{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,24]],"date-time":"2026-07-24T14:44:42Z","timestamp":1784904282514,"version":"3.55.0"},"reference-count":283,"publisher":"Oxford University Press (OUP)","issue":"1","license":[{"start":{"date-parts":[[2024,2,28]],"date-time":"2024-02-28T00:00:00Z","timestamp":1709078400000},"content-version":"vor","delay-in-days":27,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2024,5,9]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:p>Lysine post-translational modifications (PTMs) are widespread and versatile protein PTMs that are involved in diverse biological processes by regulating the fundamental functions of histone and non-histone proteins. Dysregulation of lysine PTMs is implicated in many diseases, and targeting lysine PTM regulatory factors, including writers, erasers, and readers, has become an effective strategy for disease therapy. The continuing development of mass spectrometry (MS) technologies coupled with antibody-based affinity enrichment technologies greatly promotes the discovery and decoding of PTMs. The global characterization of lysine PTMs is crucial for deciphering the regulatory networks, molecular functions, and mechanisms of action of lysine PTMs. In this review, we focus on lysine PTMs, and provide a summary of the regulatory enzymes of diverse lysine PTMs and the proteomics advances in lysine PTMs by MS technologies. We also discuss the types and biological functions of lysine PTM crosstalks on histone and non-histone proteins and current druggable targets of lysine PTM regulatory factors for disease therapy.<\/jats:p>","DOI":"10.1093\/gpbjnl\/qzae019","type":"journal-article","created":{"date-parts":[[2024,2,29]],"date-time":"2024-02-29T06:46:13Z","timestamp":1709189173000},"source":"Crossref","is-referenced-by-count":31,"title":["Substrate and Functional Diversity of Protein Lysine Post-translational Modifications"],"prefix":"10.1093","volume":"22","author":[{"ORCID":"https:\/\/orcid.org\/0009-0006-8860-5582","authenticated-orcid":false,"given":"Bingbing","family":"Hao","sequence":"first","affiliation":[{"name":"State Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences , Shanghai 201203,","place":["China"]},{"name":"University of Chinese Academy of Sciences , Beijing 100049,","place":["China"]},{"name":"Tianjian Laboratory of Advanced Biomedical Sciences, Institute of Advanced Biomedical Sciences, Zhengzhou University , Zhengzhou 450001,","place":["China"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0008-0602-2987","authenticated-orcid":false,"given":"Kaifeng","family":"Chen","sequence":"additional","affiliation":[{"name":"State Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences , Shanghai 201203,","place":["China"]},{"name":"University of Chinese Academy of Sciences , Beijing 100049,","place":["China"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1576-4137","authenticated-orcid":false,"given":"Linhui","family":"Zhai","sequence":"additional","affiliation":[{"name":"State Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences , Shanghai 201203,","place":["China"]},{"name":"Zhongshan Institute for Drug Discovery, Shanghai Institute of Materia Medica, Chinese Academy of Sciences , Zhongshan 528400,","place":["China"]},{"name":"State Key Laboratory of Pharmaceutical Biotechnology, Nanjing University , Nanjing 210023,","place":["China"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Muyin","family":"Liu","sequence":"additional","affiliation":[{"name":"Department of Cardiology, Shanghai Institute of Cardiovascular Diseases, Zhongshan Hospital, Fudan University , Shanghai 200032,","place":["China"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1569-2604","authenticated-orcid":false,"given":"Bin","family":"Liu","sequence":"additional","affiliation":[{"name":"Jiangsu Key Laboratory of Marine Pharmaceutical Compound Screening, College of Pharmacy, Jiangsu Ocean University , Lianyungang 222005,","place":["China"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6784-9653","authenticated-orcid":false,"given":"Minjia","family":"Tan","sequence":"additional","affiliation":[{"name":"State Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences , Shanghai 201203,","place":["China"]},{"name":"University of Chinese Academy of Sciences , Beijing 100049,","place":["China"]},{"name":"Zhongshan Institute for Drug Discovery, Shanghai Institute of Materia Medica, Chinese Academy of Sciences , Zhongshan 528400,","place":["China"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2024,2,28]]},"reference":[{"key":"2024092609311935700_qzae019-B1","doi-asserted-by":"crossref","first-page":"536","DOI":"10.1038\/nrm3841","article-title":"The growing landscape of lysine acetylation links metabolism and cell signalling","volume":"15","author":"Choudhary","year":"2014","journal-title":"Nat Rev Mol Cell Biol"},{"key":"2024092609311935700_qzae019-B2","doi-asserted-by":"crossref","first-page":"90","DOI":"10.1038\/nrm.2016.140","article-title":"Metabolic regulation of gene expression through histone acylations","volume":"18","author":"Sabari","year":"2017","journal-title":"Nat Rev Mol Cell Biol"},{"key":"2024092609311935700_qzae019-B3","doi-asserted-by":"crossref","first-page":"329","DOI":"10.1038\/s41580-021-00441-y","article-title":"Modulation of cellular processes by histone and non-histone protein acetylation","volume":"23","author":"Shvedunova","year":"2022","journal-title":"Nat Rev Mol Cell Biol"},{"key":"2024092609311935700_qzae019-B4","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1038\/s41576-021-00416-x","article-title":"Interplay between chromatin marks in development and disease","volume":"23","author":"Janssen","year":"2022","journal-title":"Nat Rev Genet"},{"key":"2024092609311935700_qzae019-B5","doi-asserted-by":"crossref","first-page":"110","DOI":"10.1038\/nrc3884","article-title":"Critical roles of non-histone protein lysine methylation in human tumorigenesis","volume":"15","author":"Hamamoto","year":"2015","journal-title":"Nat Rev Cancer"},{"key":"2024092609311935700_qzae019-B6","doi-asserted-by":"crossref","first-page":"24","DOI":"10.1158\/2159-8290.CD-17-0605","article-title":"BET proteins as targets for anticancer treatment","volume":"8","author":"Stathis","year":"2018","journal-title":"Cancer Discov"},{"key":"2024092609311935700_qzae019-B7","doi-asserted-by":"crossref","first-page":"6213","DOI":"10.3390\/ijms22126213","article-title":"Small-molecule inhibitors targeting proteasome-associated deubiquitinases","volume":"22","author":"Moon","year":"2021","journal-title":"Int J Mol Sci"},{"key":"2024092609311935700_qzae019-B8","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1038\/nrd.2017.152","article-title":"Deubiquitylating enzymes and drug discovery: emerging opportunities","volume":"17","author":"Harrigan","year":"2018","journal-title":"Nat Rev Drug Discov"},{"key":"2024092609311935700_qzae019-B9","doi-asserted-by":"crossref","first-page":"917","DOI":"10.1038\/nrd4154","article-title":"Histone lysine demethylases as targets for anticancer therapy","volume":"12","author":"Hojfeldt","year":"2013","journal-title":"Nat Rev Drug Discov"},{"key":"2024092609311935700_qzae019-B10","doi-asserted-by":"crossref","first-page":"673","DOI":"10.1038\/nrd4360","article-title":"Histone deacetylases and their inhibitors in cancer, neurological diseases and immune disorders","volume":"13","author":"Falkenberg","year":"2014","journal-title":"Nat Rev Drug Discov"},{"key":"2024092609311935700_qzae019-B11","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1038\/d41573-021-00052-4","article-title":"Targeted protein degraders crowd into the clinic","volume":"20","author":"Mullard","year":"2021","journal-title":"Nat Rev Drug Discov"},{"key":"2024092609311935700_qzae019-B12","doi-asserted-by":"crossref","first-page":"100129","DOI":"10.1016\/j.mcpro.2021.100129","article-title":"Decoding post-translational modification crosstalk with proteomics","volume":"20","author":"Leutert","year":"2021","journal-title":"Mol Cell Proteomics"},{"key":"2024092609311935700_qzae019-B13","doi-asserted-by":"crossref","first-page":"943","DOI":"10.1016\/j.tibs.2019.06.003","article-title":"Analysis and interpretation of protein post-translational modification site stoichiometry","volume":"44","author":"Prus","year":"2019","journal-title":"Trends Biochem Sci"},{"key":"2024092609311935700_qzae019-B14","doi-asserted-by":"crossref","first-page":"D531","DOI":"10.1093\/nar\/gkt1093","article-title":"CPLM: a database of protein lysine modifications","volume":"42","author":"Liu","year":"2014","journal-title":"Nucleic Acids Res"},{"key":"2024092609311935700_qzae019-B15","doi-asserted-by":"crossref","first-page":"3112","DOI":"10.1038\/s41401-022-01017-y","article-title":"Proteomic characterization of post-translational modifications in drug discovery","volume":"43","author":"Zhai","year":"2022","journal-title":"Acta Pharmacol Sin"},{"key":"2024092609311935700_qzae019-B16","doi-asserted-by":"crossref","first-page":"517","DOI":"10.1038\/nrm.2017.35","article-title":"The winding path of protein methylation research: milestones and new frontiers","volume":"18","author":"Murn","year":"2017","journal-title":"Nat Rev Mol Cell Biol"},{"key":"2024092609311935700_qzae019-B17","doi-asserted-by":"crossref","first-page":"e324","DOI":"10.1038\/emm.2017.11","article-title":"Writing, erasing and reading histone lysine methylations","volume":"49","author":"Hyun","year":"2017","journal-title":"Exp Mol Med"},{"key":"2024092609311935700_qzae019-B18","doi-asserted-by":"crossref","first-page":"1092","DOI":"10.1016\/j.molcel.2019.08.026","article-title":"Lysine methylation regulators moonlighting outside the epigenome","volume":"75","author":"Cornett","year":"2019","journal-title":"Mol Cell"},{"key":"2024092609311935700_qzae019-B19","doi-asserted-by":"crossref","first-page":"547","DOI":"10.1016\/j.tig.2020.12.006","article-title":"Polycomb gene silencing mechanisms: PRC2 chromatin targeting, H3K27me3 \u201creadout\u201d, and phase separation-based compaction","volume":"37","author":"Guo","year":"2021","journal-title":"Trends Genet"},{"key":"2024092609311935700_qzae019-B20","doi-asserted-by":"crossref","first-page":"e1500737","DOI":"10.1126\/sciadv.1500737","article-title":"Regulation of gene transcription by polycomb proteins","volume":"1","author":"Aranda","year":"2015","journal-title":"Sci Adv"},{"key":"2024092609311935700_qzae019-B21","doi-asserted-by":"crossref","first-page":"11614","DOI":"10.1073\/pnas.1918776117","article-title":"Evolutionarily ancient BAH\u2013PHD protein mediates polycomb silencing","volume":"117","author":"Wiles","year":"2020","journal-title":"Proc Natl Acad Sci U S A"},{"key":"2024092609311935700_qzae019-B22","doi-asserted-by":"crossref","first-page":"6212","DOI":"10.1038\/s41467-020-20089-0","article-title":"Coupling of H3K27me3 recognition with transcriptional repression through the BAH\u2013PHD\u2013CPL2 complex in Arabidopsis","volume":"11","author":"Zhang","year":"2020","journal-title":"Nat Commun"},{"key":"2024092609311935700_qzae019-B23","doi-asserted-by":"crossref","first-page":"1384","DOI":"10.1038\/s41588-020-00729-3","article-title":"BAHCC1 binds H3K27me3 via a conserved BAH module to mediate gene silencing and oncogenesis","volume":"52","author":"Fan","year":"2020","journal-title":"Nat Genet"},{"key":"2024092609311935700_qzae019-B24","doi-asserted-by":"crossref","first-page":"566","DOI":"10.1016\/j.tig.2020.12.005","article-title":"Histone ubiquitination: an integrative signaling platform in genome stability","volume":"37","author":"Mattiroli","year":"2021","journal-title":"Trends Genet"},{"key":"2024092609311935700_qzae019-B25","doi-asserted-by":"crossref","first-page":"2404","DOI":"10.3390\/cells11152404","article-title":"Histone mono-ubiquitination in transcriptional regulation and its mark on life: emerging roles in tissue development and disease","volume":"11","author":"Oss-Ronen","year":"2022","journal-title":"Cells"},{"key":"2024092609311935700_qzae019-B26","doi-asserted-by":"crossref","first-page":"1699","DOI":"10.3390\/cells9071699","article-title":"Regulation of histone ubiquitination in response to DNA double strand breaks","volume":"9","author":"Aquila","year":"2020","journal-title":"Cells"},{"key":"2024092609311935700_qzae019-B27","doi-asserted-by":"crossref","first-page":"268","DOI":"10.1038\/s41594-020-00556-4","article-title":"BRCA1\/BARD1 site-specific ubiquitylation of nucleosomal H2A is directed by BARD1","volume":"28","author":"Witus","year":"2021","journal-title":"Nat Struct Mol Biol"},{"key":"2024092609311935700_qzae019-B28","doi-asserted-by":"crossref","first-page":"433","DOI":"10.1038\/s41586-021-03776-w","article-title":"BARD1 reads H2A lysine 15 ubiquitination to direct homologous recombination","volume":"596","author":"Becker","year":"2021","journal-title":"Nature"},{"key":"2024092609311935700_qzae019-B29","doi-asserted-by":"crossref","first-page":"5016","DOI":"10.1038\/s41467-021-25346-4","article-title":"RNF168-mediated localization of BARD1 recruits the BRCA1\u2013PALB2 complex to DNA damage","volume":"12","author":"Krais","year":"2021","journal-title":"Nat Commun"},{"key":"2024092609311935700_qzae019-B30","doi-asserted-by":"crossref","first-page":"840","DOI":"10.1016\/j.molcel.2019.11.021","article-title":"Histone H2AK119 mono-ubiquitination is essential for polycomb-mediated transcriptional repression","volume":"77","author":"Tamburri","year":"2020","journal-title":"Mol Cell"},{"key":"2024092609311935700_qzae019-B31","doi-asserted-by":"crossref","first-page":"eabc3393","DOI":"10.1126\/science.abc3393","article-title":"JARID2 and AEBP2 regulate PRC2 in the presence of H2AK119ub1 and other histone modifications","volume":"371","author":"Kasinath","year":"2021","journal-title":"Science"},{"key":"2024092609311935700_qzae019-B32","doi-asserted-by":"crossref","first-page":"439","DOI":"10.1038\/s41556-020-0484-1","article-title":"RYBP\/YAF2\u2013PRC1 complexes and histone H1-dependent chromatin compaction mediate propagation of H2AK119ub1 during cell division","volume":"22","author":"Zhao","year":"2020","journal-title":"Nat Cell Biol"},{"key":"2024092609311935700_qzae019-B33","doi-asserted-by":"crossref","first-page":"625","DOI":"10.1038\/s41588-022-01063-6","article-title":"The disordered N-terminal domain of DNMT3A recognizes H2AK119ub and is required for postnatal development","volume":"54","author":"Gu","year":"2022","journal-title":"Nat Genet"},{"key":"2024092609311935700_qzae019-B34","doi-asserted-by":"crossref","first-page":"537","DOI":"10.1038\/s41588-022-01073-4","article-title":"DNMT3A binds ubiquitinated histones to regulate bivalent genes","volume":"54","author":"Parry","year":"2022","journal-title":"Nat Genet"},{"key":"2024092609311935700_qzae019-B35","doi-asserted-by":"crossref","first-page":"1490","DOI":"10.1016\/j.cell.2019.02.002","article-title":"Mechanism of cross-talk between H2B ubiquitination and H3 methylation by Dot1L","volume":"176","author":"Worden","year":"2019","journal-title":"Cell"},{"key":"2024092609311935700_qzae019-B36","doi-asserted-by":"crossref","first-page":"1176","DOI":"10.1016\/j.biopsych.2020.12.029","article-title":"Ubiquitination of histone H2B by proteasome subunit RPT6 controls histone methylation chromatin dynamics during memory formation","volume":"89","author":"Jarome","year":"2021","journal-title":"Biol Psychiatry"},{"key":"2024092609311935700_qzae019-B37","doi-asserted-by":"crossref","first-page":"2002680","DOI":"10.1002\/advs.202002680","article-title":"USP38 couples histone ubiquitination and methylation via KDM5B to resolve inflammation","volume":"7","author":"Zhao","year":"2020","journal-title":"Adv Sci"},{"key":"2024092609311935700_qzae019-B38","doi-asserted-by":"crossref","first-page":"258","DOI":"10.1042\/bj0870258","article-title":"The presence of acetyl groups in histones","volume":"87","author":"Phillips","year":"1963","journal-title":"Biochem J"},{"key":"2024092609311935700_qzae019-B39","doi-asserted-by":"crossref","first-page":"786","DOI":"10.1073\/pnas.51.5.786","article-title":"Acetylation and methylation of histones and their possible role in the regulation of RNA synthesis","volume":"51","author":"Allfrey","year":"1964","journal-title":"Proc Natl Acad Sci U S A"},{"key":"2024092609311935700_qzae019-B40","doi-asserted-by":"crossref","first-page":"32288","DOI":"10.1074\/jbc.M109.045856","article-title":"Identification and characterization of propionylation at histone H3 lysine 23 in mammalian cells","volume":"284","author":"Liu","year":"2009","journal-title":"J Biol Chem"},{"key":"2024092609311935700_qzae019-B41","doi-asserted-by":"crossref","first-page":"812","DOI":"10.1074\/mcp.M700021-MCP200","article-title":"Lysine propionylation and butyrylation are novel post-translational modifications in histones","volume":"6","author":"Chen","year":"2007","journal-title":"Mol Cell Proteomics"},{"key":"2024092609311935700_qzae019-B42","doi-asserted-by":"crossref","first-page":"1016","DOI":"10.1016\/j.cell.2011.08.008","article-title":"Identification of 67 histone marks and histone lysine crotonylation as a new type of histone modification","volume":"146","author":"Tan","year":"2011","journal-title":"Cell"},{"key":"2024092609311935700_qzae019-B43","doi-asserted-by":"crossref","first-page":"122","DOI":"10.1038\/s41421-021-00344-4","article-title":"Histone lysine methacrylation is a dynamic post-translational modification regulated by HAT1 and SIRT2","volume":"7","author":"Delaney","year":"2021","journal-title":"Cell Discov"},{"key":"2024092609311935700_qzae019-B44","doi-asserted-by":"crossref","first-page":"177","DOI":"10.1093\/nar\/gkaa1176","article-title":"Identification of lysine isobutyrylation as a new histone modification mark","volume":"49","author":"Zhu","year":"2021","journal-title":"Nucleic Acids Res"},{"key":"2024092609311935700_qzae019-B45","doi-asserted-by":"crossref","first-page":"3374","DOI":"10.1038\/s41467-018-05567-w","article-title":"Lysine benzoylation is a histone mark regulated by SIRT2","volume":"9","author":"Huang","year":"2018","journal-title":"Nat Commun"},{"key":"2024092609311935700_qzae019-B46","doi-asserted-by":"crossref","first-page":"5548","DOI":"10.1038\/s41467-021-25867-y","article-title":"Isonicotinylation is a histone mark induced by the anti-tuberculosis first-line drug isoniazid","volume":"12","author":"Jiang","year":"2021","journal-title":"Nat Commun"},{"key":"2024092609311935700_qzae019-B47","doi-asserted-by":"crossref","first-page":"30239","DOI":"10.1074\/jbc.M704409200","article-title":"N-lysine propionylation controls the activity of propionyl-CoA synthetase","volume":"282","author":"Garrity","year":"2007","journal-title":"J Biol Chem"},{"key":"2024092609311935700_qzae019-B48","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1074\/mcp.M800224-MCP200","article-title":"Molecular characterization of propionyllysines in non-histone proteins","volume":"8","author":"Cheng","year":"2009","journal-title":"Mol Cell Proteomics"},{"key":"2024092609311935700_qzae019-B49","doi-asserted-by":"crossref","first-page":"3410","DOI":"10.1074\/jbc.RA117.000529","article-title":"Revealing the protein propionylation activity of the histone acetyltransferase MOF (males absent on the first)","volume":"293","author":"Han","year":"2018","journal-title":"J Biol Chem"},{"key":"2024092609311935700_qzae019-B50","doi-asserted-by":"crossref","first-page":"eaax0021","DOI":"10.1126\/sciadv.aax0021","article-title":"Deficient histone H3 propionylation by BRPF1\u2013KAT6 complexes in neurodevelopmental disorders and cancer","volume":"6","author":"Yan","year":"2020","journal-title":"Sci Adv"},{"key":"2024092609311935700_qzae019-B51","doi-asserted-by":"crossref","first-page":"900","DOI":"10.1021\/pr8005155","article-title":"Identification and verification of lysine propionylation and butyrylation in yeast core histones using PTMap software","volume":"8","author":"Zhang","year":"2009","journal-title":"J Proteome Res"},{"key":"2024092609311935700_qzae019-B52","doi-asserted-by":"crossref","first-page":"3903","DOI":"10.1021\/acs.biochem.8b00306","article-title":"An NAD+-dependent sirtuin depropionylase and deacetylase (Sir2La) from the probiotic bacterium Lactobacillus acidophilus NCFM","volume":"57","author":"Olesen","year":"2018","journal-title":"Biochemistry"},{"key":"2024092609311935700_qzae019-B53","doi-asserted-by":"crossref","first-page":"6768","DOI":"10.1002\/anie.201002724","article-title":"Interaction of propionylated and butyrylated histone H3 lysine marks with Brd4 bromodomains","volume":"49","author":"Vollmuth","year":"2010","journal-title":"Angew Chem Int Ed Engl"},{"key":"2024092609311935700_qzae019-B54","doi-asserted-by":"crossref","first-page":"650","DOI":"10.1016\/j.str.2017.02.003","article-title":"Recognition of histone H3K14 acylation by MORF","volume":"25","author":"Klein","year":"2017","journal-title":"Structure"},{"key":"2024092609311935700_qzae019-B55","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1016\/j.molcel.2016.03.014","article-title":"Dynamic competing histone H4 K5K8 acetylation and butyrylation are hallmarks of highly active gene promoters","volume":"62","author":"Goudarzi","year":"2016","journal-title":"Mol Cell"},{"key":"2024092609311935700_qzae019-B56","doi-asserted-by":"crossref","first-page":"1801","DOI":"10.1016\/j.str.2015.08.004","article-title":"A subset of human bromodomains recognizes butyryllysine and crotonyllysine histone peptide modifications","volume":"23","author":"Flynn","year":"2015","journal-title":"Structure"},{"key":"2024092609311935700_qzae019-B57","doi-asserted-by":"crossref","first-page":"5632342","DOI":"10.1155\/2020\/5632342","article-title":"p300-catalyzed lysine crotonylation promotes the proliferation, invasion, and migration of HeLa cells via heterogeneous nuclear ribonucleoprotein A1","volume":"2020","author":"Han","year":"2020","journal-title":"Anal Cell Pathol"},{"key":"2024092609311935700_qzae019-B58","doi-asserted-by":"crossref","first-page":"20122","DOI":"10.1074\/jbc.RA119.010302","article-title":"Gcn5 and Esa1 function as histone crotonyltransferases to regulate crotonylation-dependent transcription","volume":"294","author":"Kollenstart","year":"2019","journal-title":"J Biol Chem"},{"key":"2024092609311935700_qzae019-B59","doi-asserted-by":"crossref","first-page":"17016","DOI":"10.1038\/celldisc.2017.16","article-title":"MOF as an evolutionarily conserved histone crotonyltransferase and transcriptional activation by histone acetyltransferase-deficient and crotonyltransferase-competent CBP\/p300","volume":"3","author":"Liu","year":"2017","journal-title":"Cell Discov"},{"key":"2024092609311935700_qzae019-B60","doi-asserted-by":"crossref","first-page":"e02999","DOI":"10.7554\/eLife.02999","article-title":"Identification of \u201cerasers\u201d for lysine crotonylated histone marks using a chemical proteomics approach","volume":"3","author":"Bao","year":"2014","journal-title":"Elife"},{"key":"2024092609311935700_qzae019-B61","doi-asserted-by":"crossref","first-page":"14690","DOI":"10.1038\/s41598-018-32927-9","article-title":"Histone deacetylase (HDAC) 1 and 2 complexes regulate both histone acetylation and crotonylation in vivo","volume":"8","author":"Kelly","year":"2018","journal-title":"Sci Rep"},{"key":"2024092609311935700_qzae019-B62","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1038\/s41467-017-02651-5","article-title":"Microbiota derived short chain fatty acids promote histone crotonylation in the colon through histone deacetylases","volume":"9","author":"Fellows","year":"2018","journal-title":"Nat Commun"},{"key":"2024092609311935700_qzae019-B63","doi-asserted-by":"crossref","first-page":"898","DOI":"10.1038\/cr.2017.68","article-title":"Class I histone deacetylases are major histone decrotonylases: evidence for critical and broad function of histone crotonylation in transcription","volume":"27","author":"Wei","year":"2017","journal-title":"Cell Res"},{"key":"2024092609311935700_qzae019-B64","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1016\/j.molcel.2016.03.028","article-title":"Molecular coupling of histone crotonylation and active transcription by AF9 YEATS domain","volume":"62","author":"Li","year":"2016","journal-title":"Mol Cell"},{"key":"2024092609311935700_qzae019-B65","doi-asserted-by":"crossref","first-page":"909","DOI":"10.1016\/j.molcel.2019.09.029","article-title":"Recognition of histone crotonylation by Taf14 links metabolic state to gene expression","volume":"76","author":"Gowans","year":"2019","journal-title":"Mol Cell"},{"key":"2024092609311935700_qzae019-B66","doi-asserted-by":"crossref","first-page":"1111","DOI":"10.1038\/nchembio.2218","article-title":"Selective recognition of histone crotonylation by double PHD fingers of MOZ and DPF2","volume":"12","author":"Xiong","year":"2016","journal-title":"Nat Chem Biol"},{"key":"2024092609311935700_qzae019-B67","doi-asserted-by":"crossref","first-page":"1369","DOI":"10.1038\/s41467-022-29057-2","article-title":"Global profiling of regulatory elements in the histone benzoylation pathway","volume":"13","author":"Wang","year":"2022","journal-title":"Nat Commun"},{"key":"2024092609311935700_qzae019-B68","doi-asserted-by":"crossref","first-page":"114","DOI":"10.1093\/nar\/gkaa1130","article-title":"Histone benzoylation serves as an epigenetic mark for DPF and YEATS family proteins","volume":"49","author":"Ren","year":"2021","journal-title":"Nucleic Acids Res"},{"key":"2024092609311935700_qzae019-B69","doi-asserted-by":"crossref","first-page":"365","DOI":"10.1038\/nchembio.1497","article-title":"Lysine 2-hydroxyisobutyrylation is a widely distributed active histone mark","volume":"10","author":"Dai","year":"2014","journal-title":"Nat Chem Biol"},{"key":"2024092609311935700_qzae019-B70","doi-asserted-by":"crossref","first-page":"194","DOI":"10.1016\/j.molcel.2016.03.036","article-title":"Metabolic regulation of gene expression by histone lysine \u03b2-hydroxybutyrylation","volume":"62","author":"Xie","year":"2016","journal-title":"Mol Cell"},{"key":"2024092609311935700_qzae019-B71","doi-asserted-by":"crossref","first-page":"575","DOI":"10.1038\/s41586-019-1678-1","article-title":"Metabolic regulation of gene expression by histone lactylation","volume":"574","author":"Zhang","year":"2019","journal-title":"Nature"},{"key":"2024092609311935700_qzae019-B72","doi-asserted-by":"crossref","first-page":"663","DOI":"10.1016\/j.molcel.2018.04.011","article-title":"p300-mediated lysine 2-hydroxyisobutyrylation regulates glycolysis","volume":"70","author":"Huang","year":"2018","journal-title":"Mol Cell"},{"key":"2024092609311935700_qzae019-B73","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1038\/cr.2017.149","article-title":"Landscape of the regulatory elements for lysine 2-hydroxyisobutyrylation pathway","volume":"28","author":"Huang","year":"2018","journal-title":"Cell Res"},{"key":"2024092609311935700_qzae019-B74","first-page":"4571319","article-title":"Quantitative proteomics reveals the role of lysine 2-hydroxyisobutyrylation pathway mediated by Tip60","volume":"2022","author":"Wang","year":"2022","journal-title":"Oxid Med Cell Longev"},{"key":"2024092609311935700_qzae019-B75","doi-asserted-by":"crossref","first-page":"eabe2771","DOI":"10.1126\/sciadv.abe2771","article-title":"The regulatory enzymes and protein substrates for the lysine \u03b2-hydroxybutyrylation pathway","volume":"7","author":"Huang","year":"2021","journal-title":"Sci Adv"},{"key":"2024092609311935700_qzae019-B76","doi-asserted-by":"crossref","first-page":"eabi6696","DOI":"10.1126\/sciadv.abi6696","article-title":"Class I histone deacetylases (HDAC1\u20133) are histone lysine delactylases","volume":"8","author":"Moreno-Yruela","year":"2022","journal-title":"Sci Adv"},{"key":"2024092609311935700_qzae019-B77","doi-asserted-by":"crossref","first-page":"100","DOI":"10.1074\/mcp.M111.015875","article-title":"Lysine succinylation and lysine malonylation in histones","volume":"11","author":"Xie","year":"2012","journal-title":"Mol Cell Proteomics"},{"key":"2024092609311935700_qzae019-B78","doi-asserted-by":"crossref","first-page":"605","DOI":"10.1016\/j.cmet.2014.03.014","article-title":"Lysine glutarylation is a protein posttranslational modification regulated by SIRT5","volume":"19","author":"Tan","year":"2014","journal-title":"Cell Metab"},{"key":"2024092609311935700_qzae019-B79","doi-asserted-by":"crossref","first-page":"58","DOI":"10.1038\/nchembio.495","article-title":"Identification of lysine succinylation as a new post-translational modification","volume":"7","author":"Zhang","year":"2011","journal-title":"Nat Chem Biol"},{"key":"2024092609311935700_qzae019-B80","doi-asserted-by":"crossref","first-page":"M111.012658","DOI":"10.1074\/mcp.M111.012658","article-title":"The first identification of lysine malonylation substrates and its regulatory enzyme","volume":"10","author":"Peng","year":"2011","journal-title":"Mol Cell Proteomics"},{"key":"2024092609311935700_qzae019-B81","doi-asserted-by":"crossref","first-page":"273","DOI":"10.1038\/nature25003","article-title":"KAT2A coupled with the \u03b1-KGDH complex acts as a histone H3 succinyltransferase","volume":"552","author":"Wang","year":"2017","journal-title":"Nature"},{"key":"2024092609311935700_qzae019-B82","doi-asserted-by":"crossref","first-page":"660","DOI":"10.1016\/j.molcel.2019.08.018","article-title":"Glutarylation of histone H4 lysine 91 regulates chromatin dynamics","volume":"76","author":"Bao","year":"2019","journal-title":"Mol Cell"},{"key":"2024092609311935700_qzae019-B83","doi-asserted-by":"crossref","first-page":"1874","DOI":"10.1021\/acs.biochem.2c00308","article-title":"The acyl-CoA specificity of human lysine acetyltransferase KAT2A","volume":"61","author":"Anmangandla","year":"2022","journal-title":"Biochemistry"},{"key":"2024092609311935700_qzae019-B84","doi-asserted-by":"crossref","first-page":"806","DOI":"10.1126\/science.1207861","article-title":"Sirt5 is a NAD-dependent protein lysine demalonylase and desuccinylase","volume":"334","author":"Du","year":"2011","journal-title":"Science"},{"key":"2024092609311935700_qzae019-B85","doi-asserted-by":"crossref","first-page":"12235","DOI":"10.1038\/ncomms12235","article-title":"SIRT7 is a histone desuccinylase that functionally links to chromatin compaction and genome stability","volume":"7","author":"Li","year":"2016","journal-title":"Nat Commun"},{"key":"2024092609311935700_qzae019-B86","doi-asserted-by":"crossref","first-page":"2365","DOI":"10.1073\/pnas.1717664115","article-title":"Identification of the YEATS domain of GAS41 as a pH-dependent reader of histone succinylation","volume":"115","author":"Wang","year":"2018","journal-title":"Proc Natl Acad Sci U S A"},{"key":"2024092609311935700_qzae019-B87","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1038\/nprot.2013.164","article-title":"Proteome-wide enrichment of proteins modified by lysine methylation","volume":"9","author":"Carlson","year":"2014","journal-title":"Nat Protoc"},{"key":"2024092609311935700_qzae019-B88","doi-asserted-by":"crossref","first-page":"372","DOI":"10.1074\/mcp.O113.027870","article-title":"Immunoaffinity enrichment and mass spectrometry analysis of protein methylation","volume":"13","author":"Guo","year":"2014","journal-title":"Mol Cell Proteomics"},{"key":"2024092609311935700_qzae019-B89","doi-asserted-by":"crossref","first-page":"24.8.1","DOI":"10.1002\/cpps.16","article-title":"Global proteomics analysis of protein lysine methylation","volume":"86","author":"Cao","year":"2016","journal-title":"Curr Protoc Protein Sci"},{"key":"2024092609311935700_qzae019-B90","doi-asserted-by":"crossref","first-page":"477","DOI":"10.4161\/epi.24547","article-title":"Large-scale global identification of protein lysine methylation in vivo","volume":"8","author":"Cao","year":"2013","journal-title":"Epigenetics"},{"key":"2024092609311935700_qzae019-B91","doi-asserted-by":"crossref","first-page":"103601","DOI":"10.1016\/j.jprot.2019.103601","article-title":"Protein methylome analysis in Arabidopsis reveals regulation in RNA-related processes","volume":"213","author":"Liang","year":"2020","journal-title":"J Proteomics"},{"key":"2024092609311935700_qzae019-B92","doi-asserted-by":"crossref","first-page":"329","DOI":"10.1074\/mcp.M114.044255","article-title":"A chemical proteomics approach for global analysis of lysine monomethylome profiling","volume":"14","author":"Wu","year":"2015","journal-title":"Mol Cell Proteomics"},{"key":"2024092609311935700_qzae019-B93","doi-asserted-by":"crossref","first-page":"103614","DOI":"10.1016\/j.jprot.2019.103614","article-title":"Global characterization of proteome and lysine methylome features in EZH2 wild-type and mutant lymphoma cell lines","volume":"213","author":"Hao","year":"2020","journal-title":"J Proteomics"},{"key":"2024092609311935700_qzae019-B94","doi-asserted-by":"crossref","first-page":"e2100378","DOI":"10.1002\/pmic.202100378","article-title":"An antibody-free enrichment approach enabled by reductive glutaraldehydation for monomethyllysine proteome analysis","volume":"23","author":"Li","year":"2023","journal-title":"Proteomics"},{"key":"2024092609311935700_qzae019-B95","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1016\/j.aca.2019.03.042","article-title":"A new chromatographic approach to analyze methylproteome with enhanced lysine methylation identification performance","volume":"1068","author":"Wang","year":"2019","journal-title":"Anal Chim Acta"},{"key":"2024092609311935700_qzae019-B96","doi-asserted-by":"crossref","first-page":"2497","DOI":"10.1021\/acs.jproteome.0c00976","article-title":"Chemical depletion of histidine-containing peptides allows identification of more low-abundance methylation sites from proteome samples","volume":"20","author":"Wang","year":"2021","journal-title":"J Proteome Res"},{"key":"2024092609311935700_qzae019-B97","doi-asserted-by":"crossref","first-page":"921","DOI":"10.1038\/nbt849","article-title":"A proteomics approach to understanding protein ubiquitination","volume":"21","author":"Peng","year":"2003","journal-title":"Nat Biotechnol"},{"key":"2024092609311935700_qzae019-B98","doi-asserted-by":"crossref","first-page":"M110.002089","DOI":"10.1074\/mcp.M110.002089","article-title":"A data set of human endogenous protein ubiquitination sites","volume":"10","author":"Shi","year":"2011","journal-title":"Mol Cell Proteomics"},{"key":"2024092609311935700_qzae019-B99","doi-asserted-by":"crossref","first-page":"4566","DOI":"10.1021\/pr800468j","article-title":"Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry","volume":"7","author":"Meierhofer","year":"2008","journal-title":"J Proteome Res"},{"key":"2024092609311935700_qzae019-B100","doi-asserted-by":"crossref","first-page":"1578","DOI":"10.1074\/mcp.M112.017905","article-title":"Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues","volume":"11","author":"Wagner","year":"2012","journal-title":"Mol Cell Proteomics"},{"key":"2024092609311935700_qzae019-B101","doi-asserted-by":"crossref","first-page":"M111.013284","DOI":"10.1074\/mcp.M111.013284","article-title":"A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles","volume":"10","author":"Wagner","year":"2011","journal-title":"Mol Cell Proteomics"},{"key":"2024092609311935700_qzae019-B102","doi-asserted-by":"crossref","first-page":"868","DOI":"10.1038\/nbt.1654","article-title":"Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling","volume":"28","author":"Xu","year":"2010","journal-title":"Nat Biotechnol"},{"key":"2024092609311935700_qzae019-B103","doi-asserted-by":"crossref","first-page":"631","DOI":"10.1038\/s41594-018-0084-y","article-title":"UbiSite approach for comprehensive mapping of lysine and N-terminal ubiquitination sites","volume":"25","author":"Akimov","year":"2018","journal-title":"Nat Struct Mol Biol"},{"key":"2024092609311935700_qzae019-B104","doi-asserted-by":"crossref","first-page":"867","DOI":"10.1016\/j.molcel.2015.05.006","article-title":"Quantitative proteomic atlas of ubiquitination and acetylation in the DNA damage response","volume":"59","author":"Elia","year":"2015","journal-title":"Mol Cell"},{"key":"2024092609311935700_qzae019-B105","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1016\/j.gpb.2020.11.004","article-title":"Integrative proteomic analysis of multiple post-translational modifications in inflammatory response","volume":"20","author":"Ji","year":"2022","journal-title":"Genomics Proteomics Bioinformatics"},{"key":"2024092609311935700_qzae019-B106","doi-asserted-by":"crossref","first-page":"1868","DOI":"10.15252\/embj.201694300","article-title":"SPATA2 links CYLD to the TNF-alpha receptor signaling complex and modulates the receptor signaling outcomes","volume":"35","author":"Wagner","year":"2016","journal-title":"EMBO J"},{"key":"2024092609311935700_qzae019-B107","doi-asserted-by":"crossref","first-page":"104","DOI":"10.1055\/s-0038-1676344","article-title":"Human platelet protein ubiquitylation and changes following GPVI activation","volume":"119","author":"Unsworth","year":"2019","journal-title":"Thromb Haemost"},{"key":"2024092609311935700_qzae019-B108","doi-asserted-by":"crossref","first-page":"459","DOI":"10.1016\/j.cell.2011.09.019","article-title":"Global identification of modular cullin-RING ligase substrates","volume":"147","author":"Emanuele","year":"2011","journal-title":"Cell"},{"key":"2024092609311935700_qzae019-B109","doi-asserted-by":"crossref","first-page":"85","DOI":"10.1126\/science.1250255","article-title":"Ubiquitylome analysis identifies dysregulation of effector substrates in SPOP-mutant prostate cancer","volume":"346","author":"Theurillat","year":"2014","journal-title":"Science"},{"key":"2024092609311935700_qzae019-B110","doi-asserted-by":"crossref","first-page":"1454","DOI":"10.1038\/s41467-019-09437-x","article-title":"USP32 regulates late endosomal transport and recycling through deubiquitylation of Rab7","volume":"10","author":"Sapmaz","year":"2019","journal-title":"Nat Commun"},{"key":"2024092609311935700_qzae019-B111","doi-asserted-by":"crossref","first-page":"14449","DOI":"10.1038\/ncomms14449","article-title":"Usp9x regulates Ets-1 ubiquitination and stability to control NRAS expression and tumorigenicity in melanoma","volume":"8","author":"Potu","year":"2017","journal-title":"Nat Commun"},{"key":"2024092609311935700_qzae019-B112","doi-asserted-by":"crossref","first-page":"4770","DOI":"10.1038\/s41467-018-07185-y","article-title":"Proteome-wide analysis of USP14 substrates revealed its role in hepatosteatosis via stabilization of FASN","volume":"9","author":"Liu","year":"2018","journal-title":"Nat Commun"},{"key":"2024092609311935700_qzae019-B113","doi-asserted-by":"crossref","first-page":"325","DOI":"10.1016\/j.molcel.2011.08.025","article-title":"Systematic and quantitative assessment of the ubiquitin-modified proteome","volume":"44","author":"Kim","year":"2011","journal-title":"Mol Cell"},{"key":"2024092609311935700_qzae019-B114","doi-asserted-by":"crossref","first-page":"370","DOI":"10.1038\/nature13418","article-title":"The mitochondrial deubiquitinase USP30 opposes parkin-mediated mitophagy","volume":"510","author":"Bingol","year":"2014","journal-title":"Nature"},{"key":"2024092609311935700_qzae019-B115","doi-asserted-by":"crossref","first-page":"301","DOI":"10.1126\/science.1244851","article-title":"Lenalidomide causes selective degradation of IKZF1 and IKZF3 in multiple myeloma cells","volume":"343","author":"Kronke","year":"2014","journal-title":"Science"},{"key":"2024092609311935700_qzae019-B116","doi-asserted-by":"crossref","first-page":"183","DOI":"10.1038\/nature14610","article-title":"Lenalidomide induces ubiquitination and degradation of CK1alpha in del(5q) MDS","volume":"523","author":"Kronke","year":"2015","journal-title":"Nature"},{"key":"2024092609311935700_qzae019-B117","doi-asserted-by":"crossref","first-page":"634","DOI":"10.1038\/nmeth.2518","article-title":"Integrated proteomic analysis of post-translational modifications by serial enrichment","volume":"10","author":"Mertins","year":"2013","journal-title":"Nat Methods"},{"key":"2024092609311935700_qzae019-B118","doi-asserted-by":"crossref","first-page":"395","DOI":"10.1016\/j.cels.2016.08.009","article-title":"Highly multiplexed quantitative mass spectrometry analysis of ubiquitylomes","volume":"3","author":"Rose","year":"2016","journal-title":"Cell Syst"},{"key":"2024092609311935700_qzae019-B119","doi-asserted-by":"crossref","first-page":"359","DOI":"10.1038\/s41467-019-14175-1","article-title":"Rapid and deep-scale ubiquitylation profiling for biology and translational research","volume":"11","author":"Udeshi","year":"2020","journal-title":"Nat Commun"},{"key":"2024092609311935700_qzae019-B120","doi-asserted-by":"crossref","first-page":"4348","DOI":"10.1016\/j.cell.2021.07.016","article-title":"A proteogenomic portrait of lung squamous cell carcinoma","volume":"184","author":"Satpathy","year":"2021","journal-title":"Cell"},{"key":"2024092609311935700_qzae019-B121","doi-asserted-by":"crossref","first-page":"2660","DOI":"10.3390\/cells10102660","article-title":"The many potential fates of non-canonical protein substrates subject to NEDDylation","volume":"10","author":"Vijayasimha","year":"2021","journal-title":"Cells"},{"key":"2024092609311935700_qzae019-B122","doi-asserted-by":"crossref","first-page":"30","DOI":"10.1038\/nrm3919","article-title":"Protein neddylation: beyond cullin-RING ligases","volume":"16","author":"Enchev","year":"2015","journal-title":"Nat Rev Mol Cell Biol"},{"key":"2024092609311935700_qzae019-B123","doi-asserted-by":"crossref","first-page":"1274","DOI":"10.1021\/pr700749v","article-title":"A targeted proteomic analysis of the ubiquitin-like modifier NEDD8 and associated proteins","volume":"7","author":"Jones","year":"2008","journal-title":"J Proteome Res"},{"key":"2024092609311935700_qzae019-B124","doi-asserted-by":"crossref","first-page":"177","DOI":"10.1016\/j.jhep.2022.02.007","article-title":"Targeting NAE1-mediated protein hyper-NEDDylation halts cholangiocarcinogenesis and impacts on tumor-stroma crosstalk in experimental models","volume":"77","author":"Olaizola","year":"2022","journal-title":"J Hepatol"},{"key":"2024092609311935700_qzae019-B125","doi-asserted-by":"crossref","first-page":"4376","DOI":"10.1038\/s41467-018-06365-0","article-title":"NEDDylation promotes nuclear protein aggregation and protects the ubiquitin proteasome system upon proteotoxic stress","volume":"9","author":"Maghames","year":"2018","journal-title":"Nat Commun"},{"key":"2024092609311935700_qzae019-B126","doi-asserted-by":"crossref","first-page":"12125","DOI":"10.1038\/ncomms12125","article-title":"NEDDylation promotes stress granule assembly","volume":"7","author":"Jayabalan","year":"2016","journal-title":"Nat Commun"},{"key":"2024092609311935700_qzae019-B127","doi-asserted-by":"crossref","first-page":"210","DOI":"10.1038\/s41594-019-0370-3","article-title":"Global site-specific neddylation profiling reveals that NEDDylated cofilin regulates actin dynamics","volume":"27","author":"Vogl","year":"2020","journal-title":"Nat Struct Mol Biol"},{"key":"2024092609311935700_qzae019-B128","doi-asserted-by":"crossref","first-page":"108635","DOI":"10.1016\/j.celrep.2020.108635","article-title":"Proteome-wide identification of NEDD8 modification sites reveals distinct proteomes for canonical and atypical NEDDylation","volume":"34","author":"Lobato-Gil","year":"2021","journal-title":"Cell Rep"},{"key":"2024092609311935700_qzae019-B129","doi-asserted-by":"crossref","first-page":"715","DOI":"10.1038\/s41580-022-00500-y","article-title":"Signalling mechanisms and cellular functions of SUMO","volume":"33","author":"Vertegaal","year":"2022","journal-title":"Nat Rev Mol Cell Biol"},{"key":"2024092609311935700_qzae019-B130","doi-asserted-by":"crossref","first-page":"828","DOI":"10.3390\/molecules26040828","article-title":"SUMO and transcriptional regulation: the lessons of large-scale proteomic, modifomic and genomic studies","volume":"26","author":"Boulanger","year":"2021","journal-title":"Molecules"},{"key":"2024092609311935700_qzae019-B131","doi-asserted-by":"crossref","first-page":"1599","DOI":"10.1152\/physrev.00025.2019","article-title":"SUMO: from bench to bedside","volume":"100","author":"Chang","year":"2020","journal-title":"Physiol Rev"},{"key":"2024092609311935700_qzae019-B132","doi-asserted-by":"crossref","first-page":"M110.004796","DOI":"10.1074\/mcp.M110.004796","article-title":"A novel proteomics approach to identify SUMOylated proteins and their modification sites in human cells","volume":"10","author":"Galisson","year":"2011","journal-title":"Mol Cell Proteomics"},{"key":"2024092609311935700_qzae019-B133","doi-asserted-by":"crossref","first-page":"12432","DOI":"10.1073\/pnas.1413825111","article-title":"Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli","volume":"111","author":"Impens","year":"2014","journal-title":"Proc Natl Acad Sci U S A"},{"key":"2024092609311935700_qzae019-B134","doi-asserted-by":"crossref","first-page":"927","DOI":"10.1038\/nsmb.2890","article-title":"Uncovering global SUMOylation signaling networks in a site-specific manner","volume":"21","author":"Hendriks","year":"2014","journal-title":"Nat Struct Mol Biol"},{"key":"2024092609311935700_qzae019-B135","doi-asserted-by":"crossref","first-page":"1053","DOI":"10.1016\/j.molcel.2014.02.001","article-title":"Uncovering SUMOylation dynamics during cell-cycle progression reveals FoxM1 as a key mitotic SUMO target protein","volume":"53","author":"Schimmel","year":"2014","journal-title":"Mol Cell"},{"key":"2024092609311935700_qzae019-B136","doi-asserted-by":"crossref","first-page":"rs2","DOI":"10.1126\/scisignal.2005146","article-title":"Proteome-wide identification of SUMO2 modification sites","volume":"7","author":"Tammsalu","year":"2014","journal-title":"Sci Signal"},{"key":"2024092609311935700_qzae019-B137","doi-asserted-by":"crossref","first-page":"1374","DOI":"10.1038\/nprot.2015.095","article-title":"Proteome-wide identification of SUMO modification sites by mass spectrometry","volume":"10","author":"Tammsalu","year":"2015","journal-title":"Nat Protoc"},{"key":"2024092609311935700_qzae019-B138","doi-asserted-by":"crossref","first-page":"5409","DOI":"10.1038\/ncomms6409","article-title":"Large-scale analysis of lysine SUMOylation by SUMO remnant immunoaffinity profiling","volume":"5","author":"Lamoliatte","year":"2014","journal-title":"Nat Commun"},{"key":"2024092609311935700_qzae019-B139","doi-asserted-by":"crossref","first-page":"100164","DOI":"10.1016\/j.mcpro.2021.100164","article-title":"Identification of SUMO targets associated with the pluripotent state in human stem cells","volume":"20","author":"Mojsa","year":"2021","journal-title":"Mol Cell Proteomics"},{"key":"2024092609311935700_qzae019-B140","doi-asserted-by":"crossref","first-page":"325","DOI":"10.1038\/nsmb.3366","article-title":"Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation","volume":"24","author":"Hendriks","year":"2017","journal-title":"Nat Struct Mol Biol"},{"key":"2024092609311935700_qzae019-B141","doi-asserted-by":"crossref","first-page":"7289","DOI":"10.1038\/ncomms8289","article-title":"System-wide identification of wild-type SUMO-2 conjugation sites","volume":"6","author":"Hendriks","year":"2015","journal-title":"Nat Commun"},{"key":"2024092609311935700_qzae019-B142","doi-asserted-by":"crossref","first-page":"7754","DOI":"10.1038\/s41598-018-25150-z","article-title":"Quantitative SUMO proteomics reveals the modulation of several PML nuclear body associated proteins and an anti-senescence function of UBC9","volume":"8","author":"McManus","year":"2018","journal-title":"Sci Rep"},{"key":"2024092609311935700_qzae019-B143","doi-asserted-by":"crossref","first-page":"2342","DOI":"10.1038\/nprot.2017.105","article-title":"Identification of cross talk between SUMOylation and ubiquitylation using a sequential peptide immunopurification approach","volume":"12","author":"McManus","year":"2017","journal-title":"Nat Protoc"},{"key":"2024092609311935700_qzae019-B144","doi-asserted-by":"crossref","first-page":"834","DOI":"10.1038\/s41467-020-14581-w","article-title":"Quantitative SUMO proteomics identifies PIAS1 substrates involved in cell migration and motility","volume":"11","author":"Li","year":"2020","journal-title":"Nat Commun"},{"key":"2024092609311935700_qzae019-B145","doi-asserted-by":"crossref","first-page":"14109","DOI":"10.1038\/ncomms14109","article-title":"Uncovering the SUMOylation and ubiquitylation crosstalk in human cells using sequential peptide immunopurification","volume":"8","author":"Lamoliatte","year":"2017","journal-title":"Nat Commun"},{"key":"2024092609311935700_qzae019-B146","doi-asserted-by":"crossref","first-page":"1171","DOI":"10.1038\/s41467-017-01271-3","article-title":"Site-specific identification and quantitation of endogenous SUMO modifications under native conditions","volume":"8","author":"Lumpkin","year":"2017","journal-title":"Nat Commun"},{"key":"2024092609311935700_qzae019-B147","doi-asserted-by":"crossref","first-page":"2456","DOI":"10.1038\/s41467-018-04957-4","article-title":"Site-specific characterization of endogenous SUMOylation across species and organs","volume":"9","author":"Hendriks","year":"2018","journal-title":"Nat Commun"},{"key":"2024092609311935700_qzae019-B148","doi-asserted-by":"crossref","first-page":"338324","DOI":"10.1016\/j.aca.2021.338324","article-title":"Antibody-free enrichment method for proteome-wide analysis of endogenous SUMOylation sites","volume":"1154","author":"Li","year":"2021","journal-title":"Anal Chim Acta"},{"key":"2024092609311935700_qzae019-B149","doi-asserted-by":"crossref","first-page":"607","DOI":"10.1016\/j.molcel.2006.06.026","article-title":"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey","volume":"23","author":"Kim","year":"2006","journal-title":"Mol Cell"},{"key":"2024092609311935700_qzae019-B150","doi-asserted-by":"crossref","first-page":"834","DOI":"10.1126\/science.1175371","article-title":"Lysine acetylation targets protein complexes and co-regulates major cellular functions","volume":"325","author":"Choudhary","year":"2009","journal-title":"Science"},{"key":"2024092609311935700_qzae019-B151","doi-asserted-by":"crossref","first-page":"1000","DOI":"10.1126\/science.1179689","article-title":"Regulation of cellular metabolism by protein lysine acetylation","volume":"327","author":"Zhao","year":"2010","journal-title":"Science"},{"key":"2024092609311935700_qzae019-B152","doi-asserted-by":"crossref","first-page":"1004","DOI":"10.1126\/science.1179687","article-title":"Acetylation of metabolic enzymes coordinates carbon source utilization and metabolic flux","volume":"327","author":"Wang","year":"2010","journal-title":"Science"},{"key":"2024092609311935700_qzae019-B153","doi-asserted-by":"crossref","first-page":"21568","DOI":"10.1073\/pnas.1922330117","article-title":"KAT5 acetylates cGAS to promote innate immune response to DNA virus","volume":"117","author":"Song","year":"2020","journal-title":"Proc Natl Acad Sci U S A"},{"key":"2024092609311935700_qzae019-B154","doi-asserted-by":"crossref","first-page":"732","DOI":"10.1007\/s11426-014-5100-4","article-title":"Comprehensive profiling of lysine acetylome in Staphylococcus aureus","volume":"57","author":"Zhang","year":"2014","journal-title":"Sci China Chem"},{"key":"2024092609311935700_qzae019-B155","doi-asserted-by":"crossref","first-page":"5","DOI":"10.1016\/j.molcel.2014.03.027","article-title":"Nonenzymatic protein acylation as a carbon stress regulated by sirtuin deacylases","volume":"54","author":"Wagner","year":"2014","journal-title":"Mol Cell"},{"key":"2024092609311935700_qzae019-B156","doi-asserted-by":"crossref","first-page":"231","DOI":"10.1016\/j.cell.2018.04.033","article-title":"Time-resolved analysis reveals rapid dynamics and broad scope of the CBP\/p300 acetylome","volume":"174","author":"Weinert","year":"2018","journal-title":"Cell"},{"key":"2024092609311935700_qzae019-B157","doi-asserted-by":"crossref","first-page":"984","DOI":"10.1016\/j.chembiol.2018.05.005","article-title":"Protein acylation is a general regulatory mechanism in biosynthetic pathway of acyl-CoA-derived natural products","volume":"25","author":"Xu","year":"2018","journal-title":"Cell Chem Biol"},{"key":"2024092609311935700_qzae019-B158","doi-asserted-by":"crossref","first-page":"S109","DOI":"10.1074\/mcp.RA117.000541","article-title":"Characterization of the sperm proteome and reproductive outcomes with in vitro fertilization after a reduction in male ejaculatory abstinence reriod","volume":"18","author":"Shen","year":"2019","journal-title":"Mol Cell Proteomics"},{"key":"2024092609311935700_qzae019-B159","doi-asserted-by":"crossref","first-page":"2382","DOI":"10.1074\/mcp.M113.035659","article-title":"Lysine propionylation is a prevalent post-translational modification in Thermus thermophilus","volume":"13","author":"Okanishi","year":"2014","journal-title":"Mol Cell Proteomics"},{"key":"2024092609311935700_qzae019-B160","doi-asserted-by":"crossref","first-page":"4696","DOI":"10.1021\/acs.jproteome.6b00798","article-title":"Characterization of protein lysine propionylation in Escherichia coli: global profiling, dynamic change, and enzymatic regulation","volume":"15","author":"Sun","year":"2016","journal-title":"J Proteome Res"},{"key":"2024092609311935700_qzae019-B161","doi-asserted-by":"crossref","first-page":"1588","DOI":"10.1021\/acschembio.8b00213","article-title":"Characterization of the lysine acylomes and the substrates regulated by protein acyltransferase in Mycobacterium smegmatis","volume":"13","author":"Xu","year":"2018","journal-title":"ACS Chem Biol"},{"key":"2024092609311935700_qzae019-B162","doi-asserted-by":"crossref","first-page":"1156","DOI":"10.1074\/mcp.RA117.000372","article-title":"Protein acetylation and butyrylation regulate the phenotype and metabolic shifts of the endospore-forming Clostridium acetobutylicum","volume":"17","author":"Xu","year":"2018","journal-title":"Mol Cell Proteomics"},{"key":"2024092609311935700_qzae019-B163","doi-asserted-by":"crossref","first-page":"203","DOI":"10.1016\/j.molcel.2015.02.029","article-title":"Intracellular crotonyl-CoA stimulates transcription through p300-catalyzed histone crotonylation","volume":"58","author":"Sabari","year":"2015","journal-title":"Mol Cell"},{"key":"2024092609311935700_qzae019-B164","doi-asserted-by":"crossref","first-page":"853","DOI":"10.1016\/j.molcel.2017.07.011","article-title":"Chromodomain protein CDYL acts as a crotonyl-CoA hydratase to regulate histone crotonylation and spermatogenesis","volume":"67","author":"Liu","year":"2017","journal-title":"Mol Cell"},{"key":"2024092609311935700_qzae019-B165","doi-asserted-by":"crossref","first-page":"946","DOI":"10.1038\/cr.2017.60","article-title":"Global profiling of crotonylation on non-histone proteins","volume":"27","author":"Xu","year":"2017","journal-title":"Cell Res"},{"key":"2024092609311935700_qzae019-B166","doi-asserted-by":"crossref","first-page":"eaay4697","DOI":"10.1126\/sciadv.aay4697","article-title":"Global crotonylome reveals CDYL-regulated RPA1 crotonylation in homologous recombination-mediated DNA repair","volume":"6","author":"Yu","year":"2020","journal-title":"Sci Adv"},{"key":"2024092609311935700_qzae019-B167","doi-asserted-by":"crossref","first-page":"456","DOI":"10.1161\/CIRCRESAHA.122.321054","article-title":"Modulating lysine crotonylation in cardiomyocytes improves myocardial outcomes","volume":"131","author":"Cai","year":"2022","journal-title":"Circ Res"},{"key":"2024092609311935700_qzae019-B168","doi-asserted-by":"crossref","first-page":"76","DOI":"10.1016\/j.cbpa.2017.11.003","article-title":"Protein lipoylation: an evolutionarily conserved metabolic regulator of health and disease","volume":"42","author":"Rowland","year":"2018","journal-title":"Curr Opin Chem Biol"},{"key":"2024092609311935700_qzae019-B169","doi-asserted-by":"crossref","first-page":"717503","DOI":"10.3389\/fcell.2021.717503","article-title":"Lysine fatty acylation: regulatory enzymes, research tools, and biological function","volume":"9","author":"Komaniecki","year":"2021","journal-title":"Front Cell Dev Biol"},{"key":"2024092609311935700_qzae019-B170","doi-asserted-by":"crossref","first-page":"996","DOI":"10.1038\/s41564-018-0215-6","article-title":"N\u03b5-fatty acylation of multiple membrane-associated proteins by Shigella IcsB effector to modulate host function","volume":"3","author":"Liu","year":"2018","journal-title":"Nat Microbiol"},{"key":"2024092609311935700_qzae019-B171","doi-asserted-by":"crossref","first-page":"5487","DOI":"10.1073\/pnas.1815365116","article-title":"HDAC11 regulates type I interferon signaling through defatty-acylation of SHMT2","volume":"116","author":"Cao","year":"2019","journal-title":"Proc Natl Acad Sci U S A"},{"key":"2024092609311935700_qzae019-B172","doi-asserted-by":"crossref","first-page":"482","DOI":"10.1074\/mcp.RA117.000430","article-title":"Systematic identification of lysine 2-hydroxyisobutyrylated proteins in Proteus mirabilis","volume":"17","author":"Dong","year":"2018","journal-title":"Mol Cell Proteomics"},{"key":"2024092609311935700_qzae019-B173","doi-asserted-by":"crossref","first-page":"8782","DOI":"10.1073\/pnas.1700796114","article-title":"2-hydroxyisobutyrylation on histone H4K8 is regulated by glucose homeostasis in Saccharomyces cerevisiae","volume":"114","author":"Huang","year":"2017","journal-title":"Proc Natl Acad Sci U S A"},{"key":"2024092609311935700_qzae019-B174","doi-asserted-by":"crossref","first-page":"eaaw6703","DOI":"10.1126\/sciadv.aaw6703","article-title":"Protein lysine de-2-hydroxyisobutyrylation by CobB in prokaryotes","volume":"5","author":"Dong","year":"2019","journal-title":"Sci Adv"},{"key":"2024092609311935700_qzae019-B175","doi-asserted-by":"crossref","first-page":"142","DOI":"10.1038\/s41589-021-00906-3","article-title":"TmcA functions as a lysine 2-hydroxyisobutyryltransferase to regulate transcription","volume":"18","author":"Dong","year":"2022","journal-title":"Nat Chem Biol"},{"key":"2024092609311935700_qzae019-B176","doi-asserted-by":"crossref","first-page":"355","DOI":"10.1038\/s41422-023-00793-4","article-title":"Lysine 2-hydroxyisobutyrylation of NAT10 promotes cancer metastasis in an ac4C-dependent manner","volume":"33","author":"Liao","year":"2023","journal-title":"Cell Res"},{"key":"2024092609311935700_qzae019-B177","doi-asserted-by":"crossref","first-page":"243","DOI":"10.1038\/s41419-019-1463-y","article-title":"p53 \u03b2-hydroxybutyrylation attenuates p53 activity","volume":"10","author":"Liu","year":"2019","journal-title":"Cell Death Dis"},{"key":"2024092609311935700_qzae019-B178","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1038\/s41421-019-0103-0","article-title":"Molecular basis for hierarchical histone de-beta-hydroxybutyrylation by SIRT3","volume":"5","author":"Zhang","year":"2019","journal-title":"Cell Discov"},{"key":"2024092609311935700_qzae019-B179","doi-asserted-by":"crossref","first-page":"109487","DOI":"10.1016\/j.celrep.2021.109487","article-title":"Ketogenesis impact on liver metabolism revealed by proteomics of lysine \u03b2-hydroxybutyrylation","volume":"36","author":"Koronowski","year":"2021","journal-title":"Cell Rep"},{"key":"2024092609311935700_qzae019-B180","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1038\/s41392-021-00464-z","article-title":"MTA2 triggered R-loop trans-regulates BDH1-mediated \u03b2-hydroxybutyrylation and potentiates propagation of hepatocellular carcinoma stem cells","volume":"6","author":"Zhang","year":"2021","journal-title":"Signal Transduct Target Ther"},{"key":"2024092609311935700_qzae019-B181","doi-asserted-by":"crossref","first-page":"882","DOI":"10.1038\/s42255-020-0267-9","article-title":"Glis1 facilitates induction of pluripotency via an epigenome\u2013metabolome\u2013epigenome signalling cascade","volume":"2","author":"Li","year":"2020","journal-title":"Nat Metab"},{"key":"2024092609311935700_qzae019-B182","doi-asserted-by":"crossref","first-page":"85","DOI":"10.1186\/s13059-021-02308-z","article-title":"Histone lactylation drives oncogenesis by facilitating m6A reader protein YTHDF2 expression in ocular melanoma","volume":"22","author":"Yu","year":"2021","journal-title":"Genome Biol"},{"key":"2024092609311935700_qzae019-B183","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1038\/s41418-021-00841-9","article-title":"Lactate promotes macrophage HMGB1 lactylation, acetylation, and exosomal release in polymicrobial sepsis","volume":"29","author":"Yang","year":"2022","journal-title":"Cell Death Differ"},{"key":"2024092609311935700_qzae019-B184","doi-asserted-by":"crossref","first-page":"4464","DOI":"10.1016\/j.cell.2021.07.021","article-title":"Erythroid mitochondrial retention triggers myeloid-dependent type I interferon in human SLE","volume":"184","author":"Caielli","year":"2021","journal-title":"Cell"},{"key":"2024092609311935700_qzae019-B185","doi-asserted-by":"crossref","first-page":"109820","DOI":"10.1016\/j.celrep.2021.109820","article-title":"Protein lactylation induced by neural excitation","volume":"37","author":"Hagihara","year":"2021","journal-title":"Cell Rep"},{"key":"2024092609311935700_qzae019-B186","doi-asserted-by":"crossref","first-page":"2980","DOI":"10.1016\/j.devcel.2021.09.013","article-title":"Rheb-regulated mitochondrial pyruvate metabolism of Schwann cells linked to axon stability","volume":"56","author":"Jia","year":"2021","journal-title":"Dev Cell"},{"key":"2024092609311935700_qzae019-B187","doi-asserted-by":"crossref","first-page":"854","DOI":"10.1038\/s41592-022-01523-1","article-title":"Cyclic immonium ion of lactyllysine reveals widespread lactylation in the human proteome","volume":"19","author":"Wan","year":"2022","journal-title":"Nat Methods"},{"key":"2024092609311935700_qzae019-B188","doi-asserted-by":"crossref","first-page":"919","DOI":"10.1016\/j.molcel.2013.06.001","article-title":"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways","volume":"50","author":"Park","year":"2013","journal-title":"Mol Cell"},{"key":"2024092609311935700_qzae019-B189","doi-asserted-by":"crossref","first-page":"3509","DOI":"10.1074\/mcp.M113.031567","article-title":"Identification of lysine succinylation substrates and the succinylation regulatory enzyme CobB in Escherichia coli","volume":"12","author":"Colak","year":"2013","journal-title":"Mol Cell Proteomics"},{"key":"2024092609311935700_qzae019-B190","doi-asserted-by":"crossref","first-page":"2303","DOI":"10.1016\/j.molcel.2021.04.002","article-title":"SUCLA2-coupled regulation of GLS succinylation and activity counteracts oxidative stress in tumor cells","volume":"81","author":"Tong","year":"2021","journal-title":"Mol Cell"},{"key":"2024092609311935700_qzae019-B191","doi-asserted-by":"crossref","first-page":"4043","DOI":"10.1161\/STROKEAHA.121.034850","article-title":"Sirtuin 5-mediated lysine desuccinylation protects mitochondrial metabolism following subarachnoid hemorrhage in mice","volume":"52","author":"Xiao","year":"2021","journal-title":"Stroke"},{"key":"2024092609311935700_qzae019-B192","doi-asserted-by":"crossref","first-page":"321","DOI":"10.1016\/j.molcel.2015.05.022","article-title":"SIRT5 regulates both cytosolic and mitochondrial protein malonylation with glycolysis as a major target","volume":"59","author":"Nishida","year":"2015","journal-title":"Mol Cell"},{"key":"2024092609311935700_qzae019-B193","doi-asserted-by":"crossref","first-page":"227","DOI":"10.1074\/mcp.M114.041947","article-title":"Lysine malonylation is elevated in type 2 diabetic mouse models and enriched in metabolic associated proteins","volume":"14","author":"Du","year":"2015","journal-title":"Mol Cell Proteomics"},{"key":"2024092609311935700_qzae019-B194","doi-asserted-by":"crossref","first-page":"2060","DOI":"10.1021\/acs.jproteome.6b00264","article-title":"Global profiling of protein lysine malonylation in Escherichia coli reveals its role in energy metabolism","volume":"15","author":"Qian","year":"2016","journal-title":"J Proteome Res"},{"key":"2024092609311935700_qzae019-B195","doi-asserted-by":"crossref","first-page":"1200","DOI":"10.1021\/acschembio.7b01068","article-title":"Protein acylation affects the artificial biosynthetic pathway for pinosylvin production in engineered E. coli","volume":"13","author":"Xu","year":"2018","journal-title":"ACS Chem Biol"},{"key":"2024092609311935700_qzae019-B196","doi-asserted-by":"crossref","first-page":"529","DOI":"10.2174\/1389557516666160923132611","article-title":"Pharmacological effects of biotin in animals","volume":"17","author":"Riveron-Negrete","year":"2017","journal-title":"Mini Rev Med Chem"},{"key":"2024092609311935700_qzae019-B197","doi-asserted-by":"crossref","first-page":"207","DOI":"10.1146\/annurev-nutr-042617-104653","article-title":"Holocarboxylase synthetase: a moonlighting transcriptional coregulator of gene expression and a cytosolic regulator of biotin utilization","volume":"37","author":"Le\u00f3n-Del-R\u00edo","year":"2017","journal-title":"Annu Rev Nutr"},{"key":"2024092609311935700_qzae019-B198","doi-asserted-by":"crossref","first-page":"537","DOI":"10.1016\/j.ymgme.2011.08.030","article-title":"Biotinylation is a natural, albeit rare, modification of human histones","volume":"104","author":"Kuroishi","year":"2011","journal-title":"Mol Genet Metab"},{"key":"2024092609311935700_qzae019-B199","doi-asserted-by":"crossref","first-page":"225","DOI":"10.1016\/j.jnutbio.2005.05.003","article-title":"Lysine residues in N-terminal and C-terminal regions of human histone H2A are targets for biotinylation by biotinidase","volume":"17","author":"Chew","year":"2006","journal-title":"J Nutr Biochem"},{"key":"2024092609311935700_qzae019-B200","doi-asserted-by":"crossref","first-page":"719","DOI":"10.1016\/j.bbagrm.2009.09.003","article-title":"Biotin is not a natural histone modification","volume":"1789","author":"Healy","year":"2009","journal-title":"Biochim Biophys Acta"},{"key":"2024092609311935700_qzae019-B201","doi-asserted-by":"crossref","first-page":"549","DOI":"10.1126\/science.1238327","article-title":"Functional lysine modification by an intrinsically reactive primary glycolytic metabolite","volume":"341","author":"Moellering","year":"2013","journal-title":"Science"},{"key":"2024092609311935700_qzae019-B202","doi-asserted-by":"crossref","first-page":"244","DOI":"10.1038\/nchembio.2575","article-title":"Features and regulation of non-enzymatic post-translational modifications","volume":"14","author":"Harmel","year":"2018","journal-title":"Nat Chem Biol"},{"key":"2024092609311935700_qzae019-B203","doi-asserted-by":"crossref","first-page":"513","DOI":"10.1002\/pmic.201300344","article-title":"The next level of complexity: crosstalk of post-translational modifications","volume":"14","author":"Venne","year":"2014","journal-title":"Proteomics"},{"key":"2024092609311935700_qzae019-B204","doi-asserted-by":"crossref","first-page":"682","DOI":"10.1016\/j.cell.2010.08.011","article-title":"The language of histone crosstalk","volume":"142","author":"Lee","year":"2010","journal-title":"Cell"},{"key":"2024092609311935700_qzae019-B205","doi-asserted-by":"crossref","first-page":"15912","DOI":"10.1038\/s41598-021-95398-5","article-title":"Investigating crosstalk between H3K27 acetylation and H3K4 trimethylation in CRISPR\/dCas-based epigenome editing and gene activation","volume":"11","author":"Zhao","year":"2021","journal-title":"Sci Rep"},{"key":"2024092609311935700_qzae019-B206","doi-asserted-by":"crossref","first-page":"186","DOI":"10.1016\/j.cell.2018.08.058","article-title":"Targeting epigenetic crosstalk as a therapeutic strategy for EZH2-aberrant solid tumors","volume":"175","author":"Huang","year":"2018","journal-title":"Cell"},{"key":"2024092609311935700_qzae019-B207","doi-asserted-by":"crossref","first-page":"449","DOI":"10.1016\/j.molcel.2008.07.002","article-title":"Lysine acetylation: codified crosstalk with other post-translational modifications","volume":"31","author":"Yang","year":"2008","journal-title":"Mol Cell"},{"key":"2024092609311935700_qzae019-B208","doi-asserted-by":"crossref","first-page":"207","DOI":"10.1016\/j.tcb.2009.03.001","article-title":"Crosstalk between histone modifications during the DNA damage response","volume":"19","author":"van Attikum","year":"2009","journal-title":"Trends Cell Biol"},{"key":"2024092609311935700_qzae019-B209","doi-asserted-by":"crossref","first-page":"426","DOI":"10.1016\/j.tcb.2014.01.005","article-title":"Crosstalk between ubiquitin and other post-translational modifications on chromatin during double-strand break repair","volume":"24","author":"Zhao","year":"2014","journal-title":"Trends Cell Biol"},{"key":"2024092609311935700_qzae019-B210","doi-asserted-by":"crossref","first-page":"1751","DOI":"10.1101\/gad.331231.119","article-title":"Systematic bromodomain protein screens identify homologous recombination and R-loop suppression pathways involved in genome integrity","volume":"33","author":"Kim","year":"2019","journal-title":"Genes Dev"},{"key":"2024092609311935700_qzae019-B211","doi-asserted-by":"crossref","first-page":"438","DOI":"10.1038\/s41586-021-03716-8","article-title":"Mechanisms of BRCA1\u2013BARD1 nucleosome recognition and ubiquitylation","volume":"596","author":"Hu","year":"2021","journal-title":"Nature"},{"key":"2024092609311935700_qzae019-B212","doi-asserted-by":"crossref","first-page":"eabc6663","DOI":"10.1126\/science.abc6663","article-title":"Regulation of the Dot1 histone H3K79 methyltransferase by histone H4K16 acetylation","volume":"371","author":"Valencia-Sanchez","year":"2021","journal-title":"Science"},{"key":"2024092609311935700_qzae019-B213","doi-asserted-by":"crossref","first-page":"972","DOI":"10.1038\/s41589-022-01067-7","article-title":"H2B Lys34 ubiquitination induces nucleosome distortion to stimulate Dot1L activity","volume":"18","author":"Ai","year":"2022","journal-title":"Nat Chem Biol"},{"key":"2024092609311935700_qzae019-B214","doi-asserted-by":"crossref","first-page":"1499","DOI":"10.1016\/j.celrep.2017.01.039","article-title":"CRL4DCAF8 ubiquitin ligase targets histone H3K79 and promotes H3K9 methylation in the liver","volume":"18","author":"Li","year":"2017","journal-title":"Cell Rep"},{"key":"2024092609311935700_qzae019-B215","doi-asserted-by":"crossref","first-page":"897","DOI":"10.1016\/j.molcel.2013.01.006","article-title":"RNF111-dependent neddylation activates DNA damage-induced ubiquitination","volume":"49","author":"Ma","year":"2013","journal-title":"Mol Cell"},{"key":"2024092609311935700_qzae019-B216","doi-asserted-by":"crossref","first-page":"e67952","DOI":"10.7554\/eLife.67952","article-title":"Sumoylation of the human histone H4 tail inhibits p300-mediated transcription by RNA polymerase II in cellular extracts","volume":"10","author":"Leonen","year":"2021","journal-title":"Elife"},{"key":"2024092609311935700_qzae019-B217","doi-asserted-by":"crossref","first-page":"330","DOI":"10.1016\/j.molcel.2011.03.025","article-title":"Histone methylation by PRC2 is inhibited by active chromatin marks","volume":"42","author":"Schmitges","year":"2011","journal-title":"Mol Cell"},{"key":"2024092609311935700_qzae019-B218","doi-asserted-by":"crossref","first-page":"890","DOI":"10.1038\/leu.2017.339","article-title":"SETD2-mediated crosstalk between H3K36me3 and H3K79me2 in MLL-rearranged leukemia","volume":"32","author":"Bu","year":"2018","journal-title":"Leukemia"},{"key":"2024092609311935700_qzae019-B219","doi-asserted-by":"crossref","first-page":"1068","DOI":"10.1016\/j.tplants.2018.09.004","article-title":"Protein language: post-translational modifications talking to each other","volume":"23","author":"Vu","year":"2018","journal-title":"Trends Plant Sci"},{"key":"2024092609311935700_qzae019-B220","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/s41418-021-00827-7","article-title":"Global identification of phospho-dependent SCF substrates reveals a FBXO22 phosphodegron and an ERK\u2013FBXO22\u2013BAG3 axis in tumorigenesis","volume":"29","author":"Liu","year":"2022","journal-title":"Cell Death Differ"},{"key":"2024092609311935700_qzae019-B221","doi-asserted-by":"crossref","first-page":"572","DOI":"10.1016\/j.molcel.2012.09.004","article-title":"EZH2 generates a methyl degron that is recognized by the DCAF1\/DDB1\/CUL4 E3 ubiquitin ligase complex","volume":"48","author":"Lee","year":"2012","journal-title":"Mol Cell"},{"key":"2024092609311935700_qzae019-B222","doi-asserted-by":"crossref","first-page":"5512","DOI":"10.1038\/onc.2017.158","article-title":"LSD1 demethylates HIF1\u03b1 to inhibit hydroxylation and ubiquitin-mediated degradation in tumor angiogenesis","volume":"36","author":"Lee","year":"2017","journal-title":"Oncogene"},{"key":"2024092609311935700_qzae019-B223","doi-asserted-by":"crossref","first-page":"375","DOI":"10.1016\/j.jcmgh.2022.05.006","article-title":"Epithelial SMYD5 exaggerates IBD by down-regulating mitochondrial functions via post-translational control of PGC-1\u03b1 stability","volume":"14","author":"Hou","year":"2022","journal-title":"Cell Mol Gastroenterol Hepatol"},{"key":"2024092609311935700_qzae019-B224","doi-asserted-by":"crossref","first-page":"476","DOI":"10.1074\/jbc.RA118.005336","article-title":"Proteolysis of methylated SOX2 protein is regulated by L3MBTL3 and CRL4DCAF5 ubiquitin ligase","volume":"294","author":"Zhang","year":"2019","journal-title":"J Biol Chem"},{"key":"2024092609311935700_qzae019-B225","doi-asserted-by":"crossref","first-page":"1641","DOI":"10.1038\/s41467-018-04019-9","article-title":"Methylated DNMT1 and E2F1 are targeted for proteolysis by L3MBTL3 and CRL4DCAF5 ubiquitin ligase","volume":"9","author":"Leng","year":"2018","journal-title":"Nat Commun"},{"key":"2024092609311935700_qzae019-B226","first-page":"9053","article-title":"SET8 prevents excessive DNA methylation by methylation-mediated degradation of UHRF1 and DNMT1","volume":"47","author":"Zhang","year":"2019","journal-title":"Nucleic Acids Res"},{"key":"2024092609311935700_qzae019-B227","doi-asserted-by":"crossref","first-page":"1859","DOI":"10.1080\/15384101.2015.1040965","article-title":"c-Myc is targeted to the proteasome for degradation in a SUMOylation-dependent manner, regulated by PIAS1, SENP7 and RNF4","volume":"14","author":"Gonzalez-Prieto","year":"2015","journal-title":"Cell Cycle"},{"key":"2024092609311935700_qzae019-B228","doi-asserted-by":"crossref","first-page":"195","DOI":"10.1093\/jmcb\/mjx009","article-title":"A CK2\u2013RNF4 interplay coordinates non-canonical SUMOylation and degradation of nuclear receptor FXR","volume":"9","author":"Bilodeau","year":"2017","journal-title":"J Mol Cell Biol"},{"key":"2024092609311935700_qzae019-B229","doi-asserted-by":"crossref","first-page":"809","DOI":"10.1016\/j.molcel.2016.02.032","article-title":"Glutamine triggers acetylation-dependent degradation of glutamine synthetase via the thalidomide receptor cereblon","volume":"61","author":"Nguyen","year":"2016","journal-title":"Mol Cell"},{"key":"2024092609311935700_qzae019-B230","doi-asserted-by":"crossref","first-page":"689","DOI":"10.15252\/embr.201439792","article-title":"MPP8 and SIRT1 crosstalk in E-cadherin gene silencing and epithelial\u2013mesenchymal transition","volume":"16","author":"Sun","year":"2015","journal-title":"EMBO Rep"},{"key":"2024092609311935700_qzae019-B231","doi-asserted-by":"crossref","first-page":"506","DOI":"10.1016\/j.molcel.2013.07.002","article-title":"Acetylation stabilizes ATP-citrate lyase to promote lipid biosynthesis and tumor growth","volume":"51","author":"Lin","year":"2013","journal-title":"Mol Cell"},{"key":"2024092609311935700_qzae019-B232","doi-asserted-by":"crossref","first-page":"7878","DOI":"10.1093\/nar\/gkv707","article-title":"Acetylation-dependent function of human single-stranded DNA binding protein 1","volume":"43","author":"Wu","year":"2015","journal-title":"Nucleic Acids Res"},{"key":"2024092609311935700_qzae019-B233","doi-asserted-by":"crossref","first-page":"eaai8026","DOI":"10.1126\/scisignal.aai8026","article-title":"Acetylation-dependent regulation of MDM2 E3 ligase activity dictates its oncogenic function","volume":"10","author":"Nihira","year":"2017","journal-title":"Sci Signal"},{"key":"2024092609311935700_qzae019-B234","doi-asserted-by":"crossref","first-page":"4869","DOI":"10.1158\/0008-5472.CAN-19-0442","article-title":"BRD4 promotes gastric cancer progression and metastasis through acetylation-dependent stabilization of Snail","volume":"79","author":"Qin","year":"2019","journal-title":"Cancer Res"},{"key":"2024092609311935700_qzae019-B235","doi-asserted-by":"crossref","first-page":"102141","DOI":"10.1016\/j.redox.2021.102141","article-title":"Deacetylation-dependent regulation of PARP1 by SIRT2 dictates ubiquitination of PARP1 in oxidative stress-induced vascular injury","volume":"47","author":"Zhang","year":"2021","journal-title":"Redox Biol"},{"key":"2024092609311935700_qzae019-B236","doi-asserted-by":"crossref","first-page":"2464","DOI":"10.1038\/s41467-018-04815-3","article-title":"Mutually exclusive acetylation and ubiquitylation of the splicing factor SRSF5 control tumor growth","volume":"9","author":"Chen","year":"2018","journal-title":"Nat Commun"},{"key":"2024092609311935700_qzae019-B237","doi-asserted-by":"crossref","first-page":"1331","DOI":"10.1093\/emboj\/20.6.1331","article-title":"p300\/CBP-mediated p53 acetylation is commonly induced by p53-activating agents and inhibited by MDM2","volume":"20","author":"Ito","year":"2001","journal-title":"EMBO J"},{"key":"2024092609311935700_qzae019-B238","doi-asserted-by":"crossref","first-page":"3074","DOI":"10.1158\/0008-5472.CAN-20-0233","article-title":"p300-mediated acetylation of histone demethylase JMJD1A prevents its degradation by ubiquitin ligase STUB1 and enhances its activity in prostate cancer","volume":"80","author":"Xu","year":"2020","journal-title":"Cancer Res"},{"key":"2024092609311935700_qzae019-B239","doi-asserted-by":"crossref","first-page":"5133","DOI":"10.1038\/s41467-022-32920-x","article-title":"Crosstalk between SUMOylation and ubiquitylation controls DNA end resection by maintaining MRE11 homeostasis on chromatin","volume":"13","author":"Zhang","year":"2022","journal-title":"Nat Commun"},{"key":"2024092609311935700_qzae019-B240","doi-asserted-by":"crossref","first-page":"741736","DOI":"10.3389\/fcell.2021.741736","article-title":"Hypoxia stimulates SUMOylation-dependent stabilization of KDM5B","volume":"9","author":"Zhou","year":"2021","journal-title":"Front Cell Dev Biol"},{"key":"2024092609311935700_qzae019-B241","doi-asserted-by":"crossref","first-page":"50522","DOI":"10.18632\/oncotarget.10494","article-title":"SUMOylation of PES1 upregulates its stability and function via inhibiting its ubiquitination","volume":"7","author":"Li","year":"2016","journal-title":"Oncotarget"},{"key":"2024092609311935700_qzae019-B242","first-page":"898","article-title":"ZNF451 stabilizes TWIST2 through SUMOylation and promotes epithelial-mesenchymal transition","volume":"11","author":"Zeng","year":"2021","journal-title":"Am J Cancer Res"},{"key":"2024092609311935700_qzae019-B243","doi-asserted-by":"crossref","first-page":"1246","DOI":"10.1038\/emboj.2009.83","article-title":"Crosstalk between sumoylation and acetylation regulates p53-dependent chromatin transcription and DNA binding","volume":"28","author":"Wu","year":"2009","journal-title":"EMBO J"},{"key":"2024092609311935700_qzae019-B244","doi-asserted-by":"crossref","first-page":"91","DOI":"10.1016\/j.bbrc.2021.02.099","article-title":"Methylation-dependent SUMOylation of the architectural transcription factor HMGA2","volume":"552","author":"Stabell","year":"2021","journal-title":"Biochem Biophys Res Commun"},{"key":"2024092609311935700_qzae019-B245","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1038\/nrm1547","article-title":"Function and regulation of cullin-RING ubiquitin ligases","volume":"6","author":"Petroski","year":"2005","journal-title":"Nat Rev Mol Cell Biol"},{"key":"2024092609311935700_qzae019-B246","doi-asserted-by":"crossref","first-page":"995","DOI":"10.1016\/j.cell.2008.07.022","article-title":"Structural insights into NEDD8 activation of cullin-RING ligases: conformational control of conjugation","volume":"134","author":"Duda","year":"2008","journal-title":"Cell"},{"key":"2024092609311935700_qzae019-B247","doi-asserted-by":"crossref","first-page":"1416","DOI":"10.1101\/gad.328849.119","article-title":"Regulation of histone methylation by automethylation of PRC2","volume":"33","author":"Wang","year":"2019","journal-title":"Genes Dev"},{"key":"2024092609311935700_qzae019-B248","doi-asserted-by":"crossref","first-page":"1428","DOI":"10.1101\/gad.328773.119","article-title":"Automethylation of PRC2 promotes H3K27 methylation and is impaired in H3K27M pediatric glioma","volume":"33","author":"Lee","year":"2019","journal-title":"Genes Dev"},{"key":"2024092609311935700_qzae019-B249","doi-asserted-by":"crossref","first-page":"308","DOI":"10.1038\/nsmb740","article-title":"Regulation of the p300 HAT domain via a novel activation loop","volume":"11","author":"Thompson","year":"2004","journal-title":"Nat Struct Mol Biol"},{"key":"2024092609311935700_qzae019-B250","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1038\/nrc3430","article-title":"MDM2, MDMX and p53 in oncogenesis and cancer therapy","volume":"13","author":"Wade","year":"2013","journal-title":"Nat Rev Cancer"},{"key":"2024092609311935700_qzae019-B251","doi-asserted-by":"crossref","first-page":"18939","DOI":"10.1074\/jbc.M113.454470","article-title":"Auto-ubiquitination of Mdm2 enhances its substrate ubiquitin ligase activity","volume":"288","author":"Ranaweera","year":"2013","journal-title":"J Biol Chem"},{"key":"2024092609311935700_qzae019-B252","doi-asserted-by":"crossref","first-page":"100193","DOI":"10.1016\/j.mcpro.2022.100193","article-title":"An expanding repertoire of protein acylations","volume":"21","author":"Xu","year":"2022","journal-title":"Mol Cell Proteomics"},{"key":"2024092609311935700_qzae019-B253","doi-asserted-by":"crossref","first-page":"1118","DOI":"10.1158\/2159-8290.CD-20-0751","article-title":"Targeting the p300\/CBP axis in lethal prostate cancer","volume":"11","author":"Welti","year":"2021","journal-title":"Cancer Discov"},{"key":"2024092609311935700_qzae019-B254","doi-asserted-by":"crossref","first-page":"2502","DOI":"10.1002\/hep.30544","article-title":"Aberrant super-enhancer landscape in human hepatocellular carcinoma","volume":"69","author":"Tsang","year":"2019","journal-title":"Hepatology"},{"key":"2024092609311935700_qzae019-B255","doi-asserted-by":"crossref","first-page":"2649","DOI":"10.1158\/0008-5472.CAN-18-2331","article-title":"MITF expression predicts therapeutic vulnerability to p300 inhibition in human melanoma","volume":"79","author":"Kim","year":"2019","journal-title":"Cancer Res"},{"key":"2024092609311935700_qzae019-B256","doi-asserted-by":"crossref","first-page":"641","DOI":"10.1186\/s12885-018-4559-3","article-title":"p300 promotes proliferation, migration, and invasion via inducing epithelial\u2013mesenchymal transition in non-small cell lung cancer cells","volume":"18","author":"Hou","year":"2018","journal-title":"BMC Cancer"},{"key":"2024092609311935700_qzae019-B257","doi-asserted-by":"crossref","first-page":"279","DOI":"10.1038\/onc.2015.92","article-title":"The epigenetic regulators CBP and p300 facilitate leukemogenesis and represent therapeutic targets in acute myeloid leukemia","volume":"35","author":"Giotopoulos","year":"2016","journal-title":"Oncogene"},{"key":"2024092609311935700_qzae019-B258","doi-asserted-by":"crossref","first-page":"108","DOI":"10.1038\/nature11606","article-title":"EZH2 inhibition as a therapeutic strategy for lymphoma with EZH2-activating mutations","volume":"492","author":"McCabe","year":"2012","journal-title":"Nature"},{"key":"2024092609311935700_qzae019-B259","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1038\/nchembio721","article-title":"Identification of a specific inhibitor of the histone methyltransferase SU(VAR)3-9","volume":"1","author":"Greiner","year":"2005","journal-title":"Nat Chem Biol"},{"key":"2024092609311935700_qzae019-B260","doi-asserted-by":"crossref","first-page":"513","DOI":"10.1038\/nature09806","article-title":"The histone methyltransferase SETDB1 is recurrently amplified in melanoma and accelerates its onset","volume":"471","author":"Ceol","year":"2011","journal-title":"Nature"},{"key":"2024092609311935700_qzae019-B261","doi-asserted-by":"crossref","first-page":"823","DOI":"10.1038\/nrc2253","article-title":"MLL translocations, histone modifications and leukaemia stem-cell development","volume":"7","author":"Krivtsov","year":"2007","journal-title":"Nat Rev Cancer"},{"key":"2024092609311935700_qzae019-B262","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1016\/j.cell.2020.03.042","article-title":"Epigenetic therapy for epithelioid sarcoma","volume":"181","author":"Rothbart","year":"2020","journal-title":"Cell"},{"key":"2024092609311935700_qzae019-B263","doi-asserted-by":"crossref","first-page":"100992","DOI":"10.1016\/j.blre.2022.100992","article-title":"Follicular lymphoma: the long and winding road leading to your cure?","volume":"57","author":"Gordon","year":"2023","journal-title":"Blood Rev"},{"key":"2024092609311935700_qzae019-B264","doi-asserted-by":"crossref","first-page":"732","DOI":"10.1038\/nature07884","article-title":"An inhibitor of NEDD8-activating enzyme as a new approach to treat cancer","volume":"458","author":"Soucy","year":"2009","journal-title":"Nature"},{"key":"2024092609311935700_qzae019-B265","doi-asserted-by":"crossref","first-page":"1069","DOI":"10.1111\/cts.12972","article-title":"Asia-inclusive global development of pevonedistat: clinical pharmacology and translational research enabling a phase 3 multiregional clinical trial","volume":"14","author":"Zhou","year":"2021","journal-title":"Clin Transl Sci"},{"key":"2024092609311935700_qzae019-B266","doi-asserted-by":"crossref","first-page":"114334","DOI":"10.1016\/j.ejmech.2022.114334","article-title":"Small-molecule MDM2 inhibitors in clinical trials for cancer therapy","volume":"236","author":"Wang","year":"2022","journal-title":"Eur J Med Chem"},{"key":"2024092609311935700_qzae019-B267","doi-asserted-by":"crossref","first-page":"1345","DOI":"10.1126\/science.1177319","article-title":"Identification of a primary target of thalidomide teratogenicity","volume":"327","author":"Ito","year":"2010","journal-title":"Science"},{"key":"2024092609311935700_qzae019-B268","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1038\/nature13527","article-title":"Structure of the DDB1-CRBN E3 ubiquitin ligase in complex with thalidomide","volume":"512","author":"Fischer","year":"2014","journal-title":"Nature"},{"key":"2024092609311935700_qzae019-B269","doi-asserted-by":"crossref","first-page":"eaal3755","DOI":"10.1126\/science.aal3755","article-title":"Anticancer sulfonamides target splicing by inducing RBM39 degradation via recruitment to DCAF15","volume":"356","author":"Han","year":"2017","journal-title":"Science"},{"key":"2024092609311935700_qzae019-B270","doi-asserted-by":"crossref","first-page":"403","DOI":"10.1038\/nature01071","article-title":"A cryptic protease couples deubiquitination and degradation by the proteasome","volume":"419","author":"Yao","year":"2002","journal-title":"Nature"},{"key":"2024092609311935700_qzae019-B271","doi-asserted-by":"crossref","first-page":"6656","DOI":"10.1021\/acs.chemrev.8b00008","article-title":"Chemical and biochemical perspectives of protein lysine methylation","volume":"118","author":"Luo","year":"2018","journal-title":"Chem Rev"},{"key":"2024092609311935700_qzae019-B272","doi-asserted-by":"crossref","first-page":"1892","DOI":"10.1021\/acs.jmedchem.9b01318","article-title":"p97: an emerging target for cancer, neurodegenerative diseases, and viral infections","volume":"63","author":"Huryn","year":"2020","journal-title":"J Med Chem"},{"key":"2024092609311935700_qzae019-B273","doi-asserted-by":"crossref","first-page":"508","DOI":"10.1634\/theoncologist.8-6-508","article-title":"Velcade: U.S. FDA approval for the treatment of multiple myeloma progressing on prior therapy","volume":"8","author":"Kane","year":"2003","journal-title":"Oncologist"},{"key":"2024092609311935700_qzae019-B274","doi-asserted-by":"crossref","first-page":"4559","DOI":"10.1158\/1078-0432.CCR-13-0755","article-title":"U.S. Food and Drug Administration approval: carfilzomib for the treatment of multiple myeloma","volume":"19","author":"Herndon","year":"2013","journal-title":"Clin Cancer Res"},{"key":"2024092609311935700_qzae019-B275","doi-asserted-by":"crossref","first-page":"792","DOI":"10.1016\/j.cell.2017.04.023","article-title":"The logic of the 26S proteasome","volume":"169","author":"Collins","year":"2017","journal-title":"Cell"},{"key":"2024092609311935700_qzae019-B276","doi-asserted-by":"crossref","first-page":"101956","DOI":"10.1016\/j.gde.2022.101956","article-title":"The evolution of post-translational modifications","volume":"76","author":"Bradley","year":"2022","journal-title":"Curr Opin Genet Dev"},{"key":"2024092609311935700_qzae019-B277","doi-asserted-by":"crossref","first-page":"264","DOI":"10.1038\/nrm2861","article-title":"Histone variants\u2013ancient wrap artists of the epigenome","volume":"11","author":"Talbert","year":"2010","journal-title":"Nat Rev Mol Cell Biol"},{"key":"2024092609311935700_qzae019-B278","doi-asserted-by":"crossref","first-page":"1700300","DOI":"10.1002\/pmic.201700300","article-title":"Systematic proteomic analysis of protein methylation in prokaryotes and eukaryotes revealed distinct substrate specificity","volume":"18","author":"Zhang","year":"2018","journal-title":"Proteomics"},{"key":"2024092609311935700_qzae019-B279","doi-asserted-by":"crossref","first-page":"154","DOI":"10.1038\/s42003-019-0419-1","article-title":"Fungal acetylome comparative analysis identifies an essential role of acetylation in human fungal pathogen virulence","volume":"2","author":"Li","year":"2019","journal-title":"Commun Biol"},{"key":"2024092609311935700_qzae019-B280","doi-asserted-by":"crossref","first-page":"113793","DOI":"10.1016\/j.ab.2020.113793","article-title":"Accurate prediction of species-specific 2-hydroxyisobutyrylation sites based on machine learning frameworks","volume":"602","author":"Wang","year":"2020","journal-title":"Anal Biochem"},{"key":"2024092609311935700_qzae019-B281","doi-asserted-by":"crossref","first-page":"97","DOI":"10.1016\/j.jtbi.2017.05.005","article-title":"PSSM-Suc: accurately predicting succinylation using position specific scoring matrix into bigram for feature extraction","volume":"425","author":"Dehzangi","year":"2017","journal-title":"J Theor Biol"},{"key":"2024092609311935700_qzae019-B282","doi-asserted-by":"crossref","first-page":"1023","DOI":"10.3390\/genes11091023","article-title":"Accurately predicting glutarylation sites using sequential bi-peptide-based evolutionary features","volume":"11","author":"Arafat","year":"2020","journal-title":"Genes (Basel)"},{"key":"2024092609311935700_qzae019-B283","doi-asserted-by":"crossref","first-page":"104022","DOI":"10.1016\/j.compbiomed.2020.104022","article-title":"SEMal: accurate protein malonylation site predictor using structural and evolutionary information","volume":"125","author":"Dipta","year":"2020","journal-title":"Comput Biol Med"}],"container-title":["Genomics, Proteomics &amp; Bioinformatics"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/academic.oup.com\/gpb\/advance-article-pdf\/doi\/10.1093\/gpbjnl\/qzae019\/56794455\/qzae019.pdf","content-type":"application\/pdf","content-version":"am","intended-application":"syndication"},{"URL":"https:\/\/academic.oup.com\/gpb\/article-pdf\/22\/1\/qzae019\/59350534\/qzae019.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/academic.oup.com\/gpb\/article-pdf\/22\/1\/qzae019\/59350534\/qzae019.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2024,9,26]],"date-time":"2024-09-26T09:32:59Z","timestamp":1727343179000},"score":1,"resource":{"primary":{"URL":"https:\/\/academic.oup.com\/gpb\/article\/doi\/10.1093\/gpbjnl\/qzae019\/7616102"}},"subtitle":[],"editor":[{"given":"Yu","family":"Xue","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"editor"}]}],"short-title":[],"issued":{"date-parts":[[2024,2,1]]},"references-count":283,"journal-issue":{"issue":"1","published-print":{"date-parts":[[2024,5,9]]}},"URL":"https:\/\/doi.org\/10.1093\/gpbjnl\/qzae019","relation":{},"ISSN":["1672-0229","2210-3244"],"issn-type":[{"value":"1672-0229","type":"print"},{"value":"2210-3244","type":"electronic"}],"subject":[],"published-other":{"date-parts":[[2024,2,1]]},"published":{"date-parts":[[2024,2,1]]},"article-number":"qzae019"}}