{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,23]],"date-time":"2026-10-23T19:47:28Z","timestamp":1792784848697,"version":"4.5.0"},"reference-count":80,"publisher":"American Chemical Society (ACS)","issue":"41","license":[{"start":{"date-parts":[[2026,10,5]],"date-time":"2026-10-05T00:00:00Z","timestamp":1791158400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2026,10,5]],"date-time":"2026-10-05T00:00:00Z","timestamp":1791158400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2026,10,5]],"date-time":"2026-10-05T00:00:00Z","timestamp":1791158400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-045"}],"funder":[{"DOI":"10.13039\/501100004921","name":"Shanghai Jiao Tong University","doi-asserted-by":"publisher","award":["WH510363004\/013"],"award-info":[{"award-number":["WH510363004\/013"]}],"id":[{"id":"10.13039\/501100004921","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100010040","name":"Taishan Scholar Project of Shandong Province","doi-asserted-by":"publisher","award":["tsqn202306268"],"award-info":[{"award-number":["tsqn202306268"]}],"id":[{"id":"10.13039\/501100010040","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100019446","name":"Medical and Health Science and Technology Development Project of Shandong Province","doi-asserted-by":"publisher","award":["202513051332"],"award-info":[{"award-number":["202513051332"]}],"id":[{"id":"10.13039\/501100019446","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100007129","name":"Natural Science Foundation of Shandong Province","doi-asserted-by":"publisher","award":["ZR2025MS120"],"award-info":[{"award-number":["ZR2025MS120"]}],"id":[{"id":"10.13039\/501100007129","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Shanghai Key Laboratory for Antibody-Drug Conjugates with Innovative Target, Shanghai Jiao Tong University","award":["24dz2261300"],"award-info":[{"award-number":["24dz2261300"]}],"id":[{"id":"https:\/\/ror.org\/0220qvk04","id-type":"ROR","asserted-by":"crossref"}]},{"name":"Natural Science Foundation of Shanghai","award":["25ZR1402193"],"award-info":[{"award-number":["25ZR1402193"]}]},{"name":"National Natural Science Foundation of China (NSFC)","award":["22207065"],"award-info":[{"award-number":["22207065"]}],"id":[{"id":"https:\/\/ror.org\/01h0zpd94","id-type":"ROR","asserted-by":"crossref"}]},{"name":"National Natural Science Foundation of China (NSFC)","award":["32501108"],"award-info":[{"award-number":["32501108"]}],"id":[{"id":"https:\/\/ror.org\/01h0zpd94","id-type":"ROR","asserted-by":"crossref"}]},{"name":"Shanghai Frontiers Science Center of Drug Target Identification and Delivery, Shanghai Jiao Tong University","award":["ZXWH2170101"],"award-info":[{"award-number":["ZXWH2170101"]}],"id":[{"id":"https:\/\/ror.org\/0220qvk04","id-type":"ROR","asserted-by":"crossref"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2026,10,21]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Histone methyltransferase Dot1L is the sole non-SET-domain lysine methyltransferase that exclusively catalyzes nucleosomal histone H3 lysine 79 (H3K79) methylation, and its dysregulation is tightly associated with leukemogenesis and other human diseases. While the regulation of Dot1L activity by histone substrate modifications (e.g., H2BK120Ub, H2BK34Ub, and H4K16ac) has been well characterized biochemically and structurally, the regulatory mechanisms underlying intrinsic phosphorylation and acetylation within its catalytically essential lysine-rich region (LRR) remain poorly understood, largely limited by the lack of homogeneous Dot1L proteins with site-specific post-translational modifications (PTMs). Here, we develop a modular semisynthetic strategy combining peptide hydrazide ligation and Sortase A-mediated chemoenzymatic ligation to construct homogeneous Dot1L catalytic domain (1\u2013416) variants bearing site-specific PTM patterns: unmodified, penta-phosphorylated, penta-acetylated, and dual penta-phosphorylated\/penta-acetylated. By splitting Dot1L(1\u2013416) into a recombinant N-terminal fragment and a chemically synthesized C-terminal LRR fragment, we further optimize a hybrid microwave\/manual solid-phase peptide synthesis to overcome the \u03b2-elimination of phosphoserine and phosphothreonine residues, enabling efficient and precise preparation of multiphosphopeptides. Biochemical characterizations demonstrate that both phosphorylation and acetylation individually repress Dot1L-catalyzed nucleosomal H3K79 methylation, and dual modifications exert a synergistic inhibitory effect on its catalytic activity. Mechanistically, these intrinsic PTMs attenuate the binding affinity of Dot1L to nucleosomes, which directly accounts for the impaired catalytic activity. This work establishes a generalizable semi-synthetic platform for generating PTM-defined epigenetic enzymes and unveils the synergistic inhibitory regulation of Dot1L activity on nucleosomal H3K79 methylation by its intrinsic phosphorylation and acetylation.<\/jats:p>","DOI":"10.1021\/jacs.6c07839","type":"journal-article","created":{"date-parts":[[2026,10,5]],"date-time":"2026-10-05T07:02:19Z","timestamp":1791183739000},"page":"44057-44069","source":"Crossref","is-referenced-by-count":0,"title":["Semisynthesis of Multiphosphorylated\nand Acetylated\nHistone Methyltransferase Dot1L Reveals Synergistic Inhibition of\nNucleosomal H3K79 Methylation"],"prefix":"10.1021","volume":"148","author":[{"given":"Meixuan","family":"Xin","sequence":"first","affiliation":[{"name":"Shanghai Jiao Tong University , , ,","place":["Shanghai, China, 200240"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Longjie","family":"Yu","sequence":"additional","affiliation":[{"name":"Shandong First Medical University & Shandong Academy of Medical Sciences , , ,","place":["Jinan, China, 250117"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0002-8101-9047","authenticated-orcid":true,"given":"Xin","family":"Chen","sequence":"additional","affiliation":[{"name":"Shanghai Jiao Tong University , , ,","place":["Shanghai, China, 200240"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yun","family":"Liu","sequence":"additional","affiliation":[{"name":"Shanghai Jiao Tong University , , ,","place":["Shanghai, China, 200240"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Danyu","family":"Chen","sequence":"additional","affiliation":[{"name":"Shandong First Medical University & Shandong Academy of Medical Sciences , , ,","place":["Jinan, China, 250117"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Akejiang","family":"Adeerjiang","sequence":"additional","affiliation":[{"name":"Shanghai Jiao Tong University , , ,","place":["Shanghai, China, 200240"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Qi","family":"Shu","sequence":"additional","affiliation":[{"name":"Shanghai Jiao Tong University , , ,","place":["Shanghai, China, 200240"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0005-6856-2776","authenticated-orcid":true,"given":"Yulei","family":"Li","sequence":"additional","affiliation":[{"name":"Shandong First Medical University & Shandong Academy of Medical Sciences , , ,","place":["Jinan, China, 250117"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3378-5874","authenticated-orcid":true,"given":"Huasong","family":"Ai","sequence":"additional","affiliation":[{"name":"Shanghai Jiao Tong University , , ,","place":["Shanghai, China, 200240"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2026,10,5]]},"reference":[{"key":"2026102111064386300_cit1","doi-asserted-by":"publisher","first-page":"459","DOI":"10.1016\/j.cell.2009.02.027","article-title":"RAD6-Mediated\ntranscription-coupled H2B ubiquitylation directly stimulates H3K4\nmethylation in human cells","volume":"137","author":"Kim","year":"2009","journal-title":"Cell"},{"key":"2026102111064386300_cit2","doi-asserted-by":"publisher","first-page":"722","DOI":"10.1016\/j.molcel.2012.06.002","article-title":"Repair,\nRestore: The Active Role\nof Chromatin in the DNA Damage Response","volume":"46","author":"Soria","year":"2012","journal-title":"Mol.\nCell"},{"key":"2026102111064386300_cit3","doi-asserted-by":"publisher","first-page":"1052","DOI":"10.1016\/S0960-9822(02)00901-6","article-title":"Methylation of H3-lysine\n79 is mediated by a new family of HMTases without a SET domain","volume":"12","author":"Feng","year":"2002","journal-title":"Curr. Biol."},{"key":"2026102111064386300_cit4","doi-asserted-by":"publisher","first-page":"745","DOI":"10.1016\/S0092-8674(02)00759-6","article-title":"Dot1p modulates\nsilencing in yeast by methylation of the nucleosome core","volume":"109","author":"van Leeuwen","year":"2002","journal-title":"Cell"},{"key":"2026102111064386300_cit5","doi-asserted-by":"publisher","first-page":"711","DOI":"10.1016\/S0092-8674(03)00114-4","article-title":"Structure\nof the catalytic domain of human DOT1L, a non-SET domain nucleosomal\nhistone methyltransferase","volume":"112","author":"Min","year":"2003","journal-title":"Cell"},{"key":"2026102111064386300_cit6","doi-asserted-by":"publisher","first-page":"437","DOI":"10.1534\/genetics.109.101899","article-title":"The Dot1\nhistone methyltransferase and the Rad9 checkpoint adaptor contribute\nto cohesin-dependent double-strand break repair by sister chromatid\nrecombination in Saccharomyces cerevisiae","volume":"182","author":"Conde","year":"2009","journal-title":"Genetics"},{"key":"2026102111064386300_cit7","doi-asserted-by":"publisher","first-page":"2533","DOI":"10.1182\/blood-2012-11-465120","article-title":"Leukemic\ntransformation by the MLL-AF6 fusion\noncogene requires the H3K79 methyltransferase Dot1l","volume":"121","author":"Deshpande","year":"2013","journal-title":"Blood"},{"key":"2026102111064386300_cit8","doi-asserted-by":"publisher","first-page":"4483","DOI":"10.1182\/blood-2010-03-276501","article-title":"Early mammalian\nerythropoiesis requires the Dot1L methyltransferase","volume":"116","author":"Feng","year":"2010","journal-title":"Blood"},{"key":"2026102111064386300_cit9","doi-asserted-by":"publisher","first-page":"4759","DOI":"10.1182\/blood-2010-12-327668","article-title":"Requirement\nfor Dot1l in murine postnatal hematopoiesis and leukemogenesis by\nMLL translocation","volume":"117","author":"Jo","year":"2011","journal-title":"Blood"},{"key":"2026102111064386300_cit10","doi-asserted-by":"publisher","first-page":"6912","DOI":"10.1182\/blood-2011-02-334359","article-title":"DOT1L, the H3K79 methyltransferase,\nis required for MLL-AF9-mediated leukemogenesis","volume":"117","author":"Nguyen","year":"2011","journal-title":"Blood"},{"key":"2026102111064386300_cit11","doi-asserted-by":"publisher","first-page":"167","DOI":"10.1016\/j.cell.2005.02.020","article-title":"hDOT1L links\nhistone methylation to leukemogenesis","volume":"121","author":"Okada","year":"2005","journal-title":"Cell"},{"key":"2026102111064386300_cit12","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pgen.1003611","article-title":"Histone methyltransferase\nDOT1L drives\nrecovery of gene expression after a genotoxic attack","volume":"9","author":"Oksenych","year":"2013","journal-title":"PLoS Genet"},{"key":"2026102111064386300_cit13","doi-asserted-by":"publisher","first-page":"68","DOI":"10.1016\/j.gde.2016.03.015","article-title":"The role\nof DOT1L in the maintenance\nof leukemia gene expression","volume":"36","author":"Wang","year":"2016","journal-title":"Curr. Opin. Genet.\nDev."},{"key":"2026102111064386300_cit14","doi-asserted-by":"publisher","first-page":"8430","DOI":"10.1128\/MCB.25.19.8430-8443.2005","article-title":"Role of Dot1-dependent histone H3 methylation in G1\nand S phase DNA damage checkpoint functions of Rad9","volume":"25","author":"Wysocki","year":"2005","journal-title":"Mol. Cell. Biol."},{"key":"2026102111064386300_cit15","doi-asserted-by":"publisher","first-page":"1669","DOI":"10.1158\/1535-7163.MCT-16-0693","article-title":"Mechanisms\nof Pinometostat (EPZ-5676) Treatment-Emergent\nResistance in MLL-Rearranged Leukemia","volume":"16","author":"Campbell","year":"2017","journal-title":"Mol.\nCancer Ther."},{"key":"2026102111064386300_cit16","doi-asserted-by":"publisher","first-page":"812","DOI":"10.1038\/nature06906","article-title":"Chemically ubiquitylated\nhistone H2B stimulates hDot1L-mediated intranucleosomal methylation","volume":"453","author":"McGinty","year":"2008","journal-title":"Nature"},{"key":"2026102111064386300_cit17","doi-asserted-by":"publisher","first-page":"34655","DOI":"10.1074\/jbc.C200433200","article-title":"Ubiquitination of histone\nH2B by Rad6 is required for efficient Dot1-mediated methylation of\nhistone H3 lysine 79","volume":"277","author":"Ng","year":"2002","journal-title":"J. Biol. Chem."},{"key":"2026102111064386300_cit18","doi-asserted-by":"publisher","DOI":"10.1126\/science.abc6663","article-title":"Regulation of the\nDot1 histone H3K79 methyltransferase by histone H4K16 acetylation","volume":"371","author":"Valencia-Sa\u0301nchez","year":"2021","journal-title":"Science"},{"key":"2026102111064386300_cit19","doi-asserted-by":"publisher","first-page":"1010","DOI":"10.1016\/j.molcel.2019.03.029","article-title":"Structural Basis\nof Dot1L Stimulation by Histone H2B Lysine 120 Ubiquitination","volume":"74","author":"Valencia-Sa\u0301nchez","year":"2019","journal-title":"Mol. Cell"},{"key":"2026102111064386300_cit20","doi-asserted-by":"publisher","first-page":"1681","DOI":"10.1016\/j.celrep.2019.01.058","article-title":"Structural\nBasis for Recognition\nof Ubiquitylated Nucleosome by Dot1L Methyltransferase","volume":"26","author":"Anderson","year":"2019","journal-title":"Cell Rep."},{"key":"2026102111064386300_cit21","doi-asserted-by":"publisher","first-page":"330","DOI":"10.1038\/s41422-019-0146-7","article-title":"Structural basis of the crosstalk between histone H2B\nmonoubiquitination\nand H3 lysine 79 methylation on nucleosome","volume":"29","author":"Yao","year":"2019","journal-title":"Cell Res."},{"key":"2026102111064386300_cit22","doi-asserted-by":"publisher","first-page":"1490","DOI":"10.1016\/j.cell.2019.02.002","article-title":"Mechanism\nof Cross-talk between H2B Ubiquitination and H3Methylation by Dot1L","volume":"176","author":"Worden","year":"2019","journal-title":"Cell"},{"key":"2026102111064386300_cit23","doi-asserted-by":"publisher","first-page":"972","DOI":"10.1038\/s41589-022-01067-7","article-title":"H2B Lys34 Ubiquitination Induces Nucleosome\nDistortion to Stimulate\nDot1L Activity","volume":"18","author":"Ai","year":"2022","journal-title":"Nat. Chem. Biol."},{"key":"2026102111064386300_cit24","doi-asserted-by":"publisher","first-page":"245","DOI":"10.1038\/s41422-022-00773-0","article-title":"Fructose-1,6-bisphosphatase\n1 dephosphorylates I\u03baB\u03b1 and suppresses colorectal tumorigenesis","volume":"33","author":"Zhu","year":"2023","journal-title":"Cell Res."},{"key":"2026102111064386300_cit25","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.2315242121","article-title":"ALK signaling primes\nthe DNA damage response sensitizing ALK-driven neuroblastoma to therapeutic\nATR inhibition","volume":"121","author":"Borena\u0308s","year":"2024","journal-title":"Proc. Natl. Acad. Sci. U. S.\nA."},{"key":"2026102111064386300_cit26","doi-asserted-by":"publisher","first-page":"55","DOI":"10.1038\/nature18003","article-title":"Proteogenomics connects somatic mutations\nto\nsignalling in breast cancer","volume":"534","author":"Mertins","year":"2016","journal-title":"Nature"},{"key":"2026102111064386300_cit27","doi-asserted-by":"publisher","first-page":"1758","DOI":"10.7150\/thno.39013","article-title":"CBP mediated DOT1L acetylation confers DOT1L\nstability and promotes\ncancer metastasis","volume":"10","author":"Liu","year":"2020","journal-title":"Theranostics"},{"key":"2026102111064386300_cit28","doi-asserted-by":"publisher","first-page":"112885","DOI":"10.1016\/j.celrep.2023.112885","article-title":"Histone H3K79 methylation\nby DOT1L promotes Aurora B localization at centromeres in mitosis","volume":"42","author":"Yang","year":"2023","journal-title":"Cell Rep."},{"key":"2026102111064386300_cit29","doi-asserted-by":"publisher","first-page":"109739","DOI":"10.1016\/j.celrep.2021.109739","article-title":"DOT1L O-GlcNAcylation\npromotes its protein stability and MLL-fusion leukemia cell proliferation","volume":"36","author":"Song","year":"2021","journal-title":"Cell Rep."},{"key":"2026102111064386300_cit30","doi-asserted-by":"publisher","first-page":"1060","DOI":"10.1007\/s11426-024-1950-1","article-title":"Recent advances in chemical protein synthesis: method\ndevelopments and biological applications","volume":"67","author":"Dong","year":"2024","journal-title":"Sci.\nChina: Chem."},{"key":"2026102111064386300_cit31","doi-asserted-by":"publisher","first-page":"2515","DOI":"10.1007\/s11427-024-2860-5","article-title":"Advances in the chemical\nsynthesis of human proteoforms","volume":"68","author":"Yang","year":"2025","journal-title":"Sci. China Life\nSci."},{"key":"2026102111064386300_cit32","doi-asserted-by":"publisher","first-page":"1442","DOI":"10.1021\/acscentsci.4c00642","article-title":"Chemical Synthesis of Human Proteoforms and Application\nin Biomedicine","volume":"10","author":"Ai","year":"2024","journal-title":"ACS Cent. Sci."},{"key":"2026102111064386300_cit33","doi-asserted-by":"publisher","DOI":"10.1002\/anie.202111266","article-title":"Chemical\nSynthesis and Semisynthesis of Lipidated Proteins","volume":"61","author":"Hanna","year":"2022","journal-title":"Angew. Chem. Int. Ed."},{"key":"2026102111064386300_cit34","doi-asserted-by":"publisher","first-page":"2688","DOI":"10.1021\/acs.accounts.3c00388","article-title":"Exploiting\nChemical Protein Synthesis to Study the Role of Tyrosine Sulfation\non Anticoagulants from Hematophagous Organisms","volume":"56","author":"Maxwell","year":"2023","journal-title":"Acc. Chem. Res."},{"key":"2026102111064386300_cit35","doi-asserted-by":"publisher","first-page":"338","DOI":"10.1039\/B700141J","article-title":"Total chemical\nsynthesis of proteins","volume":"38","author":"Kent","year":"2009","journal-title":"Chem. Soc. Rev."},{"key":"2026102111064386300_cit36","doi-asserted-by":"publisher","first-page":"18","DOI":"10.1016\/j.cbpa.2018.02.001","article-title":"Chemical chromatin ubiquitylation","volume":"45","author":"Jbara","year":"2018","journal-title":"Curr. Opin.\nChem. Biol."},{"key":"2026102111064386300_cit37","doi-asserted-by":"publisher","first-page":"10025","DOI":"10.1039\/D3SC03664B","article-title":"Synthesis of ubiquitinated proteins for biochemical and functional\nanalysis","volume":"14","author":"Kriegesmann","year":"2023","journal-title":"Chem. Sci."},{"key":"2026102111064386300_cit38","doi-asserted-by":"publisher","first-page":"3051","DOI":"10.1021\/acs.chemrev.9b00450","article-title":"Chemoenzymatic Semisynthesis\nof Proteins","volume":"120","author":"Thompson","year":"2020","journal-title":"Chem. Rev."},{"key":"2026102111064386300_cit39","doi-asserted-by":"publisher","first-page":"1090","DOI":"10.1021\/jacs.9b12558","article-title":"Peptide Ligation\nat High Dilution\nvia Reductive Diselenide-Selenoester Ligation","volume":"142","author":"Chisholm","year":"2020","journal-title":"J. Am. Chem. Soc."},{"key":"2026102111064386300_cit40","doi-asserted-by":"publisher","DOI":"10.1002\/anie.202519647","article-title":"Semi-Synthesis of Immunogenic Mycobacterial\nLipoproteins via Aryl Selenoester-Mediated Expressed Protein Ligation","volume":"65","author":"Kambanis","year":"2026","journal-title":"Angew. Chem. Int. Ed."},{"key":"2026102111064386300_cit41","doi-asserted-by":"publisher","DOI":"10.1002\/anie.202200163","article-title":"Expressed Protein Selenoester Ligation","volume":"61","author":"Kulkarni","year":"2022","journal-title":"Angew.\nChem. Int. Ed."},{"key":"2026102111064386300_cit42","doi-asserted-by":"publisher","first-page":"5336","DOI":"10.1021\/jacs.1c02280","article-title":"Chemical Synthesis of Phosphorylated Insulin-like Growth\nFactor Binding Protein 2","volume":"143","author":"Premdjee","year":"2021","journal-title":"J. Am. Chem. Soc."},{"key":"2026102111064386300_cit43","doi-asserted-by":"publisher","first-page":"870","DOI":"10.1038\/s41467-021-21209-0","article-title":"General synthetic\nstrategy for regioselective ultrafast formation of disulfide bonds\nin peptides and proteins","volume":"12","author":"Laps","year":"2021","journal-title":"Nat. Commun."},{"key":"2026102111064386300_cit44","doi-asserted-by":"publisher","first-page":"12374","DOI":"10.1002\/anie.201503309","article-title":"Convergent\nversus sequential\nprotein synthesis: the case of ubiquitinated and glycosylated H2B","volume":"54","author":"Seenaiah","year":"2015","journal-title":"Angew. Chem. Int. Ed."},{"key":"2026102111064386300_cit45","doi-asserted-by":"publisher","first-page":"8059","DOI":"10.1002\/anie.201303844","article-title":"Convergent\nchemical synthesis of histone H2B protein for the site-specific ubiquitination\nat Lys34","volume":"52","author":"Siman","year":"2013","journal-title":"Angew. Chem. Int. Ed."},{"key":"2026102111064386300_cit46","doi-asserted-by":"publisher","first-page":"3154","DOI":"10.1038\/s41467-018-05628-0","article-title":"Palladium prompted on-demand cysteine\nchemistry for the synthesis of challenging and uniquely modified proteins","volume":"9","author":"Jbara","year":"2018","journal-title":"Nat. Commun."},{"key":"2026102111064386300_cit47","doi-asserted-by":"publisher","first-page":"4972","DOI":"10.1002\/anie.201600638","article-title":"Chemical Synthesis of Phosphorylated\nHistone H2A at Tyr57 Reveals\nInsight into the Inhibition Mode of the SAGA Deubiquitinating Module","volume":"55","author":"Jbara","year":"2016","journal-title":"Angew. Chem. Int. Ed."},{"key":"2026102111064386300_cit48","doi-asserted-by":"publisher","first-page":"25788","DOI":"10.1021\/jacs.4c08416","article-title":"A Versatile Method for Site-Specific\nChemical Installation of Aromatic Posttranslational Modification Analogs\ninto Proteins","volume":"146","author":"Lin","year":"2024","journal-title":"J. Am. Chem. 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