Recent development of analytical methods for disease-specific protein<i>O</i>-GlcNAcylation

DOI Web Site 1 Citations
  • Wenhua Hu
    Center for Clinical Mass Spectrometry, College of Pharmaceutical Sciences, Soochow University, Suzhou, Jiangsu, 215123, China
  • Guolin Zhang
    Suzhou Institute for Drug Control, Suzhou, Jiangsu, 215104, China
  • 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
  • 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
  • Peng Zhang
    Department of Orthopedics, The Second Affiliated Hospital of Soochow University, Suzhou, Jiangsu, 215004, China
  • Wenjin Xiao
    Department of Endocrinology, The Second Affiliated Hospital of Soochow University, Suzhou, Jiangsu, 215004, China
  • Man Xue
    Suzhou Institute for Drug Control, Suzhou, Jiangsu, 215104, China
  • Zhaohui Lu
    Health Examination Center, The Second Affiliated Hospital of Soochow University, Suzhou, Jiangsu, 215004, China
  • Shuang Yang
    Center for Clinical Mass Spectrometry, College of Pharmaceutical Sciences, Soochow University, Suzhou, Jiangsu, 215123, China

Abstract

<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>

Journal

  • RSC Advances

    RSC Advances 13 (1), 264-280, 2023

    Royal Society of Chemistry (RSC)

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