Morphological changes in diabetic kidney are associated with increased O-GlcNAcylation of cytoskeletal proteins including α-actinin 4-Reference-Cited by-同舟云学术

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Morphological changes in diabetic kidney are associated with increased O-GlcNAcylation of cytoskeletal proteins including α-actinin 4

Published:2011-09-21 Issue:1 Volume:8 Page:
ISSN:1542-6416
Container-title:Clinical Proteomics
language:en
Short-container-title:Clin Proteom

Author:

Akimoto Yoshihiro,Miura Yuri,Toda Tosifusa,Wolfert Margreet A,Wells Lance,Boons Geert-Jan,Hart Gerald W,Endo Tamao,Kawakami Hayato

Publisher

Springer Science and Business Media LLC

Subject

Clinical Biochemistry,Molecular Biology,Molecular Medicine,Clinical Biochemistry,Molecular Biology,Molecular Medicine

Link

http://link.springer.com/content/pdf/10.1186/1559-0275-8-15.pdf

Reference41 articles.

1. Wells L, Vosseller K, Hart GW: Glycosylation of nucleocytoplasmic proteins: signal transduction and O-GlcNAc. Science. 2001, 291: 2376-2378. 10.1126/science.1058714

2. Hart GW, Housley MP, Slawson C: Cycling of O-linked β-N-acetylglucosamine on nucleocytoplasmic proteins. Nature. 2007, 446: 1017-1022. 10.1038/nature05815

3. Butkinaree C, Park K, Hart GW: O-linked β-N-acetylglucosamine (O-GlcNAc): Extensive crosstalk with phosphorylation to regulate signaling and transcription in response to nutrients and stress. Biochim Biophys Acta. 2010, 1800: 96-106.

4. Yang X, Ongusaha PP, Miles PD: Phosphoinositide signaling links O-GlcNAc transferase to insulin resistance. Nature. 2008, 451: 964-969. 10.1038/nature06668

5. Teo CF, Wollaston-Hayden EE, Wells L: Hexosamine flux, the O-GlcNAc modification, and the development of insulin resistance in adipocytes. Mol Cell Endocrinol. 2010, 318: 44-53. 10.1016/j.mce.2009.09.022

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