Journal ArticleDOI
The role of cysteine residues as redox-sensitive regulatory switches.
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TLDR
A variety of proteins, including transcription factors, molecular chaperones and protein tyrosine phosphatases, are regulated via redox processes, and common mechanisms underlie the sensitivity of cysteines to redox, such as proximity to polar and charged groups.About:
This article is published in Current Opinion in Structural Biology.The article was published on 2004-12-01. It has received 315 citations till now. The article focuses on the topics: Protein tyrosine phosphatase & Cysteine.read more
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The NOX Family of ROS-Generating NADPH Oxidases: Physiology and Pathophysiology
Karen Bedard,Karl-Heinz Krause +1 more
TL;DR: This review summarizes the current state of knowledge of the functions of NOX enzymes in physiology and pathology.
Journal ArticleDOI
A dynamic pathway for calcium-independent activation of CaMKII by methionine oxidation
Jeffrey R. Erickson,Mei Ling A. Joiner,Xiaoqun Guan,William Kutschke,Jinying Yang,Carmine V. Oddis,Ryan K. Bartlett,John S. Lowe,Susan E. O'Donnell,Nukhet Aykin-Burns,Matthew C. Zimmerman,Kathy Zimmerman,Amy-Joan L. Ham,Robert M. Weiss,Douglas R. Spitz,Madeline A. Shea,Roger J. Colbran,Peter J. Mohler,Mark E. Anderson +18 more
TL;DR: It is shown that oxidation of paired regulatory domain methionine residues sustains CaMKII activity in the absence of Ca2+/CaM and highlights the critical importance of oxidation-dependent CaMK II activation to AngII and ischemic myocardial apoptosis.
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Nox proteins in signal transduction
TL;DR: This review will discuss recent literature on Nox protein tissue distribution, subcellular localization, activation, and the resulting signal transduction mechanisms.
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Nitric oxide and redox mechanisms in the immune response
David A. Wink,Harry B. Hines,Robert Y.S. Cheng,Christopher H. Switzer,Wilmarie Flores-Santana,Michael P. Vitek,Lisa A. Ridnour,Carol A. Colton +7 more
TL;DR: The chemistry of NO and ROS in the context of antipathogen activity and immune regulation is discussed and similarities and differences between murine and human production of these intermediates are discussed.
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Hydrogen peroxide: a Jekyll and Hyde signalling molecule
David R. Gough,Thomas G. Cotter +1 more
TL;DR: This work examines the factors and circumstances that determine whether H2O2 acts in a pro-survival or deleterious manner, and reveals that the diverse functions of ROS can be determined by the subcellular source, location and duration of these molecules within the cell.
References
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Structure, mechanism and regulation of peroxiredoxins
TL;DR: Using crystal structures, a detailed catalytic cycle has been derived for typical 2-Cys Prxs, including a model for the redox-regulated oligomeric state proposed to control enzyme activity.
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Protein Tyrosine Phosphatases in the Human Genome
Andres Alonso,Joanna Sasin,Nunzio Bottini,Ilan Friedberg,Iddo Friedberg,Andrei L. Osterman,Adam Godzik,Tony Hunter,Jack E. Dixon,Tomas Mustelin +9 more
TL;DR: The set of 107 genes in the human genome that encode members of the four protein tyrosine phosphatase (PTP) families are presented and the role of these enzymes in human disease will be discussed.
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Oxidant signals and oxidative stress.
TL;DR: These new studies have significantly altered the authors' understanding of how reactive oxygen species participate in diverse processes from tumourigenesis to ageing.
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Peroxiredoxin Evolution and the Regulation of Hydrogen Peroxide Signaling
TL;DR: It is suggested that this adaptation allows 2-Cys Prxs to act as floodgates, keeping resting levels of hydrogen peroxide low, while permitting higher levels during signal transduction, and is proposed to be the structural origins of sensitivity.
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Epidermal Growth Factor (EGF)-induced Generation of Hydrogen Peroxide ROLE IN EGF RECEPTOR-MEDIATED TYROSINE PHOSPHORYLATION
TL;DR: In this paper, the role of reactive oxygen species (ROS) in epidermal growth factor (EGF) signaling was investigated, and the dependence of H2O2 production on the intrinsic tyrosine kinase activity of the EGF receptor and the autophosphorylation sites located in its COOH-terminal tail was investigated.