The Metabolic Chemical Reporter 6-Azido-6-deoxy-glucose Further Reveals the Substrate Promiscuity of O-GlcNAc Transferase and Catalyzes the Discovery of Intracellular Protein Modification by O-Glucose-Reference-Cited by-同舟云学术

The Metabolic Chemical Reporter 6-Azido-6-deoxy-glucose Further Reveals the Substrate Promiscuity of O-GlcNAc Transferase and Catalyzes the Discovery of Intracellular Protein Modification by O-Glucose

Published:2018-05-17 Issue:23 Volume:140 Page:7092-7100
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Darabedian Narek,Gao Jinxu¹,Chuh Kelly N.,Woo Christina M.¹^ORCID,Pratt Matthew R.^ORCID

Affiliation:

1. Department of Chemistry and Chemical Biology, Harvard University, Cambridge, Massachusetts 02138, United States

Funder

Division of Chemistry

National Cancer Institute

Damon Runyon Cancer Research Foundation

Harvard University

Susan G. Komen for the Cure

American Cancer Society

Burroughs Wellcome Fund

National Institute of General Medical Sciences

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/jacs.7b13488

Reference39 articles.

1. A little sugar goes a long way: The cell biology of O-GlcNAc

2. Protein O-GlcNAcylation: emerging mechanisms and functions

3. O-GlcNAc processing enzymes: catalytic mechanisms, substrate specificity, and enzyme regulation

4. The O-GlcNAc transferase gene resides on the X chromosome and is essential for embryonic stem cell viability and mouse ontogeny

5. Ogt -Dependent X-Chromosome-Linked Protein Glycosylation Is a Requisite Modification in Somatic Cell Function and Embryo Viability

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