PRL phosphatases as potential molecular targets in cancer.
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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 proteinProtein-tyrosine phosphatase 4A3 (PTP4A3) promotes vascular endothelial growth factor signaling and enables endothelial cell motility.Expression and prognostic impact of the protein tyrosine phosphatases PRL-1, PRL-2, and PRL-3 in breast cancerThe protein-phosphatome of the human malaria parasite Plasmodium falciparumDrosophila PRL-1 is a growth inhibitor that counteracts the function of the Src oncogenePRL-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 ProteinPRL-3, a metastasis associated tyrosine phosphatase, is involved in FLT3-ITD signaling and implicated in anti-AML therapyPhotooxygenation of an amino-thienopyridone yields a more potent PTP4A3 inhibitor.Metastasis-associated phosphatase PRL-2 regulates tumor cell migration and invasion.Investigational inhibitors of PTP4A3 phosphatase as antineoplastic agents.EndoGI modulates Notch signaling and axon guidance in Drosophila.Targeting PTPs with small molecule inhibitors in cancer treatmentPRL2/PTP4A2 phosphatase is important for hematopoietic stem cell self-renewal.The effect of pentamidine on melanoma ex vivo.Inhibition of cellular Shp2 activity by a methyl ester analog of SPI-112.Phosphatase of regenerating liver-1 promotes cell migration and invasion and regulates filamentous actin dynamics.VEGF promotes the transcription of the human PRL-3 gene in HUVEC through transcription factor MEF2CProtein tyrosine phosphatases as potential therapeutic targets.Independent oncogenic and therapeutic significance of phosphatase PRL-3 in FLT3-ITD-negative acute myeloid leukemia.Genome wide in silico analysis of Plasmodium falciparum phosphatome.Protein tyrosine phosphatase 4A2 expression predicts overall and disease-free survival of human breast cancer and is associated with estrogen and progestin receptor status.Expression of phosphatase of regenerating liver family genes during embryogenesis: an evolutionary developmental analysis among Drosophila, amphioxus, and zebrafishTargeting protein tyrosine phosphatases for anticancer drug discovery.Integrating virtual and biochemical screening for protein tyrosine phosphatase inhibitor discovery.Protein tyrosine phosphatase 4A3 (PTP4A3) is required for Xenopus laevis cranial neural crest migration in vivo.PRL-3 siRNA inhibits the metastasis of B16-BL6 mouse melanoma cells in vitro and in vivo.The prognostic significance of protein tyrosine phosphatase 4A2 in breast cancer.Engineering the first chimeric antibody in targeting intracellular PRL-3 oncoprotein for cancer therapy in mice.Analysis of molecular determinants of PRL-3.TNFAIP8: a new effector for Galpha(i) coupling to reduce cell death and induce cell transformation.Suppression of cell migration is promoted by miR-944 through targeting of SIAH1 and PTP4A1 in breast cancer cells.Overexpression and involvement in migration by the metastasis-associated phosphatase PRL-3 in human myeloma cellsThe pro-metastasis tyrosine phosphatase, PRL-3 (PTP4A3), is a novel mediator of oncogenic function of BCR-ABL in human chronic myeloid leukemiaGeneration of conditional knockout alleles for PRL-3.Antimetastatic effect of halichondramide, a trisoxazole macrolide from the marine sponge Chondrosia corticata, on human prostate cancer cells via modulation of epithelial-to-mesenchymal transition.Protein tyrosine phosphatases: dual-specificity phosphatases in health and disease.Expression of phosphatase regenerating liver 3 is an independent prognostic indicator for gastric cancerRole of phosphatase of regenerating liver 1 (PRL1) in spermatogenesis.1H, 15N, 13C resonance assignments of the reduced and active form of human Protein Tyrosine Phosphatase, PRL-1.Enzyme activity of phosphatase of regenerating liver is controlled by the redox environment and its C-terminal residues.
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PRL phosphatases as potential molecular targets in cancer.
description
2005 nî lūn-bûn
@nan
2005年の論文
@ja
2005年学术文章
@wuu
2005年学术文章
@zh-cn
2005年学术文章
@zh-hans
2005年学术文章
@zh-my
2005年学术文章
@zh-sg
2005年學術文章
@yue
2005年學術文章
@zh
2005年學術文章
@zh-hant
name
PRL phosphatases as potential molecular targets in cancer.
@ast
PRL phosphatases as potential molecular targets in cancer.
@en
type
label
PRL phosphatases as potential molecular targets in cancer.
@ast
PRL phosphatases as potential molecular targets in cancer.
@en
prefLabel
PRL phosphatases as potential molecular targets in cancer.
@ast
PRL phosphatases as potential molecular targets in cancer.
@en
P2093
P1476
PRL phosphatases as potential molecular targets in cancer.
@en
P2093
Bret J Stephens
Daniel D Von Hoff
Haiyong Han
Vijay Gokhale
P304
P356
10.1158/1535-7163.MCT-05-0248
P577
2005-11-01T00:00:00Z