Mechanism of Fully Reversible, pH-Sensitive Inhibition of Human Glutamine Synthetase by Tyrosine Nitration-Reference-Cited by-同舟云学术

Mechanism of Fully Reversible, pH-Sensitive Inhibition of Human Glutamine Synthetase by Tyrosine Nitration

Published:2020-06-17 Issue:7 Volume:16 Page:4694-4705
ISSN:1549-9618
Container-title:Journal of Chemical Theory and Computation
language:en
Short-container-title:J. Chem. Theory Comput.

Author:

Frieg Benedikt¹²,Görg Boris³,Qvartskhava Natalia³,Jeitner Thomas⁴,Homeyer Nadine¹,Häussinger Dieter³,Gohlke Holger¹²^ORCID

Affiliation:

1. Institute for Pharmaceutical and Medicinal Chemistry, Heinrich Heine University Düsseldorf, Düsseldorf, Germany

2. John von Neumann Institute for Computing (NIC), Jülich Supercomputing Centre (JSC), and Institute of Biological Information Processing (IBI-7: Structural Biochemistry), Forschungszentrum Jülich GmbH, Jülich, Germany

3. Clinic for Gastroenterology, Hepatology, and Infectious Diseases, Heinrich Heine University Düsseldorf, Düsseldorf, Germany

4. Department of Biochemistry and Molecular Biology, New York Medical College, Valhalla, New York 10595, United States

Funder

Deutsche Forschungsgemeinschaft

Publisher

American Chemical Society (ACS)

Subject

Physical and Theoretical Chemistry,Computer Science Applications

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.jctc.0c00249

Reference69 articles.

1. [27] Glutamine synthetase from mammalian tissues

2. Crystal Structures of Mammalian Glutamine Synthetases Illustrate Substrate-Induced Conformational Changes and Provide Opportunities for Drug and Herbicide Design

3. Glutamine Synthetase: Glial Localization in Brain

4. Glutamate-glutamine Cycling in the Epileptic Human Hippocampus

5. Hepatocyte Heterogeneity in Glutamine and Ammonia Metabolism and the Role of an Intercellular Glutamine Cycle during Ureogenesis in Perfused Rat Liver

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