PRL-1, a unique nuclear protein tyrosine phosphatase, affects cell growth
about
Phosphatase of regenerating liver 2 (PRL2) is essential for placental development by down-regulating PTEN (Phosphatase and Tensin Homologue Deleted on Chromosome 10) and activating Akt proteinP-TEN, the tumor suppressor from human chromosome 10q23, is a dual-specificity phosphataseProtein tyrosine phosphatases--from housekeeping enzymes to master regulators of signal transductionExpression and prognostic impact of the protein tyrosine phosphatases PRL-1, PRL-2, and PRL-3 in breast cancerPhosphatase of regenerating liver-3 promotes motility and metastasis of mouse melanoma cellsA transcriptome map of cellular transformation by the fos oncogeneDrosophila PRL-1 is a growth inhibitor that counteracts the function of the Src oncogeneStructural insights into molecular function of the metastasis-associated phosphatase PRL-3Structural and functional characterization of a novel phosphatase from the Arabidopsis thaliana gene locus At1g05000PRL-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 ProteinLigand Binding Reduces Conformational Flexibility in the Active Site of Tyrosine Phosphatase Related to Biofilm Formation A (TpbA) from Pseudomonas aeruginosaCloning and characterization of a Saccharomyces cerevisiae gene encoding the low molecular weight protein-tyrosine phosphatase.Regulatory mechanisms of phosphatase of regenerating liver (PRL)-3Prenylation-dependent association of protein-tyrosine phosphatases PRL-1, -2, and -3 with the plasma membrane and the early endosomeThe 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 receptor-like protein-tyrosine phosphatase DEP-1 is constitutively associated with a 64-kDa protein serine/threonine kinaseThe TriTryp phosphatome: analysis of the protein phosphatase catalytic domainsCellular localization of PRL-1 and PRL-2 gene expression in normal adult human tissuesThe gene encoding human nuclear protein tyrosine phosphatase, PRL-1. Cloning, chromosomal localization, and identification of an intron enhancerHRS/SRp40-mediated inclusion of the fibronectin EIIIB exon, a possible cause of increased EIIIB expression in proliferating liverMetastasis-associated phosphatase PRL-2 regulates tumor cell migration and invasion.Targeted deletion of the metastasis-associated phosphatase Ptp4a3 (PRL-3) suppresses murine colon cancer.Investigational inhibitors of PTP4A3 phosphatase as antineoplastic agents.Integrated analysis of global mRNA and protein expression data in HEK293 cells overexpressing PRL-1.Structural Basis of the Oncogenic Interaction of Phosphatase PRL-1 with the Magnesium Transporter CNNM2.Suppression of the protein tyrosine phosphatase receptor type O gene (PTPRO) by methylation in hepatocellular carcinomasTargeting PTPs with small molecule inhibitors in cancer treatmentPRL2/PTP4A2 phosphatase is important for hematopoietic stem cell self-renewal.Role of protein phosphatases in the regulation of human mast cell and basophil function.The RNA-binding specificity of the mouse Dazl proteinOncogenic function and prognostic significance of protein tyrosine phosphatase PRL-1 in hepatocellular carcinomaCharacterization of farnesylated protein tyrosine phosphatase TcPRL-1 from Trypanosoma cruziPhosphatase of regenerating liver-1 promotes cell migration and invasion and regulates filamentous actin dynamics.High levels of glucose-6-phosphatase gene and protein expression reflect an adaptive response in proliferating liver and diabetesPhosphatase of regenerating liver: a novel target for cancer therapy.Profiling of Hodgkin's lymphoma cell line L1236 and germinal center B cells: identification of Hodgkin's lymphoma-specific genes.Dynamic recruitment of microRNAs to their mRNA targets in the regenerating liverExpression of phosphatase of regenerating liver family genes during embryogenesis: an evolutionary developmental analysis among Drosophila, amphioxus, and zebrafish
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P2860
PRL-1, a unique nuclear protein tyrosine phosphatase, affects cell growth
description
1994 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
1994 թվականի հունիսին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 1994
@ast
im Juni 1994 veröffentlichter wissenschaftlicher Artikel
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scientific journal article
@en
vedecký článok (publikovaný 1994/06/01)
@sk
vědecký článek publikovaný v roce 1994
@cs
wetenschappelijk artikel (gepubliceerd op 1994/06/01)
@nl
наукова стаття, опублікована в червні 1994
@uk
مقالة علمية (نشرت في يونيو 1994)
@ar
name
PRL-1, a unique nuclear protein tyrosine phosphatase, affects cell growth
@ast
PRL-1, a unique nuclear protein tyrosine phosphatase, affects cell growth
@en
PRL-1, a unique nuclear protein tyrosine phosphatase, affects cell growth
@nl
type
label
PRL-1, a unique nuclear protein tyrosine phosphatase, affects cell growth
@ast
PRL-1, a unique nuclear protein tyrosine phosphatase, affects cell growth
@en
PRL-1, a unique nuclear protein tyrosine phosphatase, affects cell growth
@nl
prefLabel
PRL-1, a unique nuclear protein tyrosine phosphatase, affects cell growth
@ast
PRL-1, a unique nuclear protein tyrosine phosphatase, affects cell growth
@en
PRL-1, a unique nuclear protein tyrosine phosphatase, affects cell growth
@nl
P2093
P2860
P3181
P356
P1476
PRL-1, a unique nuclear protein tyrosine phosphatase, affects cell growth
@en
P2093
C. S. Abrams
D. E. Cressman
R. H. Diamond
P2860
P304
P3181
P356
10.1128/MCB.14.6.3752
P407
P577
1994-06-01T00:00:00Z