Recent development of analytical methods for disease-specific protein<i>O</i>-GlcNAcylation
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- Wenhua Hu
- Center for Clinical Mass Spectrometry, College of Pharmaceutical Sciences, Soochow University, Suzhou, Jiangsu, 215123, China
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- Guolin Zhang
- Suzhou Institute for Drug Control, Suzhou, Jiangsu, 215104, China
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- Yu Zhou
- Laboratory Medicine Center, Department of Clinical Laboratory, Zhejiang Provincial People's Hospital, Affiliated People's Hospital, Hangzhou Medical College, Hangzhou, Zhejiang, 310014, China
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- Jun Xia
- Laboratory Medicine Center, Department of Clinical Laboratory, Zhejiang Provincial People's Hospital, Affiliated People's Hospital, Hangzhou Medical College, Hangzhou, Zhejiang, 310014, China
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- Peng Zhang
- Department of Orthopedics, The Second Affiliated Hospital of Soochow University, Suzhou, Jiangsu, 215004, China
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- Wenjin Xiao
- Department of Endocrinology, The Second Affiliated Hospital of Soochow University, Suzhou, Jiangsu, 215004, China
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- Man Xue
- Suzhou Institute for Drug Control, Suzhou, Jiangsu, 215104, China
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- Zhaohui Lu
- Health Examination Center, The Second Affiliated Hospital of Soochow University, Suzhou, Jiangsu, 215004, China
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- Shuang Yang
- Center for Clinical Mass Spectrometry, College of Pharmaceutical Sciences, Soochow University, Suzhou, Jiangsu, 215123, China
抄録
<jats:p>The enzymatic modification of protein serine or threonine residues by<jats:italic>N</jats:italic>-acetylglucosamine, namely<jats:italic>O</jats:italic>-GlcNAcylation, is a ubiquitous post-translational modification that frequently occurs in the nucleus and cytoplasm.</jats:p>
収録刊行物
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- RSC Advances
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RSC Advances 13 (1), 264-280, 2023
Royal Society of Chemistry (RSC)