Prenylation-dependent association of protein-tyrosine phosphatases PRL-1, -2, and -3 with the plasma membrane and the early endosome
about
Protein-tyrosine phosphatase 4A3 (PTP4A3) promotes vascular endothelial growth factor signaling and enables endothelial cell motility.Epigenetic regulation of human alpha1d-adrenergic receptor gene expression: a role for DNA methylation in Sp1-dependent regulationDrosophila PRL-1 is a growth inhibitor that counteracts the function of the Src oncogeneStructural insights into molecular function of the metastasis-associated phosphatase PRL-3PRL-1 Protein Promotes ERK1/2 and RhoA Protein Activation through a Non-canonical Interaction with the Src Homology 3 Domain of p115 Rho GTPase-activating ProteinRegulatory mechanisms of phosphatase of regenerating liver (PRL)-3The tyrosine phosphatase PRL-1 localizes to the endoplasmic reticulum and the mitotic spindle and is required for normal mitosisInteraction of farnesylated PRL-2, a protein-tyrosine phosphatase, with the beta-subunit of geranylgeranyltransferase IIATF-7, a novel bZIP protein, interacts with the PRL-1 protein-tyrosine phosphataseThe TriTryp phosphatome: analysis of the protein phosphatase catalytic domainsCellular localization of PRL-1 and PRL-2 gene expression in normal adult human tissuesIdentification of a novel prenyl and palmitoyl modification at the CaaX motif of Cdc42 that regulates RhoGDI bindingMetastasis-associated phosphatase PRL-2 regulates tumor cell migration and invasion.Investigational inhibitors of PTP4A3 phosphatase as antineoplastic agents.Structural Basis of the Oncogenic Interaction of Phosphatase PRL-1 with the Magnesium Transporter CNNM2.Phosphatase of regenerating liver-3 localizes to cyto-membrane and is required for B16F1 melanoma cell metastasis in vitro and in vivoTherapeutic potential of PRL-3 targeting and clinical significance of PRL-3 genomic amplification in gastric cancerPRL2 links magnesium flux and sex-dependent circadian metabolic rhythmsPRL-3 promotes telomere deprotection and chromosomal instability.Characterization of farnesylated protein tyrosine phosphatase TcPRL-1 from Trypanosoma cruziPhosphatase of regenerating liver-1 promotes cell migration and invasion and regulates filamentous actin dynamics.Rapid analysis of protein farnesyltransferase substrate specificity using peptide libraries and isoprenoid diphosphate analogues.A PTP4A3 peptide PIMAP39 modulates TNF-alpha levels and endotoxic shock.Protein tyrosine phosphatases as potential therapeutic targets.A role of autophagy in PTP4A3-driven cancer progression.Phosphatase of regenerating liver: a novel target for cancer therapy.Lipid posttranslational modifications. Farnesyl transferase inhibitors.Expression of phosphatase of regenerating liver family genes during embryogenesis: an evolutionary developmental analysis among Drosophila, amphioxus, and zebrafishMiR-339-5p regulates the growth, colony formation and metastasis of colorectal cancer cells by targeting PRL-1Targeting protein tyrosine phosphatases for anticancer drug discovery.Farnesyltransferase inhibitors in breast cancer therapy.Tissue-specific alterations of PRL-1 and PRL-2 expression in cancerEngineering the first chimeric antibody in targeting intracellular PRL-3 oncoprotein for cancer therapy in mice.Analysis of molecular determinants of PRL-3.Colon cancer: prevalence, screening, gene expression and mutation, and risk factors and assessment.Oxidative stress-induced expression and modulation of Phosphatase of Regenerating Liver-1 (PRL-1) in mammalian retina.Upregulation of protein tyrosine phosphatase type IVA member 3 (PTP4A3/PRL-3) is associated with tumor differentiation and a poor prognosis in human hepatocellular carcinomaGeneration of conditional knockout alleles for PRL-3.PRL-3: a metastasis-associated phosphatase in search of a function.Expression of phosphatase regenerating liver 3 is an independent prognostic indicator for gastric cancer
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P2860
Prenylation-dependent association of protein-tyrosine phosphatases PRL-1, -2, and -3 with the plasma membrane and the early endosome
description
2000 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
article publié dans la revue scientifique Journal of Biological Chemistry
@fr
artículu científicu espublizáu en 2000
@ast
im Juli 2000 veröffentlichter wissenschaftlicher Artikel
@de
scientific article (publication date: 14 July 2000)
@en
vedecký článok (publikovaný 2000/07/14)
@sk
vědecký článek publikovaný v roce 2000
@cs
wetenschappelijk artikel (gepubliceerd op 2000/07/14)
@nl
наукова стаття, опублікована в липні 2000
@uk
name
Prenylation-dependent associat ...... embrane and the early endosome
@ast
Prenylation-dependent associat ...... embrane and the early endosome
@en
Prenylation-dependent associat ...... embrane and the early endosome
@nl
type
label
Prenylation-dependent associat ...... embrane and the early endosome
@ast
Prenylation-dependent associat ...... embrane and the early endosome
@en
Prenylation-dependent associat ...... embrane and the early endosome
@nl
prefLabel
Prenylation-dependent associat ...... embrane and the early endosome
@ast
Prenylation-dependent associat ...... embrane and the early endosome
@en
Prenylation-dependent associat ...... embrane and the early endosome
@nl
P2093
P2860
P3181
P356
P1476
Prenylation-dependent associat ...... embrane and the early endosome
@en
P2093
P2860
P304
P3181
P356
10.1074/JBC.M000453200
P407
P577
2000-07-14T00:00:00Z