Simultaneous and site-specific profiling of heterogeneity and turnover in protein <i>S</i>-acylation by intact <i>S</i>-acylated peptide analysis with a cleavable bioorthogonal tag-Reference-Cited by-同舟云学术

Simultaneous and site-specific profiling of heterogeneity and turnover in protein S-acylation by intact S-acylated peptide analysis with a cleavable bioorthogonal tag

Published:2024 Issue: Volume: Page:
ISSN:0003-2654
Container-title:The Analyst
language:en
Short-container-title:Analyst

Author:

Wu Roujun¹,Ji Guanghui¹,Chen Weiyu¹,Zhang Lei²,Fang Caiyun¹,Lu Haojie¹²^ORCID

Affiliation:

1. Department of Chemistry and Liver Cancer Institute, Zhongshan Hospital, Fudan University, Shanghai 200433, P. R. China

2. Institutes of Biomedical Sciences and NHC Key Laboratory of Glycoconjugates Research, Fudan University, Shanghai 200032, P. R. China

Abstract

A novel method for the analysis of S-acylproteome by site-specifically profiling dynamicity and acyl chain heterogeneity in protein S-acylation by analyzing intact S-acylated peptides.

Funder

National Key Research and Development Program of China

National Natural Science Foundation of China

Publisher

Royal Society of Chemistry (RSC)

Subject

Electrochemistry,Spectroscopy,Environmental Chemistry,Biochemistry,Analytical Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2024/AN/D3AN02059B

Reference31 articles.

1. Regulation of Dynamic Protein S-Acylation

2. Dynamic Protein Acylation: New Substrates, Mechanisms, and Drug Targets

3. Proteome-Scale Analysis of Protein S-Acylation Comes of Age

4. Palmitoylated proteins: purification and identification

5. Ultradeep Palmitoylomics Enabled by Dithiodipyridine-Functionalized Magnetic Nanoparticles

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