Mass Spectrometry for O-GlcNAcylation

O-linked β-N-acetylglucosamine modification (O-GlcNAcylation) at proteins with low-abundance expression level and species diversity, shows important roles in plenty of biological processes. O-GlcNAcylations with abnormal expression levels are associated with many diseases. Systematically profiling o...

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Autores principales: Yin, Ruoting, Wang, Xin, Li, Cheng, Gou, Yuhan, Ma, Xuecheng, Liu, Yongzhao, Peng, Jianfang, Wang, Chao, Zhang, Ying
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2021
Materias:
Chemistry
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8685217/
https://www.ncbi.nlm.nih.gov/pubmed/34938717
http://dx.doi.org/10.3389/fchem.2021.737093
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author Yin, Ruoting
Wang, Xin
Li, Cheng
Gou, Yuhan
Ma, Xuecheng
Liu, Yongzhao
Peng, Jianfang
Wang, Chao
Zhang, Ying
author_facet Yin, Ruoting
Wang, Xin
Li, Cheng
Gou, Yuhan
Ma, Xuecheng
Liu, Yongzhao
Peng, Jianfang
Wang, Chao
Zhang, Ying
author_sort Yin, Ruoting
collection PubMed
description O-linked β-N-acetylglucosamine modification (O-GlcNAcylation) at proteins with low-abundance expression level and species diversity, shows important roles in plenty of biological processes. O-GlcNAcylations with abnormal expression levels are associated with many diseases. Systematically profiling of O-GlcNAcylation at qualitative or quantitative level is vital for their function understanding. Recently, the combination of affinity enrichment, metabolic labeling or chemical tagging with mass spectrometry (MS) have made significant contributions to structure-function mechanism elucidating of O-GlcNAcylations in organisms. Herein, this review provides a comprehensive update of MS-based methodologies for quali-quantitative characterization of O-GlcNAcylation.
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spelling pubmed-86852172021-12-21 Mass Spectrometry for O-GlcNAcylation Yin, Ruoting Wang, Xin Li, Cheng Gou, Yuhan Ma, Xuecheng Liu, Yongzhao Peng, Jianfang Wang, Chao Zhang, Ying Front Chem Chemistry O-linked β-N-acetylglucosamine modification (O-GlcNAcylation) at proteins with low-abundance expression level and species diversity, shows important roles in plenty of biological processes. O-GlcNAcylations with abnormal expression levels are associated with many diseases. Systematically profiling of O-GlcNAcylation at qualitative or quantitative level is vital for their function understanding. Recently, the combination of affinity enrichment, metabolic labeling or chemical tagging with mass spectrometry (MS) have made significant contributions to structure-function mechanism elucidating of O-GlcNAcylations in organisms. Herein, this review provides a comprehensive update of MS-based methodologies for quali-quantitative characterization of O-GlcNAcylation. Frontiers Media S.A. 2021-12-06 /pmc/articles/PMC8685217/ /pubmed/34938717 http://dx.doi.org/10.3389/fchem.2021.737093 Text en Copyright © 2021 Yin, Wang, Li, Gou, Ma, Liu, Peng, Wang and Zhang. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Chemistry
Yin, Ruoting
Wang, Xin
Li, Cheng
Gou, Yuhan
Ma, Xuecheng
Liu, Yongzhao
Peng, Jianfang
Wang, Chao
Zhang, Ying
Mass Spectrometry for O-GlcNAcylation
title Mass Spectrometry for O-GlcNAcylation
title_full Mass Spectrometry for O-GlcNAcylation
title_fullStr Mass Spectrometry for O-GlcNAcylation
title_full_unstemmed Mass Spectrometry for O-GlcNAcylation
title_short Mass Spectrometry for O-GlcNAcylation
title_sort mass spectrometry for o-glcnacylation
topic Chemistry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8685217/
https://www.ncbi.nlm.nih.gov/pubmed/34938717
http://dx.doi.org/10.3389/fchem.2021.737093
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