High-throughput quantitative top-down proteomics.

High-throughput quantitative top-down proteomics.
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DOI:
10.1039/c9mo00154a
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发表时间:
2020-04-01
期刊:
影响因子:
2.9
通讯作者:
Wu S
Wu S
中科院分区:
生物学4区
文献类型:
--
作者:
Cupp-Sutton KA;Wu S

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自上而下的质谱(MS)在蛋白质组水平上分析完整的蛋白质,这使研究人员能够更好地了解蛋白质修饰的功能。最近,自上而下的蛋白质组学由于高分辨率质谱仪的进步、液相色谱(LC)分离效率的提高以及数据分析软件的进步而越来越受欢迎。一些独特的蛋白质蛋白质型,已区分使用自上而下的MS,甚至已被证明表现出显着的变化,在生物功能相比,类似的蛋白质型。然而,特定蛋白质型的定性鉴定可能不足以确定该蛋白质型的生物相关性。定量自上而下的MS方法已被显着应用于蛋白质的不同生物学功能的研究,并允许研究人员在蛋白质,而不是肽,水平上探索蛋白质组。在这里,我们回顾了自上而下的MS方法,已被用来定量识别完整的蛋白质,讨论目前的应用定量自上而下的MS分析,并提出了新的领域,定量自上而下的MS分析可能会实施。
Top-down mass spectrometry (MS) analyzes intact proteins at the proteoform level, which allows researchers to better understand the functions of protein modifications. Recently, top-down proteomics has increased in popularity due to advancements in high-resolution mass spectrometers, increased efficiency in liquid chromatography (LC) separation, and advances in data analysis software. Some unique protein proteoforms, which have been distinguished using top-down MS, have even been shown to exhibit marked variation in biological function compared to similar proteoforms. However, the qualitative identification of a particular proteoform may not be enough to determine the biological relevance of that proteoform. Quantitative top-down MS methods have been notably applied to the study of the differing biological functions of protein proteoforms and have allowed researchers to explore proteomes at the proteoform, rather than the peptide, level. Here, we review the top-down MS methods that have been used to quantitatively identify intact proteins, discuss current applications of quantitative top-down MS analysis, and present new areas where quantitative top-down MS analysis may be implemented.
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