Kuzbanian controls proteolytic processing of Notch and mediates lateral inhibition during Drosophila and vertebrate neurogenesis
about
Metalloprotease-disintegrin MDC9: intracellular maturation and catalytic activityEvidence for an interaction of the metalloprotease-disintegrin tumour necrosis factor alpha convertase (TACE) with mitotic arrest deficient 2 (MAD2), and of the metalloprotease-disintegrin MDC9 with a novel MAD2-related protein, MAD2betaInteraction of the metalloprotease disintegrins MDC9 and MDC15 with two SH3 domain-containing proteins, endophilin I and SH3PX1TspanC8 tetraspanins regulate ADAM10/Kuzbanian trafficking and promote Notch activation in flies and mammalsEvidence for regulation of the tumor necrosis factor alpha-convertase (TACE) by protein-tyrosine phosphatase PTPH1Metalloproteinase-like, disintegrin-like, cysteine-rich proteins MDC2 and MDC3: novel human cellular disintegrins highly expressed in the brainAn Epstein-Barr virus protein interacts with NotchA metalloprotease-disintegrin, MDC9/meltrin-gamma/ADAM9 and PKCdelta are involved in TPA-induced ectodomain shedding of membrane-anchored heparin-binding EGF-like growth factor.ADAM 23/MDC3, a human disintegrin that promotes cell adhesion via interaction with the alphavbeta3 integrin through an RGD-independent mechanismActivated notch inhibits myogenic activity of the MADS-Box transcription factor myocyte enhancer factor 2CADAMTS-1: a metalloproteinase-disintegrin essential for normal growth, fertility, and organ morphology and functionSignaling from axon guidance receptorsThe Notch1 receptor is cleaved constitutively by a furin-like convertaseMolecular mechanisms for the conversion of zymogens to active proteolytic enzymesThe cysteine-rich domain regulates ADAM protease function in vivo.Crystal structure of the catalytic domain of human tumor necrosis factor-alpha-converting enzymeIdentification and preliminary characterization of mouse Adam33Aggrecanases and cartilage matrix degradationA Disintegrin and Metalloprotease (ADAM): Historical Overview of Their FunctionsHeparin-binding epidermal growth factor-like growth factor/diphtheria toxin receptor in normal and neoplastic hematopoiesisNon-canonical Notch signaling: emerging role and mechanismFaster embryonic segmentation through elevated Delta-Notch signalling.The Wnt receptor Frizzled-4 modulates ADAM13 metalloprotease activityADAMTS-1 is an active metalloproteinase associated with the extracellular matrixConstitutive and regulated alpha-secretase cleavage of Alzheimer's amyloid precursor protein by a disintegrin metalloproteaseMDC-L, a novel metalloprotease disintegrin cysteine-rich protein family member expressed by human lymphocytesCatalytic properties of ADAM19Notch ligand endocytosis: mechanistic basis of signaling activityCloning and initial characterization of mouse meltrin beta and analysis of the expression of four metalloprotease-disintegrins in bone cellsADAMTS-1 protein anchors at the extracellular matrix through the thrombospondin type I motifs and its spacing regionADAM-15 inhibits wound healing in human intestinal epithelial cell monolayersADAMs: key components in EGFR signalling and developmentHes1 and Hes5 as notch effectors in mammalian neuronal differentiation.Fringe glycosyltransferases differentially modulate Notch1 proteolysis induced by Delta1 and Jagged1O-fucosylation of DLL3 is required for its function during somitogenesisCellular localization of the disintegrin CRII-7/rMDC15 mRNA in rat PNS and CNS and regulated expression in postnatal development and after nerve injuryDefects in limb, craniofacial, and thymic development in Jagged2 mutant miceTumor necrosis factor-alpha-converting enzyme is required for cleavage of erbB4/HER4Delta-1 activation of notch-1 signaling results in HES-1 transactivation.Identification and characterization of ADAM41, a novel ADAM metalloproteinase in Xenopus.
P2860
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P2860
Kuzbanian controls proteolytic processing of Notch and mediates lateral inhibition during Drosophila and vertebrate neurogenesis
description
1997 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 1997
@ast
im Juli 1997 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 1997/07/25)
@sk
vědecký článek publikovaný v roce 1997
@cs
wetenschappelijk artikel (gepubliceerd op 1997/07/25)
@nl
наукова стаття, опублікована в липні 1997
@uk
مقالة علمية (نشرت في 25-7-1997)
@ar
name
Kuzbanian controls proteolytic ...... la and vertebrate neurogenesis
@ast
Kuzbanian controls proteolytic ...... la and vertebrate neurogenesis
@en
Kuzbanian controls proteolytic ...... la and vertebrate neurogenesis
@nl
type
label
Kuzbanian controls proteolytic ...... la and vertebrate neurogenesis
@ast
Kuzbanian controls proteolytic ...... la and vertebrate neurogenesis
@en
Kuzbanian controls proteolytic ...... la and vertebrate neurogenesis
@nl
prefLabel
Kuzbanian controls proteolytic ...... la and vertebrate neurogenesis
@ast
Kuzbanian controls proteolytic ...... la and vertebrate neurogenesis
@en
Kuzbanian controls proteolytic ...... la and vertebrate neurogenesis
@nl
P3181
P1433
P1476
Kuzbanian controls proteolytic ...... la and vertebrate neurogenesis
@en
P2093
P304
P3181
P356
10.1016/S0092-8674(00)80335-9
P407
P577
1997-07-25T00:00:00Z