Cross-Linking Protein Glutathionylation Mediated by O2-Arylated Bis-Diazeniumdiolate “Double JS-K”-Reference-Cited by-同舟云学术

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Cross-Linking Protein Glutathionylation Mediated by O2-Arylated Bis-Diazeniumdiolate “Double JS-K”

Published:2012-11-09 Issue:12 Volume:25 Page:2670-2677
ISSN:0893-228X
Container-title:Chemical Research in Toxicology
language:en
Short-container-title:Chem. Res. Toxicol.

Author:

Holland Ryan J.¹,Maciag Anna E.²,Kumar Varun³,Shi Lei³,Saavedra Joseph E.²,Prud'homme Robert K.³,Chakrapani Harinath⁴,Keefer Larry K.¹

Affiliation:

1. Chemical Biology Laboratory, Frederick National Laboratory for Cancer Research, Frederick, Maryland 21702, United States

2. Basic Science Program, SAIC-Frederick, Frederick National Laboratory for Cancer Research, Frederick, Maryland 21702, United States

3. Department of Chemical and Biological Engineering, Princeton University, Princeton, New Jersey 08544, United States

4. Indian Institute of Science Education and Research, Pune 411008, India

Publisher

American Chemical Society (ACS)

Subject

Toxicology,General Medicine

Link

https://pubs.acs.org/doi/pdf/10.1021/tx3003142

Reference22 articles.

1. S-Glutathionylation: From Molecular Mechanisms to Health Outcomes

2. Molecular Mechanisms and Clinical Implications of Reversible ProteinS-Glutathionylation

3. Antitumor Activity of JS-K [O2-(2,4-Dinitrophenyl) 1-[(4-Ethoxycarbonyl)piperazin-1-yl]diazen-1-ium-1,2-diolate] and Related O2-Aryl Diazeniumdiolates in Vitro and in Vivo

4. JS-K, a GST-activated nitric oxide generator, induces DNA double-strand breaks, activates DNA damage response pathways, and induces apoptosis in vitro and in vivo in human multiple myeloma cells

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