Glutathione Transferase Superfamily Behaves Like Storage Proteins for Dinitrosyl-Diglutathionyl-Iron Complex in Heterogeneous Systems-Reference-Cited by-同舟云学术

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Glutathione Transferase Superfamily Behaves Like Storage Proteins for Dinitrosyl-Diglutathionyl-Iron Complex in Heterogeneous Systems

Published:2003-10 Issue:43 Volume:278 Page:42294-42299
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Turella Paola,Pedersen Jens Z.,Caccuri Anna Maria,De Maria Francesca,Mastroberardino Piergiorgio,Bello Mario Lo,Federici Giorgio,Ricci Giorgio

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference15 articles.

1. The Specific Interaction of Dinitrosyl-Diglutathionyl-Iron Complex, a Natural NO Carrier, with the Glutathione Transferase Superfamily

2. Mass spectrometric analysis of rat liver cytosolic glutathione S-transferases: modifications are limited to N-terminal processing

3. Human Glutathione Transferase P1-1 and Nitric Oxide Carriers

4. Mechanism of Nitric Oxide Release from S-Nitrosothiols

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2. Mechanistic and Kinetic Insights into Cellular Uptake of Biomimetic Dinitrosyl Iron Complexes and Intracellular Delivery of NO for Activation of Cytoprotective HO-1;JACS Au;2024-03-29

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4. Structural insights into the interactions of glutathione transferases with a nitric oxide carrier and sodium nitroprusside;Biochemical and Biophysical Research Communications;2023-03

5. The good Samaritan glutathione-S-transferase P1: An evolving relationship in nitric oxide metabolism mediated by the direct interactions between multiple effector molecules;Redox Biology;2023-02

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