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Identification of lysine acetylome in cervical cancer by label-free quantitative proteomics.


ABSTRACT: Background:Lysine acetylation is a post-translational modification that regulates a diversity of biological processes, including cancer development. Methods:Here, we performed the quantitative acetylproteomic analysis of three primary cervical cancer tissues and corresponding adjacent normal tissues by using the label-free proteomics approach. Results:We identified a total of 928 lysine acetylation sites from 1547 proteins, in which 495 lysine acetylation sites corresponding to 296 proteins were quantified. Further, 41 differentially expressed lysine acetylation sites corresponding to 30 proteins were obtained in cervical cancer tissues compared with adjacent normal tissues (Fold change?>?2 and P?

SUBMITTER: Zhang L 

PROVIDER: S-EPMC7247262 | biostudies-literature | 2020

REPOSITORIES: biostudies-literature

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Identification of lysine acetylome in cervical cancer by label-free quantitative proteomics.

Zhang Lu L   Wang Wanyue W   Zhang Shanqiang S   Wang Yuxin Y   Guo Weikang W   Liu Yunduo Y   Wang Yaoxian Y   Zhang Yunyan Y  

Cancer cell international 20200524


<h4>Background</h4>Lysine acetylation is a post-translational modification that regulates a diversity of biological processes, including cancer development.<h4>Methods</h4>Here, we performed the quantitative acetylproteomic analysis of three primary cervical cancer tissues and corresponding adjacent normal tissues by using the label-free proteomics approach.<h4>Results</h4>We identified a total of 928 lysine acetylation sites from 1547 proteins, in which 495 lysine acetylation sites correspondin  ...[more]

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