Structure–Activity Relationships of Potent, Targeted Covalent Inhibitors That Abolish Both the Transamidation and GTP Binding Activities of Human Tissue Transglutaminase-Reference-Cited by-同舟云学术

Structure–Activity Relationships of Potent, Targeted Covalent Inhibitors That Abolish Both the Transamidation and GTP Binding Activities of Human Tissue Transglutaminase

Published:2017-09-14 Issue:18 Volume:60 Page:7910-7927
ISSN:0022-2623
Container-title:Journal of Medicinal Chemistry
language:en
Short-container-title:J. Med. Chem.

Author:

Akbar Abdullah¹,McNeil Nicole M. R.¹,Albert Marie R.¹,Ta Viviane¹,Adhikary Gautam²,Bourgeois Karine¹,Eckert Richard L.²,Keillor Jeffrey W.¹^ORCID

Affiliation:

1. Department of Chemistry and Biomolecular Sciences, University of Ottawa, 10 Marie-Curie, Ottawa, Ontario K1N 6N5, Canada

2. Department of Biochemistry and Molecular Biology, University of Maryland School of Medicine, Baltimore, Maryland 21201, United States

Funder

University of Ottawa

Natural Sciences and Engineering Research Council of Canada

Publisher

American Chemical Society (ACS)

Subject

Drug Discovery,Molecular Medicine

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.jmedchem.7b01070

Reference72 articles.

1. Transglutaminase 2: A molecular Swiss army knife

2. Transglutaminase Regulation of Cell Function

3. Tissue transglutaminase: an enzyme with a split personality

4. Opposite Effects of Ca2+ and GTP Binding on Tissue Transglutaminase Tertiary Structure

5. Regulation of the activities of the mammalian transglutaminase family of enzymes

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