The metastasis-associated gene Prl-3 is a p53 target involved in cell-cycle regulation.
about
Drosophila PRL-1 is a growth inhibitor that counteracts the function of the Src oncogeneRegulatory mechanisms of phosphatase of regenerating liver (PRL)-3PRL-3, a metastasis associated tyrosine phosphatase, is involved in FLT3-ITD signaling and implicated in anti-AML therapyAntibody Array Revealed PRL-3 Affects Protein Phosphorylation and Cytokine SecretionQuantitative proteomic analysis of gene regulation by miR-34a and miR-34cMetastasis-associated phosphatase PRL-2 regulates tumor cell migration and invasion.Targeted deletion of the metastasis-associated phosphatase Ptp4a3 (PRL-3) suppresses murine colon cancer.Therapeutic potential of PRL-3 targeting and clinical significance of PRL-3 genomic amplification in gastric cancerRetroviral integration mutagenesis in mice and comparative analysis in human AML identify reduced PTP4A3 expression as a prognostic indicator.VEGF promotes the transcription of the human PRL-3 gene in HUVEC through transcription factor MEF2CA role of autophagy in PTP4A3-driven cancer progression.Phosphatase of regenerating liver: a novel target for cancer therapy.Independent oncogenic and therapeutic significance of phosphatase PRL-3 in FLT3-ITD-negative acute myeloid leukemia.Src-mediated phosphorylation of the tyrosine phosphatase PRL-3 is required for PRL-3 promotion of Rho activation, motility and invasionProtein tyrosine phosphatase 4A3 (PTP4A3) is required for Xenopus laevis cranial neural crest migration in vivo.Arsenic in cancer treatment: challenges for application of realgar nanoparticles (a minireview).Correlation between Liver Metastases and the Level of PRL-3 mRNA Expression in Patients with Primary Colorectal Cancer.The prognostic significance of protein tyrosine phosphatase 4A2 in breast cancer.The pro-metastasis tyrosine phosphatase, PRL-3 (PTP4A3), is a novel mediator of oncogenic function of BCR-ABL in human chronic myeloid leukemiaPRL-3 promotes cell adhesion by interacting with JAM2 in colon cancer.Loss of the oncogenic phosphatase PRL-3 promotes a TNF-R1 feedback loop that mediates triple-negative breast cancer growth.Phosphatase of regenerating liver 3 (PRL3) provokes a tyrosine phosphoproteome to drive prometastatic signal transductionIdentification of proteins suppressing the functions of oncogenic phosphatase of regenerating liver 1 and 3.PRL-3 promotes the motility, invasion, and metastasis of LoVo colon cancer cells through PRL-3-integrin beta1-ERK1/2 and-MMP2 signaling.PRL-3 phosphatase and cancer metastasis.Molecular mechanisms of the PRL phosphatases.Phosphatase of regenerating liver 3 (PRL-3) is overexpressed in human prostate cancer tissue and promotes growth and migration.Genome-wide functional genetic screen with the anticancer agent AMPI-109 identifies PRL-3 as an oncogenic driver in triple-negative breast cancers.The Hippo pathway promotes cell survival in response to chemical stress.Thioredoxin-related protein 32 (TRP32) specifically reduces oxidized phosphatase of regenerating liver (PRL).Overexpression of PTP4A3 is associated with metastasis and unfavorable prognosis in bladder cancer.Genomic gain of the PRL-3 gene may represent poor prognosis of primary colorectal cancer, and associate with liver metastasis.Deletion of Ptp4a3 reduces clonogenicity and tumor-initiation ability of colitis-associated cancer cells in mice.Prognostic significance of high phosphatase of regenerating liver-3 expression in patients with gastric cancer who underwent curative gastrectomy.f-scLVM: scalable and versatile factor analysis for single-cell RNA-seq.PRL‑3 increases the aggressive phenotype of prostate cancer cells in vitro and its expression correlates with high-grade prostate tumors in patients.Suppression of protein tyrosine phosphatase N23 predisposes to breast tumorigenesis via activation of FYN kinase.Expression of PRL-3 regulates proliferation and invasion of breast cancer cells in vitro.Neural crest specification by Prohibitin1 depends on transcriptional regulation of prl3 and vangl1.A loss-of-function genetic screening reveals synergistic targeting of AKT/mTOR and WTN/β-catenin pathways for treatment of AML with high PRL-3 phosphatase.
P2860
Q27326713-928D5B8B-9E50-4DBD-8148-B586B1E8DB02Q28066318-944E3296-7655-4B94-978B-163FE736DA2BQ28388468-2B728D25-DBF7-4232-86C0-E359B7A8BF09Q28469321-45058CFB-BC52-4E07-A77B-81DB69E1B977Q28541011-29BC4D05-D6BB-4373-8B44-795D833B3E1BQ30371232-F9E5FA6F-55E8-4220-9E9D-541BC9245915Q30420119-A7A8DF3E-24E2-4B65-A56F-0DAA6BF11D7CQ33863328-5E246F4A-D53C-4C5C-9713-6D562DA12A8FQ34058661-CEC9E424-3899-4A86-8FC0-C8489B9F463DQ34071838-4DDA097A-FBC6-41FD-A8E9-9E03FF9189D0Q34344700-70028954-F7E8-4DD1-AB8A-003DBA8E6FBAQ34437541-2D8F27F3-7A45-4CDA-9C46-46C887C54748Q34507306-4A03AFBF-43AA-4EBB-9C2A-EC3EF6A171F1Q34731436-AF6BF831-86CB-4173-A55D-A1C324EF5CC3Q35078466-F953F22F-5D32-4C6D-B103-716485617845Q35155855-C45299A3-77B5-42DB-AF21-5A232B955386Q35555652-E3DCA8E8-79EB-4EC6-B229-6F55C5B6E1F6Q35867697-01F1249B-A4CE-4B1D-8A94-6C0EC238D78BQ36510458-180D24D6-693B-41BC-AAEA-2CCD2F7EBE26Q37204478-CEE68356-0CA2-4C1F-8437-93D8C8FB626CQ37224273-8EC82A73-8498-4EA4-96F7-E90488014F63Q37389005-21B41F91-D343-4500-BC5B-77C20ABAFEF6Q37406431-7B578976-F500-454E-BCBF-EFF201BE5B32Q37472041-A1A14F6B-E4D7-41E6-82D1-0DCC748CE807Q37807363-4BF86830-0EDD-4B3B-879E-527E92B4288FQ37993157-EDACB0FD-A911-45E1-BAEC-5C90A423E760Q38786529-3CA3B714-31E8-4D01-9AD0-BA7C960E9811Q38791488-9658D74E-0DF8-419B-83C4-A084A7BA6CCDQ38869982-391C6026-3AAC-4731-B42D-DA0157AD2806Q39202231-16FB5BB1-AD6F-44A8-ADFF-ECB08E76D778Q40967704-488343F4-3EA1-4E82-8D38-005DA50EE50EQ41127993-5A7FE9A3-0BA4-4D8E-BB75-E94F07E0107EQ41911593-F6F0CF24-6E11-4D2D-BD8B-CCD143F602D9Q43678272-568F55BD-A4FF-4698-A544-60E3B61728EAQ46726359-9C9B3E8F-902A-4EAD-8395-8770AD649BAEQ47104255-5C2D4555-F323-43E8-8CDC-D7331BA7D951Q47608480-E941936E-866A-4D9E-AEEE-93ADD8D5FDDAQ47694771-A9A402E7-E48D-4615-84E0-FB45645919A7Q50571729-B6AFF235-62B8-4266-BC31-5E8B0EABEA2AQ52668830-664CD7A9-BFE9-4DF9-AAC0-9D64929A891B
P2860
The metastasis-associated gene Prl-3 is a p53 target involved in cell-cycle regulation.
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年学术文章
@wuu
2008年学术文章
@zh-cn
2008年学术文章
@zh-hans
2008年学术文章
@zh-my
2008年学术文章
@zh-sg
2008年學術文章
@yue
2008年學術文章
@zh
2008年學術文章
@zh-hant
name
The metastasis-associated gene Prl-3 is a p53 target involved in cell-cycle regulation.
@en
type
label
The metastasis-associated gene Prl-3 is a p53 target involved in cell-cycle regulation.
@en
prefLabel
The metastasis-associated gene Prl-3 is a p53 target involved in cell-cycle regulation.
@en
P2093
P2860
P1433
P1476
The metastasis-associated gene Prl-3 is a p53 target involved in cell-cycle regulation.
@en
P2093
Adam J Krieg
Amato J Giaccia
Laura D Attardi
Navneeta Pathak
Philipp Kaldis
Shashwati Basak
Suzanne B R Jacobs
P2860
P304
P356
10.1016/J.MOLCEL.2008.04.002
P577
2008-05-01T00:00:00Z