Deciphering combinatorial post-translational modifications by top-down mass spectrometry

被引：37

作者：

Brodbelt, Jennifer S. ^{[1
]}

机构：

[1] Univ Texas Austin, Dept Chem, Austin, TX 78712 USA

来源：

CURRENT OPINION IN CHEMICAL BIOLOGY | 2022年 / 70卷

基金：

美国国家卫生研究院;

关键词：

Proteomics; Top-down; Ion activation; Internal ions; Ion-ion re-actions; Proteoform; ELECTRON-TRANSFER DISSOCIATION; NM ULTRAVIOLET PHOTODISSOCIATION; PROTON-TRANSFER REACTIONS; INTACT PROTEINS; CAPTURE DISSOCIATION; SEQUENCE COVERAGE; ION PARKING; PROTEOMICS; PROTEOFORMS; FRAGMENTATION;

D O I：

10.1016/j.cbpa.2022.102180

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Post-translational modifications (PTMs) create vast structural and functional diversity of proteins, ultimately modulating protein function and degradation, influencing cellular signaling, and regulating transcription. The combinatorial patterns of PTMs increase the heterogeneity of proteins and further mediates their interactions. Advances in mass spectrometrybased proteomics have resulted in identification of thousands of proteins and allowed characterization of numerous types and sites of PTMs. Examination of intact proteins, termed the top-down approach, offers the potential to map protein sequences and localize multiple PTMs on each protein, providing the most comprehensive cataloging of proteoforms. This review describes some of the dividends of using mass spectrometry to analyze intact proteins and showcases innovative strategies that have enhanced the promise of top-down proteomics for exploring the impact of combinatorial PTMs in unsurpassed detail.

引用

页数：12

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