(Q27621646)

1

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L F Iversen

2

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C B Jeppesen

3

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S Branner

4

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K Norris

5

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H B Rasmussen

6

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K B Møller

7

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N P Møller

Journal of Biological Chemistry

8

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language of work or name

English

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publication date

10 March 2000

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published in

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volume

275

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issue

10

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page(s)

7101-8

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cites work

Protein tyrosine phosphatases: a diverse family of intracellular and transmembrane enzymes

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The Croonian Lecture 1997. The phosphorylation of proteins on tyrosine: its role in cell growth and disease

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Protein tyrosine phosphatases take off.

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Structure and function of the protein tyrosine phosphatases

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

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Tiludronate inhibits protein tyrosine phosphatase activity in osteoclasts.

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Protein-tyrosine phosphatase activity regulates osteoclast formation and function: inhibition by alendronate

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Crystal structure of human protein tyrosine phosphatase 1B

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Cloning of a cDNA for a major human protein-tyrosine-phosphatase

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A protein-tyrosine phosphatase with sequence similarity to the SH2 domain of the protein-tyrosine kinases

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Expression, purification and crystallization of human phosphotyrosine phosphatase 1B.

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Processing of X-ray diffraction data collected in oscillation mode

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The CCP4 suite: programs for protein crystallography

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AMoRe: an automated package for molecular replacement

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

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Phosphonate inhibitors of protein-tyrosine and serine/threonine phosphatases

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Structural basis for inhibition of the protein tyrosine phosphatase 1B by phosphotyrosine peptide mimetics

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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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Crystal structure of Yersinia protein tyrosine phosphatase at 2.5 A and the complex with tungstate

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Dissecting the catalytic mechanism of protein-tyrosine phosphatases

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Inhibition of protein tyrosine phosphatases PTP1B and CD45 by sulfotyrosyl peptides

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Thiophosphorylated substrate analogs are potent active site-directed inhibitors of protein-tyrosine phosphatases

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Ligands for the Tyrosine Kinase p56lckSH2 Domain: Discovery of Potent Dipeptide Derivatives with Monocharged, Nonhydrolyzable Phosphate Replacements

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

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

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Insulin receptor-associated protein tyrosine phosphatase(s): role in insulin action

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How does alendronate inhibit protein-tyrosine phosphatases?

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Why is phosphonodifluoromethyl phenylalanine a more potent inhibitory moiety than phosphonomethyl phenylalanine toward protein-tyrosine phosphatases?

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Small molecule interactions with protein-tyrosine phosphatase PTP1B and their use in inhibitor design

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Structure-based design and synthesis of small molecule protein-tyrosine phosphatase 1B inhibitors

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A peptide-based protein-tyrosine phosphatase inhibitor specifically enhances insulin receptor function in intact cells

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Thiophosphorylated RCM-lysozyme, an active site-directed protein tyrosine phosphatase inhibitor, inhibits G2/M transition during mitotic cell cycle and uncouples MPF activation from G2/M transition

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Potent Inhibition of Insulin Receptor Dephosphorylation by a Hexamer Peptide Containing the Phosphotyrosyl Mimetic F2Pmp

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Protein-tyrosine phosphatase inhibition by a peptide containing the phosphotyrosyl mimetic, L-O-malonyltyrosine

21 January 2018

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Potent inhibition of protein-tyrosine phosphatase by phosphotyrosine-mimic containing cyclic peptides

21 January 2018

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4'-O-[2-(2-fluoromalonyl)]-L-tyrosine: a phosphotyrosyl mimic for the preparation of signal transduction inhibitory peptides

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21 January 2018

Identifiers

DOI

10.1074/JBC.275.10.7101

1 reference

Consolidated OpenCitations Corpus – April 2017

1 reference

Consolidated OpenCitations Corpus – April 2017

PubMed publication ID

10702277

1 reference

Consolidated OpenCitations Corpus – April 2017