Probing the molecular basis for potent and selective protein-tyrosine phosphatase 1B inhibition (Q44112967)

29 November 2017

Probing the molecular basis for potent and selective protein-tyrosine phosphatase 1B inhibition (English)

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29 November 2017

Xiao-Ling Guo

1

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29 November 2017

Kui Shen

2

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29 November 2017

Fang Wang

3

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29 November 2017

David S Lawrence

4

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29 November 2017

Zhong-Yin Zhang

5

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29 November 2017

language of work or name

English

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publication date

21 August 2002

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Journal of Biological Chemistry

29 November 2017

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29 November 2017

277

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29 November 2017

43

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29 November 2017

41014-41022

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Signaling--2000 and beyond

29 November 2017

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https://api.crossref.org/works/10.1074%2FJBC.M207347200

Protein tyrosine phosphatases: prospects for therapeutics

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Initial sequencing and analysis of the human genome

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Protein tyrosine phosphatases: structure and function, substrate specificity, and inhibitor development

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Substrate specificity of the protein tyrosine phosphatases

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Protein tyrosine phosphatase substrate specificity: size and phosphotyrosine positioning requirements in peptide substrates

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Structural basis for phosphotyrosine peptide recognition by protein tyrosine phosphatase 1B

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Structural basis of plasticity in protein tyrosine phosphatase 1B substrate recognition

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Identification of a second aryl phosphate-binding site in protein-tyrosine phosphatase 1B: a paradigm for inhibitor design

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Acquisition of a specific and potent PTP1B inhibitor from a novel combinatorial library and screening procedure

21 January 2018

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Molecular basis for substrate specificity of protein-tyrosine phosphatase 1B.

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A continuous spectrophotometric and fluorimetric assay for protein tyrosine phosphatase using phosphotyrosine-containing peptides

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Conformational and dynamic changes of Yersinia protein tyrosine phosphatase induced by ligand binding and active site mutation and revealed by H/D exchange and electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry

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Osmotic loading of neutralizing antibodies demonstrates a role for protein-tyrosine phosphatase 1B in negative regulation of the insulin action pathway

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Protein-tyrosine phosphatase 1B is a negative regulator of insulin- and insulin-like growth factor-I-stimulated signaling

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Protein-tyrosine phosphatase 1B complexes with the insulin receptor in vivo and is tyrosine-phosphorylated in the presence of insulin

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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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Identification of protein-tyrosine phosphatase 1B as the major tyrosine phosphatase activity capable of dephosphorylating and activating c-Src in several human breast cancer cell lines

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Protein tyrosine phosphatase 1B interacts with and is tyrosine phosphorylated by the epidermal growth factor receptor

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

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Protein tyrosine phosphatase 1B antagonizes signalling by oncoprotein tyrosine kinase p210 bcr-abl in vivo

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The nonreceptor protein tyrosine phosphatase PTP1B binds to the cytoplasmic domain of N-cadherin and regulates the cadherin-actin linkage

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Direct binding of the proline-rich region of protein tyrosine phosphatase 1B to the Src homology 3 domain of p130(Cas)

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Hydrogen exchange/electrospray ionization mass spectrometry studies of substrate and inhibitor binding and conformational changes of Escherichia coli dihydrodipicolinate reductase

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Identification of protein-protein interfaces by decreased amide proton solvent accessibility

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Applications of mass spectrometry to signal transduction

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The Cys(X)5Arg catalytic motif in phosphoester hydrolysis

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Visualization of the cysteinyl-phosphate intermediate of a protein-tyrosine phosphatase by x-ray crystallography

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Altering the nucleophile specificity of a protein-tyrosine phosphatase-catalyzed reaction. Probing the function of the invariant glutamine residues

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Is the PTPase-vanadate complex a true transition state analogue?

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Steric hindrance as a basis for structure-based design of selective inhibitors of protein-tyrosine phosphatases

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Residue 259 is a key determinant of substrate specificity of protein-tyrosine phosphatases 1B and alpha

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Protein-tyrosine phosphatases: structure, mechanism, and inhibitor discovery

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Comparative kinetic analysis and substrate specificity of the tandem catalytic domains of the receptor-like protein-tyrosine phosphatase alpha

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Assessment of protein-tyrosine phosphatase 1B substrate specificity using "inverse alanine scanning"

21 January 2018

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Potent and highly selective inhibitors of the protein tyrosine phosphatase 1B

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Overexpression of the protein tyrosine phosphatase PTP1B in human breast cancer: association with p185c-erbB-2 protein expression

21 January 2018

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Mechanism of inhibition of protein-tyrosine phosphatases by vanadate and pervanadate

21 January 2018

1 reference

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21 January 2018

Identifiers

DOI

10.1074/JBC.M207347200

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29 November 2017

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