Reversible oxidation of the membrane distal domain of receptor PTPalpha is mediated by a cyclic sulfenamide. - Wikidata - wikimedia - TriplyDB

Reversible oxidation of the membrane distal domain of receptor PTPalpha is mediated by a cyclic sulfenamide.

Reversible oxidation of the membrane distal domain of receptor PTPalpha is mediated by a cyclic sulfenamide.

http://www.wikidata.org/entity/Q33269246

about

Reactivation of oxidized PTP1B and PTEN by thioredoxin 1 Cellular biochemistry methods for investigating protein tyrosine phosphatases Effect of ionic strength and oxidation on the P-loop conformation of the protein tyrosine phosphatase-like phytase, PhyAsr Crystal Structure of the Human Lymphoid Tyrosine Phosphatase Catalytic Domain: Insights into Redox Regulation,Crystal structure of the yeast Sac1: implications for its phosphoinositide phosphatase function Vascular Bioactivation of Nitroglycerin by Aldehyde Dehydrogenase-2: REACTION INTERMEDIATES REVEALED BY CRYSTALLOGRAPHY AND MASS SPECTROMETRY Structure of the catalytic domain of protein tyrosine phosphatase sigma in the sulfenic acid form The family-wide structure and function of human dual-specificity protein phosphatases Structure of the catalytic phosphatase domain of MTMR8: implications for dimerization, membrane association and reversible oxidation A Drosophila-centric view of protein tyrosine phosphatases Redox regulation of dimerization of the receptor protein-tyrosine phosphatases RPTPalpha, LAR, RPTPmu and CD45 Reactive oxygen species (ROS) homeostasis and redox regulation in cellular signaling Thiol redox biochemistry: insights from computer simulations Thiol-based redox switches Protection of a single-cysteine redox switch from oxidative destruction: On the functional role of sulfenyl amide formation in the redox-regulated enzyme PTP1B.Glutathione peroxidase's reaction intermediate selenenic acid is stabilized by the protein microenvironment.Striatal-enriched protein tyrosine phosphatase regulates the PTPα/Fyn signaling pathway Cysteine-based redox switches in enzymes Cysteine-mediated redox signaling: chemistry, biology, and tools for discovery Protein topology determines cysteine oxidation fate: the case of sulfenyl amide formation among protein families.Does the Transcription Factor NemR Use a Regulatory Sulfenamide Bond to Sense Bleach?Methods to monitor classical protein-tyrosine phosphatase oxidation.The core cysteines, (C909) of islet antigen-2 and (C945) of islet antigen-2β, are crucial to autoantibody binding in type 1 diabetes.Discovering mechanisms of signaling-mediated cysteine oxidation.A modified cysteinyl-labeling assay reveals reversible oxidation of protein tyrosine phosphatases in angiomyolipoma cells.An immunochemical approach to detect oxidized protein tyrosine phosphatases using a selective C-nucleophile tag Protein tyrosine phosphatases: regulatory mechanisms.Protein tyrosine phosphatases: structure-function relationships.Molecular basis for the resistance of human mitochondrial 2-Cys peroxiredoxin 3 to hyperoxidation Thiol-based redox switches in eukaryotic proteins.Receptor protein-tyrosine phosphatase α regulates focal adhesion kinase phosphorylation and ErbB2 oncoprotein-mediated mammary epithelial cell motility.Orchestrating redox signaling networks through regulatory cysteine switches.Targeting the reversibly oxidized protein tyrosine phosphatase superfamily.Regulation of protein tyrosine phosphatases by reversible oxidation.Protein tyrosine phosphatase structure-function relationships in regulation and pathogenesis.Cysteine-mediated redox signalling in the mitochondria.Chemical approaches to discovery and study of sources and targets of hydrogen peroxide redox signaling through NADPH oxidase proteins.Altered Met Receptor Phosphorylation and LRP1 Mediated Uptake in Cells Lacking Carbohydrate-Dependent Lysosomal Targeting.Serine dephosphorylation of receptor protein tyrosine phosphatase alpha in mitosis induces Src binding and activation.The NADPH Oxidases DUOX1 and NOX2 Play Distinct Roles in Redox Regulation of Epidermal Growth Factor Receptor Signaling.

P2860

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P2860

Reversible oxidation of the membrane distal domain of receptor PTPalpha is mediated by a cyclic sulfenamide.

http://www.wikidata.org/entity/Q33269246

description

2007 nî lūn-bûn

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2007 թուականի Յունուարին հրատարակուած գիտական յօդուած

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2007 թվականի հունվարին հրատարակված գիտական հոդված

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2007年の論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年论文

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name

Reversible oxidation of the me ...... iated by a cyclic sulfenamide.

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Reversible oxidation of the me ...... iated by a cyclic sulfenamide.

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Reversible oxidation of the me ...... iated by a cyclic sulfenamide.

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type

label

Reversible oxidation of the me ...... iated by a cyclic sulfenamide.

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Reversible oxidation of the me ...... iated by a cyclic sulfenamide.

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Reversible oxidation of the me ...... iated by a cyclic sulfenamide.

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prefLabel

Reversible oxidation of the me ...... iated by a cyclic sulfenamide.

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Reversible oxidation of the me ...... iated by a cyclic sulfenamide.

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Reversible oxidation of the me ...... iated by a cyclic sulfenamide.

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Anne Jans

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Arnoud Groen

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David Barford

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Jeroen den Hertog

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Jing Yang

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Monique Slijper

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S Mark Roe

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Simone Lemeer

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709-719

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scholarly article

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10.1021/BI061546M

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3

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46

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17223692

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