Enzyme activity of phosphatase of regenerating liver is controlled by the redox environment and its C-terminal residues. - Wikidata - awgldk - TriplyDB

Enzyme activity of phosphatase of regenerating liver is controlled by the redox environment and its C-terminal residues.

Enzyme activity of phosphatase of regenerating liver is controlled by the redox environment and its C-terminal residues.

http://www.wikidata.org/entity/Q37382038

about

Drosophila PRL-1 is a growth inhibitor that counteracts the function of the Src oncogene Integrated analysis of global mRNA and protein expression data in HEK293 cells overexpressing PRL-1.Phosphatase of regenerating liver: a novel target for cancer therapy.Lipid binding protein response to a bile acid library: a combined NMR and statistical approach.Probing residue-specific interactions in the stabilization of proteins using high-resolution NMR: a study of disulfide bond compensation.PRL-3 phosphatase and cancer metastasis.Regulation of protein tyrosine phosphatases by reversible oxidation.Molecular mechanisms of the PRL phosphatases.Characterization of the Protein Tyrosine Phosphatase LmPRL-1 Secreted by Leishmania major via the Exosome Pathway.Genome-wide functional genetic screen with the anticancer agent AMPI-109 identifies PRL-3 as an oncogenic driver in triple-negative breast cancers.Reversion of sulfenamide prodrugs in the presence of free thiol-containing proteins.The protein tyrosine phosphatase PRL-2 interacts with the magnesium transporter CNNM3 to promote oncogenesis.

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P2860

Enzyme activity of phosphatase of regenerating liver is controlled by the redox environment and its C-terminal residues.

http://www.wikidata.org/entity/Q37382038

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on May 2009

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Enzyme activity of phosphatase ...... t and its C-terminal residues.

@en

Enzyme activity of phosphatase ...... t and its C-terminal residues.

@nl

type

label

Enzyme activity of phosphatase ...... t and its C-terminal residues.

@en

Enzyme activity of phosphatase ...... t and its C-terminal residues.

@nl

prefLabel

Enzyme activity of phosphatase ...... t and its C-terminal residues.

@en

Enzyme activity of phosphatase ...... t and its C-terminal residues.

@nl

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Enzyme activity of phosphatase ...... nt and its C-terminal residues

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P2093

Andria L Skinner

http://www.w3.org/2001/XMLSchema#string

Anthony A Vartia

http://www.w3.org/2001/XMLSchema#string

Todd D Williams

http://www.w3.org/2001/XMLSchema#string

P2860

A small CDC25 dual-specificity tyrosine-phosphatase isoform in Arabidopsis thaliana

Expression and prognostic impact of the protein tyrosine phosphatases PRL-1, PRL-2, and PRL-3 in breast cancer

Phosphatase of regenerating liver-3 promotes motility and metastasis of mouse melanoma cells

Oxidation state of the active-site cysteine in protein tyrosine phosphatase 1B

Structural insights into molecular function of the metastasis-associated phosphatase PRL-3

Redox-regulated conformational changes in an SH3 domain

1H, 13C and 15N chemical shift referencing in biomolecular NMR

NMRPipe: a multidimensional spectral processing system based on UNIX pipes

Prenylation-dependent association of protein-tyrosine phosphatases PRL-1, -2, and -3 with the plasma membrane and the early endosome

Enhanced cell cycle progression and down regulation of p21(Cip1/Waf1) by PRL tyrosine phosphatases

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4262-4272

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scholarly article

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10.1021/BI900241K

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20

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48

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Jennifer S Laurence

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2009-05-01T00:00:00Z

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24252897

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19341304

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2759777

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