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首页> 外文期刊>Advances in Experimental Medicine and Biology >Chapter 9: Mass Spectrometric Analysis of Post-translational Modifications (PTMs) and Protein-Protein Interactions (PPIs)
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Chapter 9: Mass Spectrometric Analysis of Post-translational Modifications (PTMs) and Protein-Protein Interactions (PPIs)

机译:第9章:质谱分析翻译后修饰(PTM)和蛋白质-蛋白质相互作用(PPI)

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摘要

Of the 25,000-30,000 human genes, about 2 % code for proteins. However, there are about one to two million protein entities. This is primarily due to alternative splicing and post-translational modifications (PTMs). Identifying all these modifications in one proteome at a particular time point during development or during the transition from normal to cancerous cells is a great challenge to scientists. In addition, identifying the biological significance of all these modifications, as well as their nature, such as stable versus transient modifications, is an even more challenging. Furthermore, interaction of proteins and protein isoforms that have one or more stable or transient PTMs with other proteins and protein isoforms makes the study of proteins daunting and complex. Here we review some of the strategies to study proteins, protein isoforms, protein PTMs, and protein-protein interactions (PPIs). Our goal is to provide a thorough understanding of these proteins and their isoforms, PTMs and PPIs and to shed light on the biological significance of these factors.
机译:在25,000-30,000个人类基因中,约2%编码蛋白质。但是,大约有一到两百万个蛋白质实体。这主要是由于其他剪接和翻译后修饰(PTM)。在发育过程中或从正常细胞到癌细胞的过渡过程中的特定时间点,识别一个蛋白质组中的所有这些修饰对科学家来说是一个巨大的挑战。另外,鉴定所有这些修饰的生物学意义以及它们的性质,例如稳定修饰与瞬时修饰,甚至更具挑战性。此外,具有一个或多个稳定或瞬时PTM的蛋白质和蛋白质同工型与其他蛋白质和蛋白质同工型的相互作用使蛋白质研究变得艰巨而复杂。在这里,我们回顾一些研究蛋白质,蛋白质同工型,蛋白质PTM和蛋白质-蛋白质相互作用(PPI)的策略。我们的目标是全面了解这些蛋白质及其同工型,PTM和PPI,并阐明这些因素的生物学意义。

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