Insights into BAY 60-2770 Activation and S-Nitrosylation-Dependent Desensitization of Soluble Guanylyl Cyclase via Crystal Structures of Homologous Nostoc H-NOX Domain Complexes-Reference-Cited by-同舟云学术

Insights into BAY 60-2770 Activation and S-Nitrosylation-Dependent Desensitization of Soluble Guanylyl Cyclase via Crystal Structures of Homologous Nostoc H-NOX Domain Complexes

Published:2013-05-07 Issue:20 Volume:52 Page:3601-3608
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Kumar Vijay¹,Martin Faye¹,Hahn Michael G.²,Schaefer Martina²,Stamler Jonathan S.³,Stasch Johannes-Peter²,van den Akker Focco¹

Affiliation:

1. Department of Biochemistry, Case Western Reserve University, Cleveland, Ohio 44106, United States

2. Pharma Research Center, Bayer Pharma AG, Wuppertal D-42096, Germany

3. Department of Medicine and Institute for Transformative Molecular Medicine, Case Western Reserve University and University Hospitals Case Medical Center, Cleveland, Ohio 44106, United States

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi301657w

Reference52 articles.

1. Isolation of adenosine 3′,5′-monophosphate and guanosine 3′,5′-monophosphate from rat urine

2. Identification of Residues in the Heme Domain of Soluble Guanylyl Cyclase that are Important for Basal and Stimulated Catalytic Activity

3. Bildung von cyclischem Guanosin-3′,5′-monophosphat in verschiedenen Geweben der Ratte

4. Nitric oxide signaling: no longer simply on or off

5. Crystal Structure of the S-Nitroso Form of Liganded Human Hemoglobin,

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