Analysis of transition state mimicry by tight binding aminothiazoline inhibitors provides insight into catalysis by human O-GlcNAcase-Reference-Cited by-同舟云学术

Analysis of transition state mimicry by tight binding aminothiazoline inhibitors provides insight into catalysis by human O-GlcNAcase

Published:2016 Issue:6 Volume:7 Page:3742-3750
ISSN:2041-6520
Container-title:Chemical Science
language:en
Short-container-title:Chem. Sci.

Author:

Cekic N.¹²³⁴,Heinonen J. E.¹²³⁴,Stubbs K. A.¹²³⁴⁵,Roth C.⁶¹⁷⁸^ORCID,He Y.⁶¹⁷⁸,Bennet A. J.¹²³⁴,McEachern E. J.¹²³⁴,Davies G. J.⁶¹⁷⁸^ORCID,Vocadlo D. J.¹²³⁴⁹

Affiliation:

1. Department of Chemistry

2. Simon Fraser University

3. Burnaby

4. Canada

5. School of Chemistry and Biochemistry

6. York Structural Biology Laboratory

7. The University of York

8. UK

9. Department of Molecular Biology and Biochemistry

Abstract

2′-Aminothiazoline inhibitors of human OGA are tight binding transition state mimics for which binding depends on inhibitor pK_a.

Funder

Natural Sciences and Engineering Research Council of Canada

Institute of Aging

Michael Smith Foundation for Health Research

Biotechnology and Biological Sciences Research Council

Genome British Columbia

Brain Canada

Canada Research Chairs

Publisher

Royal Society of Chemistry (RSC)

Subject

General Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2016/SC/C6SC00370B

Reference57 articles.

1. Exploring the O-GlcNAc proteome: Direct identification of O-GlcNAc-modified proteins from the brain

2. Proteomic Approaches to Analyze the Dynamic Relationships Between Nucleocytoplasmic Protein Glycosylation and Phosphorylation

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4. Three Decades of Research on O-GlcNAcylation â€“ A Major Nutrient Sensor That Regulates Signaling, Transcription and Cellular Metabolism

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