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

Deciphering combinatorial post-translational modifications by top-down mass spectrometry.
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DOI:
10.1016/j.cbpa.2022.102180
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发表时间:
2022-10
影响因子:
7.8
通讯作者:
--
中科院分区:
生物学2区
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--
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翻译后修饰(PTMs)创造了蛋白质的巨大结构和功能多样性,最终调节蛋白质的功能和降解,影响细胞信号传导,并调节转录。PTM的组合模式增加了蛋白质的异质性,并进一步介导它们的相互作用。基于质谱的蛋白质组学的进展已经导致鉴定了数千种蛋白质,并允许表征多种类型和位点的PTM。检查完整的蛋白质,称为自上而下的方法,提供了潜在的映射蛋白质序列和定位每个蛋白质上的多个PTM,提供最全面的蛋白质型编目。这篇综述描述了一些使用质谱分析完整蛋白质的好处,并展示了创新的策略,增强了自上而下的蛋白质组学的承诺,探索组合PTM的影响,在无与伦比的细节。
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 spectrometry-based 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.
DOI: 10.1007/978-1-4939-6783-4_18
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