Regulation of insulin signaling through reversible oxidation of the protein-tyrosine phosphatases TC45 and PTP1B. (Q44932599)

7 December 2017

Regulation of insulin signaling through reversible oxidation of the protein-tyrosine phosphatases TC45 and PTP1B. (English)

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7 December 2017

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7 December 2017

Sandra Galic

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author name string

Tzu-Ching Meng

series ordinal

1

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7 December 2017

Deirdre A Buckley

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2

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7 December 2017

Nicholas K Tonks

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5

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7 December 2017

language of work or name

English

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publication date

10 June 2004

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Journal of Biological Chemistry

7 December 2017

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7 December 2017

279

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7 December 2017

36

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7 December 2017

37716-37725

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Signaling--2000 and beyond

7 December 2017

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https://api.crossref.org/works/10.1074%2FJBC.M404606200

Protein tyrosine phosphatases in signal transduction.

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Insulin signaling pathways in time and space.

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Structural and evolutionary relationships among protein tyrosine phosphatase domains

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A genomic perspective on protein tyrosine phosphatases: gene structure, pseudogenes, and genetic disease linkage

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'Zip codes' direct intracellular protein tyrosine phosphatases to the correct cellular 'address'.

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Combinatorial control of the specificity of protein tyrosine phosphatases

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Oxidant signals and oxidative stress

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NOX enzymes and the biology of reactive oxygen

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Active site labeling of the Yersinia protein tyrosine phosphatase: the determination of the pKa of the active site cysteine and the function of the conserved histidine 402.

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Reversible inactivation of protein-tyrosine phosphatase 1B in A431 cells stimulated with epidermal growth factor

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Reversible inactivation of the tumor suppressor PTEN by H2O2

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Reversible oxidation and inactivation of protein tyrosine phosphatases in vivo

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Redox regulation of Cdc25C.

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Insulin-stimulated hydrogen peroxide reversibly inhibits protein-tyrosine phosphatase 1b in vivo and enhances the early insulin action cascade

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Two vicinal cysteines confer a peculiar redox regulation to low molecular weight protein tyrosine phosphatase in response to platelet-derived growth factor receptor stimulation

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In vivo analysis of the RNA interference mechanism in Trypanosoma brucei.

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Role of Akt/protein kinase B in metabolism.

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Focal adhesion kinase (FAK) regulates insulin-stimulated glycogen synthesis in hepatocytes

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Development of "substrate-trapping" mutants to identify physiological substrates of protein tyrosine phosphatases

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Imaging sites of receptor dephosphorylation by PTP1B on the surface of the endoplasmic reticulum

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Autophosphorylation of the two C-terminal tyrosine residues Tyr1316 and Tyr1322 modulates the activity of the insulin receptor kinase in vitro

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Molecular basis of phosphorylation-induced activation of the NADPH oxidase

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NOXO1, Regulation of Lipid Binding, Localization, and Activation of Nox1 by the Phox Homology (PX) Domain

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Protein-tyrosine phosphatases: biological function, structural characteristics, and mechanism of catalysis

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Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate

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Preferential oxidation of the second phosphatase domain of receptor-like PTP-alpha revealed by an antibody against oxidized protein tyrosine phosphatases

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Redox-regulated rotational coupling of receptor protein-tyrosine phosphatase alpha dimers

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Abnormal mesoderm patterning in mouse embryos mutant for the SH2 tyrosine phosphatase Shp-2.

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A major health hazard: the metabolic syndrome

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Coordinated action of protein tyrosine phosphatases in insulin signal transduction

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Increased insulin sensitivity and obesity resistance in mice lacking the protein tyrosine phosphatase-1B gene

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Increased energy expenditure, decreased adiposity, and tissue-specific insulin sensitivity in protein-tyrosine phosphatase 1B-deficient mice

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TYK2 and JAK2 are substrates of protein-tyrosine phosphatase 1B

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PTP1B regulates leptin signal transduction in vivo

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Attenuation of leptin action and regulation of obesity by protein tyrosine phosphatase 1B.

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The NAD(P)H oxidase homolog Nox4 modulates insulin-stimulated generation of H2O2 and plays an integral role in insulin signal transduction

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Cloning and characterization of a mouse cDNA encoding a cytoplasmic protein-tyrosine-phosphatase

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Epidermal growth factor receptor and the adaptor protein p52Shc are specific substrates of T-cell protein tyrosine phosphatase

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The protein-tyrosine phosphatase TCPTP regulates epidermal growth factor receptor-mediated and phosphatidylinositol 3-kinase-dependent signaling

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Regulation of insulin receptor signaling by the protein tyrosine phosphatase TCPTP

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Site-selective regulation of platelet-derived growth factor beta receptor tyrosine phosphorylation by T-cell protein tyrosine phosphatase

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Murine embryonic fibroblasts lacking TC-PTP display delayed G1 phase through defective NF-kappaB activation

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COOH-terminal sequence motifs target the T cell protein tyrosine phosphatase to the ER and nucleus

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Association of PTP-PEST with the SH3 domain of p130cas; a novel mechanism of protein tyrosine phosphatase substrate recognition

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Identifiers

DOI

10.1074/JBC.M404606200

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7 December 2017

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