O-GlcNAc modification of small heat shock proteins enhances their anti-amyloid chaperone activity-Reference-Cited by-同舟云学术

O-GlcNAc modification of small heat shock proteins enhances their anti-amyloid chaperone activity

Published:2021-03-15 Issue:5 Volume:13 Page:441-450
ISSN:1755-4330
Container-title:Nature Chemistry
language:en
Short-container-title:Nat. Chem.

Author:

Balana Aaron T.^ORCID,Levine Paul M.^ORCID,Craven Timothy W.,Mukherjee Somnath,Pedowitz Nichole J.,Moon Stuart P.,Takahashi Terry T.^ORCID,Becker Christian F. W.^ORCID,Baker David^ORCID,Pratt Matthew R.^ORCID

Funder

Dornsife Chemistry-Biology Interface Training Program

U.S. Department of Health & Human Services | NIH | National Institute of General Medical Sciences

Washington Research Fund

University of Vienna

Anton Burg Foundation

Publisher

Springer Science and Business Media LLC

Subject

General Chemical Engineering,General Chemistry

Link

http://www.nature.com/articles/s41557-021-00648-8.pdf

Reference55 articles.

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2. Wani, W. Y., Chatham, J. C., Darley-Usmar, V., McMahon, L. L. & Zhang, J. O-GlcNAcylation and neurodegeneration. Brain Res. Bull. 133, 80–87 (2017).

3. Wang, A. C., Jensen, E. H., Rexach, J. E., Vinters, H. V. & Hsieh-Wilson, L. C. Loss of O-GlcNAc glycosylation in forebrain excitatory neurons induces neurodegeneration. Proc. Natl Acad. Sci. USA 113, 15120–15125 (2016).

4. Liu, F., Iqbal, K., Grundke-Iqbal, I., Hart, G. & Gong, C. O-GlcNAcylation regulates phosphorylation of tau: a mechanism involved in Alzheimer’s disease. Proc. Natl Acad. Sci. USA 101, 10804–10809 (2004).

5. Liu, F. et al. Reduced O-GlcNAcylation links lower brain glucose metabolism and tau pathology in Alzheimer’s disease. Brain 132, 1820–1832 (2009).

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