Recent development of analytical methods for disease-specific protein <i>O</i>-GlcNAcylation-Reference-Cited by-同舟云学术

Recent development of analytical methods for disease-specific protein O-GlcNAcylation

Published:2023 Issue:1 Volume:13 Page:264-280
ISSN:2046-2069
Container-title:RSC Advances
language:en
Short-container-title:RSC Adv.

Author:

Hu Wenhua¹,Zhang Guolin²,Zhou Yu³,Xia Jun³,Zhang Peng⁴,Xiao Wenjin⁵,Xue Man²,Lu Zhaohui⁶,Yang Shuang¹^ORCID

Affiliation:

1. Center for Clinical Mass Spectrometry, College of Pharmaceutical Sciences, Soochow University, Suzhou, Jiangsu, 215123, China

2. Suzhou Institute for Drug Control, Suzhou, Jiangsu, 215104, China

3. Laboratory Medicine Center, Department of Clinical Laboratory, Zhejiang Provincial People's Hospital, Affiliated People's Hospital, Hangzhou Medical College, Hangzhou, Zhejiang, 310014, China

4. Department of Orthopedics, The Second Affiliated Hospital of Soochow University, Suzhou, Jiangsu, 215004, China

5. Department of Endocrinology, The Second Affiliated Hospital of Soochow University, Suzhou, Jiangsu, 215004, China

6. Health Examination Center, The Second Affiliated Hospital of Soochow University, Suzhou, Jiangsu, 215004, China

Abstract

The enzymatic modification of protein serine or threonine residues by N-acetylglucosamine, namely O-GlcNAcylation, is a ubiquitous post-translational modification that frequently occurs in the nucleus and cytoplasm.

Funder

Soochow University

Priority Academic Program Development of Jiangsu Higher Education Institutions

Publisher

Royal Society of Chemistry (RSC)

Subject

General Chemical Engineering,General Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2023/RA/D2RA07184C

Reference201 articles.

1. On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database

2. Topography and polypeptide distribution of terminal N-acetylglucosamine residues on the surfaces of intact lymphocytes. Evidence for O-linked GlcNAc.