Notch oncoproteins depend on gamma-secretase/presenilin activity for processing and function. - sprookjes - yvandenbroek - TriplyDB

Notch oncoproteins depend on gamma-secretase/presenilin activity for processing and function.

Notch oncoproteins depend on gamma-secretase/presenilin activity for processing and function.

http://www.wikidata.org/entity/Q40559863

about

OLIG2 (BHLHB1), a bHLH transcription factor, contributes to leukemogenesis in concert with LMO1 A Foxo/Notch pathway controls myogenic differentiation and fiber type specification A Disintegrin and Metalloproteinase Domain 17 Regulates Colorectal Cancer Stem Cells and Chemosensitivity Via Notch1 Signaling.Regulation of CD23 expression by Notch2 in B-cell chronic lymphocytic leukemia Focused chemical genomics using zebrafish xenotransplantation as a pre-clinical therapeutic platform for T-cell acute lymphoblastic leukemia γ-Secretase inhibitor enhances antitumour effect of radiation in Notch-expressing lung cancer Notch signaling respecifies the hemangioblast to a cardiac fate Notch3 cooperates with the EGFR pathway to modulate apoptosis through the induction of bim.Notch regulates the angiogenic response via induction of VEGFR-1.Gliotoxin Targets Nuclear NOTCH2 in Human Solid Tumor Derived Cell Lines In Vitro and Inhibits Melanoma Growth in Xenograft Mouse Model.Clinicopathological significance of aberrant Notch receptors in intrahepatic cholangiocarcinoma.Hypoxia-induced down-regulation of microRNA-34a promotes EMT by targeting the Notch signaling pathway in tubular epithelial cells.Inhibition of Notch signaling ameliorates insulin resistance in a FoxO1-dependent manner.Targets for AD treatment: conflicting messages from γ-secretase inhibitors Loss of presenilin 2 is associated with increased iPLA2 activity and lung tumor development.Notch signaling as a therapeutic target for breast cancer treatment?Notch alters VEGF responsiveness in human and murine endothelial cells by direct regulation of VEGFR-3 expression.Therapeutic potential of oxidant mechanisms in Alzheimer's disease.Protease inhibitors as potential disease-modifying therapeutics for Alzheimer's disease.Therapeutic options in Alzheimer's disease.A notch1 ectodomain construct inhibits endothelial notch signaling, tumor growth, and angiogenesis.The expression of presenilin 1 enhances carcinogenesis and metastasis in gastric cancer.Complementary genomic screens identify SERCA as a therapeutic target in NOTCH1 mutated cancer.Notch signaling in leukemia.Characterization of the gene BmEm4, a homologue of Drosophila E(spl)m4, from the silkworm, Bombyx mori.Hyperexpression of NOTCH-1 is found in immature acute myeloid leukemia.Pathways involved in Drosophila and human cancer development: the Notch, Hedgehog, Wingless, Runt, and Trithorax pathway.Induction of apoptosis by proteasome inhibitors in B-CLL cells is associated with downregulation of CD23 and inactivation of Notch2.Inhibition of Notch and HIF enhances the antitumor effect of radiation in Notch expressing lung cancer.Sonic Hedgehog regulates Hes1 through a novel mechanism that is independent of canonical Notch pathway signalling.Combined antitumor effect of γ-secretase inhibitor and ABT-737 in Notch-expressing non-small cell lung cancer.Gliotoxin is a potent NOTCH2 transactivation inhibitor and efficiently induces apoptosis in chronic lymphocytic leukaemia (CLL) cells.Signal transduction growth factors: the effective governance of transcription and cellular adhesion in cancer invasion.Amyloid precursor protein and Presenilin1 interact with the adaptor GRB2 and modulate ERK 1,2 signaling.Activating mutations in NOTCH1 in acute myeloid leukemia and lineage switch leukemias.Opposing actions of endocannabinoids on cholangiocarcinoma growth is via the differential activation of Notch signaling.NOTCH1 activates the Wnt/β-catenin signaling pathway in colon cancer.Notch modulates VEGF action in endothelial cells by inducing Matrix Metalloprotease activity.NOTCH1 expression predicts patient prognosis in esophageal squamous cell cancer.Presenilin Mutation Suppresses Lung Tumorigenesis via Inhibition of Peroxiredoxin 6 Activity and Expression.

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P2860

Notch oncoproteins depend on gamma-secretase/presenilin activity for processing and function.

http://www.wikidata.org/entity/Q40559863

description

2004 nî lūn-bûn

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2004年の論文

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2004年論文

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2004年論文

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2004年論文

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2004年論文

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2004年論文

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2004年论文

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2004年论文

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2004年论文

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name

Notch oncoproteins depend on g ...... y for processing and function.

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type

label

Notch oncoproteins depend on g ...... y for processing and function.

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prefLabel

Notch oncoproteins depend on g ...... y for processing and function.

@en

P1433

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P1433

Journal of Biological Chemistry

P1476

Notch oncoproteins depend on g ...... y for processing and function.

@en

P2093

Andrew P Weng

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

Colleen Craig

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

Indranil Das

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

Jan Kitajewski

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

Jeffery L Kutok

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

Jon C Aster

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

Kwang-Mook Jung

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

Tae-Wan Kim

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

Yasuhiro Funahashi

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

P2860

Nicastrin modulates presenilin-mediated notch/glp-1 signal transduction and betaAPP processing

A presenilin-1/gamma-secretase cleavage releases the E-cadherin intracellular domain and regulates disassembly of adherens junctions.

Endoproteolysis of presenilin 1 and accumulation of processed derivatives in vivo

TAN-1, the human homolog of the Drosophila notch gene, is broken by chromosomal translocations in T lymphoblastic neoplasms

Intracellular cleavage of Notch leads to a heterodimeric receptor on the plasma membrane

Presenilin and nicastrin regulate each other and determine amyloid beta-peptide production via complex formation

Regulation of Notch1 and Dll4 by vascular endothelial growth factor in arterial endothelial cells: implications for modulating arteriogenesis and angiogenesis

SEL-10 is an inhibitor of notch signaling that targets notch for ubiquitin-mediated protein degradation

The Notch1 receptor is cleaved constitutively by a furin-like convertase

A novel proteolytic cleavage involved in Notch signaling: the role of the disintegrin-metalloprotease TACE

P304

30771-30780

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scholarly article

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10.1074/JBC.M309252200

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P407

P433

29

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P478

279

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P577

2004-05-03T00:00:00Z

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P698

15123653

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