Constitutively activated FLT3 phosphorylates BAD partially through pim-1. - Wikidata - wikimedia - TriplyDB

Constitutively activated FLT3 phosphorylates BAD partially through pim-1.

Constitutively activated FLT3 phosphorylates BAD partially through pim-1.

http://www.wikidata.org/entity/Q40251345

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An overview on the role of FLT3-tyrosine kinase receptor in acute myeloid leukemia: biology and treatment Targeting Pim kinases for cancer treatment: opportunities and challenges Dissection of PIM serine/threonine kinases in FLT3-ITD-induced leukemogenesis reveals PIM1 as regulator of CXCL12-CXCR4-mediated homing and migration.Ki67 and PIM1 expression predict outcome in mantle cell lymphoma treated with high dose therapy, stem cell transplantation and rituximab: a Cancer and Leukemia Group B 59909 correlative science study Synthesis and evaluation of novel inhibitors of Pim-1 and Pim-2 protein kinases.Mitochondrial integrity: preservation through Akt/Pim-1 kinase signaling in the cardiomyocyte A small molecule inhibitor of Pim protein kinases blocks the growth of precursor T-cell lymphoblastic leukemia/lymphoma.Preclinical characterization of the CDK4/6 inhibitor LY2835219: in-vivo cell cycle-dependent/independent anti-tumor activities alone/in combination with gemcitabine Gene Expression and Serum Cytokine Profiling of Low Stage CLL Identify WNT/PCP, Flt-3L/Flt-3 and CXCL9/CXCR3 as Regulators of Cell Proliferation, Survival and Migration Preservation of myocardial structure is enhanced by pim-1 engineering of bone marrow cells MicroRNA-16 is down-regulated in mutated FLT3 expressing murine myeloid FDC-P1 cells and interacts with Pim-1.Pim-1 kinase phosphorylates and stabilizes 130 kDa FLT3 and promotes aberrant STAT5 signaling in acute myeloid leukemia with FLT3 internal tandem duplication The multitargeted receptor tyrosine kinase inhibitor linifanib (ABT-869) induces apoptosis through an Akt and glycogen synthase kinase 3β-dependent pathway.Inhibition of the receptor tyrosine kinase Axl impedes activation of the FLT3 internal tandem duplication in human acute myeloid leukemia: implications for Axl as a potential therapeutic target.Molecular mechanisms of drug resistance in acute myeloid leukaemia.The Pim kinase inhibitor SGI-1776 decreases cell surface expression of P-glycoprotein (ABCB1) and breast cancer resistance protein (ABCG2) and drug transport by Pim-1-dependent and -independent mechanisms Exploiting cellular pathways to develop new treatment strategies for AML.The evolving landscape in the therapy of acute myeloid leukemia.Mechanisms of Resistance to FLT3 Inhibitors and the Role of the Bone Marrow Microenvironment.Discovery of CX-6258. A Potent, Selective, and Orally Efficacious pan-Pim Kinases Inhibitor.Effects of the JAK2 inhibitor, AZ960, on Pim/BAD/BCL-xL survival signaling in the human JAK2 V617F cell line SET-2.The FLT3 inhibitor PKC412 exerts differential cell cycle effects on leukemic cells depending on the presence of FLT3 mutations.PIM-1 mRNA expression is a potential prognostic biomarker in acute myeloid leukemia.A potential therapeutic target for FLT3-ITD AML: PIM1 kinase.The antitumor compound triazoloacridinone C-1305 inhibits FLT3 kinase activity and potentiates apoptosis in mutant FLT3-ITD leukemia cells.Receptor kinase profiles identify a rationale for multitarget kinase inhibition in immature T-ALL.Targeted therapies in Acute Myeloid Leukemia: a focus on FLT-3 inhibitors and ABT199.A novel, dual pan-PIM/FLT3 inhibitor SEL24 exhibits broad therapeutic potential in acute myeloid leukemia.Resistance to FLT3 inhibitors in acute myeloid leukemia: Molecular mechanisms and resensitizing strategies

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P2860

Constitutively activated FLT3 phosphorylates BAD partially through pim-1.

http://www.wikidata.org/entity/Q40251345

description

2006 nî lūn-bûn

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2006年の論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年论文

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2006年论文

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2006年论文

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Constitutively activated FLT3 phosphorylates BAD partially through pim-1.

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Constitutively activated FLT3 phosphorylates BAD partially through pim-1.

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Constitutively activated FLT3 phosphorylates BAD partially through pim-1.

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J.1365-2141.2006.06225.X

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British Journal of Haematology

P1476

Constitutively activated FLT3 phosphorylates BAD partially through pim-1.

@en

P2093

Donald Small

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

Kyu-Tae Kim

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

Mark Levis

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P2860

Bad, a heterodimeric partner for Bcl-XL and Bcl-2, displaces Bax and promotes cell death

Activating mutation of D835 within the activation loop of FLT3 in human hematologic malignancies.

Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery

Cell survival promoted by the Ras-MAPK signaling pathway by transcription-dependent and -independent mechanisms

The PIM-2 kinase phosphorylates BAD on serine 112 and reverses BAD-induced cell death

A FLT3-targeted tyrosine kinase inhibitor is cytotoxic to leukemia cells in vitro and in vivo

Interleukin-3-induced phosphorylation of BAD through the protein kinase Akt

Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-X(L)

Targeted disruption of the flk2/flt3 gene leads to deficiencies in primitive hematopoietic progenitors

Inhibition of mutant FLT3 receptors in leukemia cells by the small molecule tyrosine kinase inhibitor PKC412.

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10.1111/J.1365-2141.2006.06225.X

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phosphorylation