Sulfoconjugation of protein peptides and glycoproteins in physiology and diseases

Xu, Pengfei; Cai, Xinran; Guan, Xiuchen; Xie, Wen

doi:10.1016/j.pharmthera.2023.108540

Cited by 3 publications

(3 citation statements)

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“…Hence, the identification and understanding of PTMs are crucial for studies in cellular biology, disease treatment, and prevention. [2][3][4][5] Therefore, recognizing and comprehending PTMs is vital in the research of cellular biology and the management and prevention of diseases. 6 Protein glycosylation, the modification of proteins via carbohydrates, is among the most prevalent PTMs across all cells and organisms.…”

Section: Introductionmentioning

confidence: 99%

“…Posttranslational modifications (PTMs) confer functional diversity to the proteome by modulating their molecular composition, 1 which includes phosphorylcholination, glycosylation, ubiquitination, lipidation, methylation, N‐acetylation, and S‐palmitoylation, impact nearly every aspect of normal cell physiology and pathology. Hence, the identification and understanding of PTMs are crucial for studies in cellular biology, disease treatment, and prevention 2–5 . Therefore, recognizing and comprehending PTMs is vital in the research of cellular biology and the management and prevention of diseases 6 …”

Section: Introductionmentioning

confidence: 99%

“…Hence, the identification and understanding of PTMs are crucial for studies in cellular biology, disease treatment, and prevention. 2 , 3 , 4 , 5 Therefore, recognizing and comprehending PTMs is vital in the research of cellular biology and the management and prevention of diseases. 6 …”

Section: Introductionmentioning

confidence: 99%

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O‐GlcNAcylation: cellular physiology and therapeutic target for human diseases

Ye,

Ding,

Xiao

et al. 2023

MedComm

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O‐linked‐β‐N‐acetylglucosamine (O‐GlcNAcylation) is a distinctive posttranslational protein modification involving the coordinated action of O‐GlcNAc transferase and O‐GlcNAcase, primarily targeting serine or threonine residues in various proteins. This modification impacts protein functionality, influencing stability, protein–protein interactions, and localization. Its interaction with other modifications such as phosphorylation and ubiquitination is becoming increasingly evident. Dysregulation of O‐GlcNAcylation is associated with numerous human diseases, including diabetes, nervous system degeneration, and cancers. This review extensively explores the regulatory mechanisms of O‐GlcNAcylation, its effects on cellular physiology, and its role in the pathogenesis of diseases. It examines the implications of aberrant O‐GlcNAcylation in diabetes and tumorigenesis, highlighting novel insights into its potential role in cardiovascular diseases. The review also discusses the interplay of O‐GlcNAcylation with other protein modifications and its impact on cell growth and metabolism. By synthesizing current research, this review elucidates the multifaceted roles of O‐GlcNAcylation, providing a comprehensive reference for future studies. It underscores the potential of targeting the O‐GlcNAcylation cycle in developing novel therapeutic strategies for various pathologies.

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