74","author":"ED Foehr","year":"2005","unstructured":"Foehr ED, Lorente G, Vincent V, Nikolich K, Urfer R (2005) FAS associated phosphatase (FAP-1) blocks apoptosis of astrocytomas through dephosphorylation of FAS. J Neurooncol 74(3):241\u2013248. https:\/\/doi.org\/10.1007\/s11060-004-7202-x","journal-title":"J Neurooncol"},{"issue":"2","key":"3487_CR75","doi-asserted-by":"publisher","first-page":"157","DOI":"10.1007\/s00401-009-0614-0","volume":"119","author":"AC Navis","year":"2010","unstructured":"Navis AC, van den Eijnden M, Schepens JTG, Hooft R, van Huijsduijnen P, Wesseling Hendriks WJAJ (2010) Protein tyrosine phosphatases in glioma biology. Acta Neuropathol 119(2):157\u2013175. https:\/\/doi.org\/10.1007\/s00401-009-0614-0","journal-title":"Acta Neuropathol"},{"issue":"10","key":"3487_CR76","doi-asserted-by":"publisher","first-page":"5481","DOI":"10.1038\/s41380-021-01249-0","volume":"26","author":"H Hampel","year":"2021","unstructured":"Hampel H et al (2021) The Amyloid-\u03b2 Pathway in Alzheimer\u2019s Disease. Mol Psychiatry 26(10):5481\u20135503. https:\/\/doi.org\/10.1038\/s41380-021-01249-0","journal-title":"Mol Psychiatry"},{"key":"3487_CR77","doi-asserted-by":"publisher","first-page":"343","DOI":"10.1016\/B978-0-12-396456-4.00012-2","volume":"106","author":"SP Braithwaite","year":"2012","unstructured":"Braithwaite SP, Stock JB, Lombroso PJ, Nairn AC (2012) Protein phosphatases and Alzheimer\u2019s disease. Prog Mol Biol Transl Sci 106:343\u2013379. https:\/\/doi.org\/10.1016\/B978-0-12-396456-4.00012-2","journal-title":"Prog Mol Biol Transl Sci"},{"issue":"1","key":"3487_CR78","doi-asserted-by":"publisher","first-page":"123","DOI":"10.3233\/JAD-2012-129031","volume":"33","author":"J-Z Wang","year":"2013","unstructured":"Wang J-Z, Xia Y-Y, Grundke-Iqbal I, Iqbal K (2013) Abnormal hyperphosphorylation of tau: sites, regulation, and molecular mechanism of neurofibrillary degeneration. J Alzheimers Dis 33(1):123\u2013139. https:\/\/doi.org\/10.3233\/JAD-2012-129031","journal-title":"J Alzheimers Dis"},{"issue":"4","key":"3487_CR79","doi-asserted-by":"publisher","first-page":"441","DOI":"10.1111\/jnc.14961","volume":"154","author":"T-Y Hou","year":"2020","unstructured":"Hou T-Y et al (2020) Correcting abnormalities in miR-124\/PTPN1 signaling rescues tau pathology in Alzheimer\u2019s disease. J Neurochem 154(4):441\u2013457. https:\/\/doi.org\/10.1111\/jnc.14961","journal-title":"J Neurochem"},{"issue":"11","key":"3487_CR80","doi-asserted-by":"publisher","first-page":"5919","DOI":"10.3390\/ijms22115919","volume":"22","author":"R Sanuki","year":"2021","unstructured":"Sanuki R, Yamamura T (2021) Tumor suppressive effects of miR-124 and its function in neuronal development. Int J Mol Sci 22(11):5919. https:\/\/doi.org\/10.3390\/ijms22115919","journal-title":"Int J Mol Sci"},{"issue":"5","key":"3487_CR81","doi-asserted-by":"publisher","first-page":"395","DOI":"10.1016\/j.biopsych.2017.07.023","volume":"83","author":"X Wang","year":"2018","unstructured":"Wang X et al (2018) A novel MicroRNA-124\/PTPN1 signal pathway mediates synaptic and memory deficits in Alzheimer\u2019s Disease. Biol Psychiatry 83(5):395\u2013405. https:\/\/doi.org\/10.1016\/j.biopsych.2017.07.023","journal-title":"Biol Psychiatry"},{"issue":"7","key":"3487_CR82","doi-asserted-by":"publisher","first-page":"4787","DOI":"10.1007\/s12035-015-9405-x","volume":"53","author":"T Kanno","year":"2016","unstructured":"Kanno T, Tsuchiya A, Tanaka A, Nishizaki T (2016) Combination of PKC\u03b5 activation and PTP1B inhibition effectively suppresses A\u03b2-Induced GSK-3\u03b2 activation and tau phosphorylation. Mol Neurobiol 53(7):4787\u20134797. https:\/\/doi.org\/10.1007\/s12035-015-9405-x","journal-title":"Mol Neurobiol"},{"key":"3487_CR83","doi-asserted-by":"publisher","first-page":"8187","DOI":"10.1038\/srep08187","volume":"5","author":"N Jin","year":"2015","unstructured":"Jin N et al (2015) Truncation and activation of GSK-3\u03b2 by calpain I: a molecular mechanism links to tau hyperphosphorylation in Alzheimer\u2019s disease. Sci Rep 5:8187. https:\/\/doi.org\/10.1038\/srep08187","journal-title":"Sci Rep"},{"issue":"7","key":"3487_CR84","doi-asserted-by":"publisher","first-page":"1581","DOI":"10.1523\/JNEUROSCI.2120-19.2019","volume":"40","author":"KM Ricke","year":"2020","unstructured":"Ricke KM et al (2020) Neuronal protein tyrosine phosphatase 1B hastens amyloid \u03b2-Associated Alzheimer\u2019s Disease in mice. J Neurosci 40(7):1581\u20131593. https:\/\/doi.org\/10.1523\/JNEUROSCI.2120-19.2019","journal-title":"J Neurosci"},{"key":"3487_CR85","doi-asserted-by":"publisher","first-page":"66","DOI":"10.1016\/j.exger.2018.02.005","volume":"104","author":"GK Kuga","year":"2018","unstructured":"Kuga GK et al (2018) Impaired insulin signaling and spatial learning in middle-aged rats: The role of PTP1B. Exp Gerontol 104:66\u201371. https:\/\/doi.org\/10.1016\/j.exger.2018.02.005","journal-title":"Exp Gerontol"},{"key":"3487_CR86","doi-asserted-by":"publisher","first-page":"6100","DOI":"10.1523\/JNEUROSCI.0852-20.2020","volume":"40","author":"J Ghalayini","year":"2020","unstructured":"Ghalayini J (2020) Exploring the therapeutic potential of protein tyrosine phosphatase 1B in hAPP-J20 mouse model of Alzheimer\u2019s Disease. J Neurosci 40:6100\u20136102. https:\/\/doi.org\/10.1523\/JNEUROSCI.0852-20.2020","journal-title":"J Neurosci"},{"issue":"37","key":"3487_CR87","doi-asserted-by":"publisher","first-page":"7714","DOI":"10.2174\/0929867328666210412123304","volume":"28","author":"X Liang","year":"2021","unstructured":"Liang X, Hou X, Fang H (2021) Structure, function and modulation of Striatal-enriched protein tyrosine phosphatase (STEP). Curr Med Chem 28(37):7714\u20137728. https:\/\/doi.org\/10.2174\/0929867328666210412123304","journal-title":"Curr Med Chem"},{"key":"3487_CR88","doi-asserted-by":"publisher","first-page":"372","DOI":"10.1016\/j.neubiorev.2020.10.020","volume":"120","author":"L Li","year":"2021","unstructured":"Li L, Liang J, Fu H (2021) An update on the association between traumatic brain injury and Alzheimer\u2019s disease: focus on tau pathology and synaptic dysfunction. Neurosci Biobehav Rev 120:372\u2013386. https:\/\/doi.org\/10.1016\/j.neubiorev.2020.10.020","journal-title":"Neurosci Biobehav Rev"},{"issue":"1","key":"3487_CR89","doi-asserted-by":"publisher","first-page":"11771","DOI":"10.1038\/s41598-017-12236-3","volume":"7","author":"Y Wang","year":"2017","unstructured":"Wang Y, Hall RA, Lee M, Kamgar-parsi A, Bi X, Baudry M (2017) The tyrosine phosphatase PTPN13\/FAP-1 links calpain-2, TBI and tau tyrosine phosphorylation. Sci Rep 7(1):11771. https:\/\/doi.org\/10.1038\/s41598-017-12236-3","journal-title":"Sci Rep"},{"key":"3487_CR90","doi-asserted-by":"publisher","first-page":"157","DOI":"10.3389\/fnagi.2018.00157","volume":"10","author":"JA Santiago","year":"2018","unstructured":"Santiago JA, Bottero V, Potashkin JA (2018) Evaluation of RNA blood biomarkers in the Parkinson\u2019s disease biomarkers program. Front Aging Neurosci 10:157. https:\/\/doi.org\/10.3389\/fnagi.2018.00157","journal-title":"Front Aging Neurosci"},{"key":"3487_CR91","doi-asserted-by":"publisher","unstructured":"Feng C-W, Chen N-F, Chan T-F, Chen W-F (2020) Therapeutic role of protein tyrosine phosphatase 1B in Parkinson\u2019s Disease via antineuroinflammation and neuroprotection in vitro and in vivo. Parkinson\u2019s Disease :1\u201315. https:\/\/doi.org\/10.1155\/2020\/8814236","DOI":"10.1155\/2020\/8814236"},{"issue":"1","key":"3487_CR92","doi-asserted-by":"publisher","first-page":"76","DOI":"10.1038\/s41431-019-0487-1","volume":"28","author":"R Bend","year":"2020","unstructured":"Bend R et al (2020) Phenotype and mutation expansion of the PTPN23 associated disorder characterized by neurodevelopmental delay and structural brain abnormalities. Eur J Hum Genet 28(1):76\u201387. https:\/\/doi.org\/10.1038\/s41431-019-0487-1","journal-title":"Eur J Hum Genet"},{"issue":"11\u201312","key":"3487_CR93","doi-asserted-by":"publisher","first-page":"1455","DOI":"10.1007\/s00439-017-1850-3","volume":"136","author":"N Sowada","year":"2017","unstructured":"Sowada N et al (2017) Mutations of PTPN23 in developmental and epileptic encephalopathy. Hum Genet 136(11\u201312):1455\u20131461. https:\/\/doi.org\/10.1007\/s00439-017-1850-3","journal-title":"Hum Genet"},{"key":"3487_CR94","doi-asserted-by":"publisher","unstructured":"Meer Gv, Voelker DR, Feigenson GW (2008) Membrane lipids: where they are and how they behave. Nat Rev Mol Cell Biol 9(2):112\u201324. https:\/\/doi.org\/10.1038\/nrm2330","DOI":"10.1038\/nrm2330"},{"issue":"4","key":"3487_CR95","doi-asserted-by":"publisher","first-page":"224","DOI":"10.1016\/j.tem.2021.01.006","volume":"32","author":"M Falabella","year":"2021","unstructured":"Falabella M, Vernon HJ, Hanna MG, Claypool SM, Pitceathly RDS (2021) Cardiolipin, Mitochondria, and neurological disease. Trends Endocrinol Metab 32(4):224\u2013237. https:\/\/doi.org\/10.1016\/j.tem.2021.01.006","journal-title":"Trends Endocrinol Metab"},{"issue":"4","key":"3487_CR96","doi-asserted-by":"publisher","first-page":"223","DOI":"10.1038\/nchembio727","volume":"1","author":"VE Kagan","year":"2005","unstructured":"Kagan VE et al (2005) Cytochrome c acts as a cardiolipin oxygenase required for release of proapoptotic factors. Nat Chem Biol 1(4):223\u2013232. https:\/\/doi.org\/10.1038\/nchembio727","journal-title":"Nat Chem Biol"},{"issue":"1","key":"3487_CR97","doi-asserted-by":"publisher","first-page":"57","DOI":"10.1016\/s0092-8674(00)81683-9","volume":"100","author":"D Hanahan","year":"2000","unstructured":"Hanahan D, Weinberg RA (2000) The hallmarks of cancer. Cell 100(1):57\u201370. https:\/\/doi.org\/10.1016\/s0092-8674(00)81683-9","journal-title":"Cell"},{"issue":"2","key":"3487_CR98","doi-asserted-by":"publisher","first-page":"197","DOI":"10.1016\/j.molcel.2005.06.008","volume":"19","author":"DJ Pagliarini","year":"2005","unstructured":"Pagliarini DJ et al (2005) Involvement of a mitochondrial phosphatase in the regulation of ATP production and insulin secretion in pancreatic beta cells. Mol Cell 19(2):197\u2013207. https:\/\/doi.org\/10.1016\/j.molcel.2005.06.008","journal-title":"Mol Cell"},{"issue":"1","key":"3487_CR99","doi-asserted-by":"publisher","first-page":"e53803","DOI":"10.1371\/journal.pone.0053803","volume":"8","author":"NM Niemi","year":"2013","unstructured":"Niemi NM, Lanning NJ, Westrate LM, MacKeigan JP (2013) Downregulation of the mitochondrial phosphatase PTPMT1 is sufficient to promote cancer cell death. PLoS ONE 8(1):e53803. https:\/\/doi.org\/10.1371\/journal.pone.0053803","journal-title":"PLoS ONE"},{"issue":"6","key":"3487_CR100","doi-asserted-by":"publisher","first-page":"690","DOI":"10.1016\/j.cmet.2011.04.007","volume":"13","author":"J Zhang","year":"2011","unstructured":"Zhang J et al (2011) Mitochondrial phosphatase PTPMT1 is essential for cardiolipin biosynthesis. Cell Metab 13(6):690\u2013700. https:\/\/doi.org\/10.1016\/j.cmet.2011.04.007","journal-title":"Cell Metab"}],"container-title":["Molecular Neurobiology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s12035-023-03487-5.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/article\/10.1007\/s12035-023-03487-5\/fulltext.html","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s12035-023-03487-5.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,9,27]],"date-time":"2023-09-27T01:30:08Z","timestamp":1695778208000},"score":1,"resource":{"primary":{"URL":"https:\/\/link.springer.com\/10.1007\/s12035-023-03487-5"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2023,7,17]]},"references-count":100,"journal-issue":{"issue":"11","published-print":{"date-parts":[[2023,11]]}},"alternative-id":["3487"],"URL":"https:\/\/doi.org\/10.1007\/s12035-023-03487-5","relation":{},"ISSN":["0893-7648","1559-1182"],"issn-type":[{"value":"0893-7648","type":"print"},{"value":"1559-1182","type":"electronic"}],"subject":[],"published":{"date-parts":[[2023,7,17]]},"assertion":[{"value":"27 March 2023","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"5 July 2023","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"17 July 2023","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Declarations"}},{"value":"Not applicable.","order":2,"name":"Ethics","group":{"name":"EthicsHeading","label":"Ethics Approval"}},{"value":"Not applicable \u2014 no research involving human subjects is included in this manuscript.","order":3,"name":"Ethics","group":{"name":"EthicsHeading","label":"Consent to Participate"}},{"value":"Not applicable.","order":4,"name":"Ethics","group":{"name":"EthicsHeading","label":"Consent for Publication"}},{"value":"Authors declare no conflict of interests.","order":5,"name":"Ethics","group":{"name":"EthicsHeading","label":"Competing Interests"}}]}}