Protein tyrosine phosphatases: counting the trees in the forest (Q77946535)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9931406%20AND%20SRC:MED&resulttype=core&format=json

9 December 2019

review article

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title

Protein tyrosine phosphatases: counting the trees in the forest (English)

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9931406%20AND%20SRC:MED&resulttype=core&format=json

9 December 2019

author name string

R Hooft van Huijsduijnen

series ordinal

1

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9931406%20AND%20SRC:MED&resulttype=core&format=json

9 December 2019

publication date

1 December 1998

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9931406%20AND%20SRC:MED&resulttype=core&format=json

9 December 2019

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9931406%20AND%20SRC:MED&resulttype=core&format=json

9 December 2019

volume

225

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9 December 2019

issue

1-2

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9 December 2019

page(s)

1-8

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9 December 2019

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Crystal structure of human protein tyrosine phosphatase 1B

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Protein tyrosine phosphatases take off.

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Protein tyrosine phosphatases as adhesion receptors

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Catalytic Activation of the Phosphatase MKP-3 by ERK2 Mitogen-Activated Protein Kinase

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1002 protein phosphatases?

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Tyrosine phosphatases in T-cell development and signalling

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Cellular regulation by protein phosphorylation: a historical overview

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

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Identification of p130(cas) as a substrate for the cytosolic protein tyrosine phosphatase PTP-PEST.

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Use of vanadate as protein-phosphotyrosine phosphatase inhibitor

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Acidic residues are involved in substrate recognition by two soluble protein tyrosine phosphatases, PTP-5 and rrbPTP-1

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7 January 2021

Crystal structure of the tyrosine phosphatase SHP-2

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The crystal structure of domain 1 of receptor protein-tyrosine phosphatase mu

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Protein kinases and phosphatases: the yin and yang of protein phosphorylation and signaling

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Intracellular Signalling: Switching off signals

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

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An emerging family of dual specificity MAP kinase 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 tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate

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Roles of protein-tyrosine phosphatases in growth factor signalling

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

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Role of phosphatases in lymphocyte activation.

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7 January 2021

Protein tyrosine phosphatases in signal transduction.

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7 January 2021

Regulation of immune function by protein tyrosine phosphatases

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Protein tyrosine phosphatase roles in the regulation of lymphocyte signaling

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Phosphatases and tumorigenesis

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Protein phosphorylation and dephosphorylation in physiologic and oncologic processes

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Receptor-like protein tyrosine phosphatases: alike and yet so different

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Vanadium salts as insulin substitutes: mechanisms of action, a scientific and therapeutic tool in diabetes mellitus research

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Catalytic specificity of protein-tyrosine kinases is critical for selective signalling

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

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The coordinated action of protein tyrosine phosphatases and kinases in cell signaling

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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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From form to function: signaling by protein tyrosine phosphatases.

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A single mutation converts a novel phosphotyrosine binding domain into a dual-specificity phosphatase.

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Crystal structure of the dual specificity protein phosphatase VHR

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Structure, mechanism, and specificity of protein-tyrosine phosphatases

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

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7 January 2021

Substrate specificity of the protein tyrosine phosphatases

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Transition state and rate-limiting step of the reaction catalyzed by the human dual-specificity phosphatase, VHR

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Stimulation by phospholipids of a protein-tyrosine-phosphatase containing two src homology 2 domains

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7 January 2021

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Identifiers

DOI

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9931406%20AND%20SRC:MED&resulttype=core&format=json

9 December 2019

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