Primary sequence determinants responsible for site-selective dephosphorylation of the PDGF beta-receptor by the receptor-like protein tyrosine phosphatase DEP-1 (Q24299634)

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English	Primary sequence determinants responsible for site-selective dephosphorylation of the PDGF beta-receptor by the receptor-like protein tyrosine phosphatase DEP-1	scientific article

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scholarly article

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Primary sequence determinants responsible for site-selective dephosphorylation of the PDGF beta-receptor by the receptor-like protein tyrosine phosphatase DEP-1 (English)

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Protein tyrosine phosphatase receptor type J

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GOA release 2020-03-11

phosphatase activity

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GOA release 2020-03-11

author name string

Camilla Persson

1

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Ulla Engström

2

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Sherry L Mowbray

3

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Arne Ostman

4

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language of work or name

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publication date

24 April 2002

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517

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1-3

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27-31

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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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https://api.crossref.org/works/10.1016%2FS0014-5793%2802%2902570-X

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Cell signaling by receptor tyrosine kinases

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Protein tyrosine kinase structure and function

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https://api.crossref.org/works/10.1016%2FS0014-5793%2802%2902570-X

21 January 2018

Regulation of receptor tyrosine kinase signaling by protein tyrosine phosphatases

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Expression of DEP-1, a receptor-like protein-tyrosine-phosphatase, is enhanced with increasing cell density

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21 January 2018

Cloning and characterization of rat density-enhanced phosphatase-1, a protein tyrosine phosphatase expressed by vascular cells

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Protein tyrosine phosphatase CD148-mediated inhibition of T-cell receptor signal transduction is associated with reduced LAT and phospholipase Cgamma1 phosphorylation

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Thyroid cell transformation inhibits the expression of a novel rat protein tyrosine phosphatase

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Rat protein tyrosine phosphatase eta suppresses the neoplastic phenotype of retrovirally transformed thyroid cells through the stabilization of p27(Kip1).

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An extracellular ligand increases the specific activity of the receptor-like protein tyrosine phosphatase DEP-1.

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Site-selective dephosphorylation of the platelet-derived growth factor beta-receptor by the receptor-like protein-tyrosine phosphatase DEP-1

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

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Affinity selection from peptide libraries to determine substrate specificity of protein tyrosine phosphatases

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

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Molecular basis for the dephosphorylation of the activation segment of the insulin receptor by protein tyrosine phosphatase 1B

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

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21 January 2018

Structural basis for substrate specificity of protein-tyrosine phosphatase SHP-1

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21 January 2018

Structural and evolutionary relationships among protein tyrosine phosphatase domains

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https://api.crossref.org/works/10.1016%2FS0014-5793%2802%2902570-X

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Sequence-specific recognition of peptide substrates by the low Mr phosphotyrosine protein phosphatase isoforms.

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Specificity of T-cell protein tyrosine phosphatase toward phosphorylated synthetic peptides

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

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7 January 2021

Identifiers

10.1016/S0014-5793(02)02570-X

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