A metalloprotease-disintegrin participating in myoblast fusion
about
Metalloprotease-disintegrin MDC9: intracellular maturation and catalytic activityCloning and characterization of ADAMTS11, an aggrecanase from the ADAMTS familyEvidence 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 SH3PX1Molecular cloning of MADM: a catalytically active mammalian disintegrin-metalloprotease expressed in various cell typesA novel synaptobrevin/VAMP homologous protein (VAMP5) is increased during in vitro myogenesis and present in the plasma membraneMDC9, a widely expressed cellular disintegrin containing cytoplasmic SH3 ligand domainsFLRG, a new ADAM12-associated protein, modulates osteoclast differentiationSpecific interaction of the recombinant disintegrin-like domain of MDC-15 (metargidin, ADAM-15) with integrin alphavbeta3Metalloproteinase-like, disintegrin-like, cysteine-rich proteins MDC2 and MDC3: novel human cellular disintegrins highly expressed in the brainPolymerase chain reaction selects a novel disintegrin proteinase from CD40-activated germinal center dendritic cellsCloning and characterization of ADAM28: evidence for autocatalytic pro-domain removal and for cell surface localization of mature ADAM28A 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 mechanismADAMTS-1: a metalloproteinase-disintegrin essential for normal growth, fertility, and organ morphology and functionThe cysteine-rich domain of human ADAM 12 supports cell adhesion through syndecans and triggers signaling events that lead to beta1 integrin-dependent cell spreadingDrosophila myoblast city encodes a conserved protein that is essential for myoblast fusion, dorsal closure, and cytoskeletal organizationA positive feedback loop between Dumbfounded and Rolling pebbles leads to myotube enlargement in DrosophilaRole of transmembrane 4 superfamily (TM4SF) proteins CD9 and CD81 in muscle cell fusion and myotube maintenanceADAM 12 protease induces adipogenesis in transgenic miceAggrecanases and cartilage matrix degradationSyndecans in tumor cell adhesion and signalingA Disintegrin and Metalloprotease (ADAM): Historical Overview of Their FunctionsThe beneficial role of proteolysis in skeletal muscle growth and stress adaptationThe potential of sarcospan in adhesion complex replacement therapeutics for the treatment of muscular dystrophyA 45,000-M(r) glycoprotein in the Sendai virus envelope triggers virus-cell fusionADAMTS-1 is an active metalloproteinase associated with the extracellular matrixADAMTS: a novel family of proteases with an ADAM protease domain and thrombospondin 1 repeatsConstitutive 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 ADAM19Direct interaction between the cytoplasmic tail of ADAM 12 and the Src homology 3 domain of p85alpha activates phosphatidylinositol 3-kinase in C2C12 cellsAssociation of the ADAM33 gene with asthma and bronchial hyperresponsivenessCloning 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 monolayersThe metalloprotease disintegrin ADAM8. Processing by autocatalysis is required for proteolytic activity and cell adhesionMyomaker is a membrane activator of myoblast fusion and muscle formation.Adamts-1 is essential for the development and function of the urogenital systemThe small muscle-specific protein Csl modifies cell shape and promotes myocyte fusion in an insulin-like growth factor 1-dependent manner
P2860
Q22008720-B0393981-DB30-4130-B9E8-84245253E374Q22010479-659CBF38-8C72-4068-8E75-31B4F5A6F376Q22010696-25E6AFD4-A02B-4999-A344-18070C800E54Q22010715-BD7FB29C-E521-4A16-A29B-BC697C98C20BQ24310056-D96E5E71-BD9A-4E2D-8AEF-8339047EF5A2Q24310308-300764EB-FF26-459D-BD1A-DC70E0C778B4Q24316013-2D3307AB-770C-4DE6-8FFD-1DD5F1CCFB7AQ24318438-BAA671F4-8D4D-4DD8-AB0B-0345BE4D6BA5Q24319074-0F8AE459-DB23-45E8-A918-7D0042FD7AF5Q24321609-74902991-9F9D-4C9A-B985-ADE01CE15841Q24336346-B6D00A94-1404-46A1-A5A1-EA8549B6FBF7Q24532037-4B8BAE89-66C2-4F62-84F8-0905FA569F06Q24533465-D5FEEC6A-7D4E-4626-8F72-313FEC01953BQ24548850-57734F0B-43F2-4720-8182-7DA05704A66DQ24618923-02514DD5-BB77-4260-BBBF-4A470F6E9969Q24669779-9E9D194A-0683-4808-A439-133D977C83D8Q24676790-05E14696-5532-40C2-9FD5-0751313146E3Q24678756-529BE4B0-3138-44EA-8C1D-07D441B1A6B2Q24683519-AF7E32DF-10BB-4D04-8B39-47A3241A7FF2Q24685092-BF771541-F23A-4BA6-9D62-89BA93F8AC0AQ24804310-57B839A4-D258-4FEC-A71A-F5EB5F821024Q24807364-5CA4E11B-491E-4586-9A11-5B527705E767Q26749364-3DD7AC67-F627-49AC-90E8-83E815AFA967Q26750990-82C57695-D719-4EA7-B38D-BC3E3337E4C1Q26827638-7EA75AF8-59C0-4145-9888-B109C2310F33Q27480846-0978F05A-749C-454C-AE76-8BDD61C88DABQ28137781-42CF060E-F1A8-47D8-9392-AE6BAE949B4FQ28139902-ED19C93D-6409-4650-97E0-C45DE5FD29D6Q28140038-38EB3B07-7158-456C-BF04-F7626BF6511EQ28145371-8DFEE189-7584-4659-A4D1-6B42A16305C0Q28189426-5FC68353-7EC9-43ED-9D68-03C104326DEBQ28213611-991D2061-DB7A-49BA-A40B-A10379B1D018Q28214089-095FCBB8-BDAD-4CAD-8B33-A6AD2FAB0944Q28261454-27479846-66E4-4D1D-8E1A-7D9A171740F1Q28271196-C6372240-5EE4-4A7A-ABA1-7F1D3E405443Q28281377-2846E179-4B14-48A8-B914-D55A8CDBAC14Q28511911-AB27A66B-C36B-4CC7-9C43-3BB82B7CFBB5Q28586981-1A0A4557-EB96-4A7A-838B-BD604A699410Q28588557-66C473F2-7D57-4994-BDC1-D5E05B9D89A9Q28593716-17D6546F-84B7-4191-B431-D6ECDE16B8D6
P2860
A metalloprotease-disintegrin participating in myoblast fusion
description
1995 nî lūn-bûn
@nan
1995 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
name
A metalloprotease-disintegrin participating in myoblast fusion
@ast
A metalloprotease-disintegrin participating in myoblast fusion
@en
A metalloprotease-disintegrin participating in myoblast fusion
@en-gb
A metalloprotease-disintegrin participating in myoblast fusion
@nl
type
label
A metalloprotease-disintegrin participating in myoblast fusion
@ast
A metalloprotease-disintegrin participating in myoblast fusion
@en
A metalloprotease-disintegrin participating in myoblast fusion
@en-gb
A metalloprotease-disintegrin participating in myoblast fusion
@nl
prefLabel
A metalloprotease-disintegrin participating in myoblast fusion
@ast
A metalloprotease-disintegrin participating in myoblast fusion
@en
A metalloprotease-disintegrin participating in myoblast fusion
@en-gb
A metalloprotease-disintegrin participating in myoblast fusion
@nl
P2093
P921
P3181
P356
P1433
P1476
A metalloprotease-disintegrin participating in myoblast fusion
@en
P2093
A Fujisawa-Sehara
T Kurisaki
T Yagami-Hiromasa
Y Nabeshima
P2888
P3181
P356
10.1038/377652A0
P407
P577
1995-10-19T00:00:00Z
P6179
1009810434