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Substrate and Functional Diversity of Protein Lysine Post-translational Modifica
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作者 Bingbing Hao Kaifeng Chen +3 位作者 Linhui Zhai Muyin Liu Bin Liu Minjia Tan 《Genomics, Proteomics & Bioinformatics》 SCIE CAS CSCD 2024年第1期29-49,共21页
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.Dysr... 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. 展开更多
关键词 Protein lysine PTM regulatory enzyme PTM crosstalk Drug target ACYLATION
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