Specific interaction of the recombinant disintegrin-like domain of MDC-15 (metargidin, ADAM-15) with integrin alphavbeta3
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Interaction of the metalloprotease disintegrins MDC9 and MDC15 with two SH3 domain-containing proteins, endophilin I and SH3PX1The disintegrin domain of ADAM9: a ligand for multiple beta1 renal integrinsCatalytic activity of ADAM8, ADAM15, and MDC-L (ADAM28) on synthetic peptide substrates and in ectodomain cleavage of CD23Role of ADAM-9 disintegrin-cysteine-rich domains in human keratinocyte migrationADAM 23/MDC3, a human disintegrin that promotes cell adhesion via interaction with the alphavbeta3 integrin through an RGD-independent mechanismThe cysteine-rich domain of human ADAM 12 supports cell adhesion through syndecans and triggers signaling events that lead to beta1 integrin-dependent cell spreadingThe cysteine-rich domain regulates ADAM protease function in vivo.ADAM8 as a drug target in pancreatic cancer.Dynamics and functional differences between dendroaspin and rhodostomin: Insights into protein scaffolds in integrin recognitionMDC-L, a novel metalloprotease disintegrin cysteine-rich protein family member expressed by human lymphocytesFertilin beta and other ADAMs as integrin ligands: insights into cell adhesion and fertilizationThe lymphocyte metalloprotease MDC-L (ADAM 28) is a ligand for the integrin alpha4beta1Upregulation of ADAM19 in chronic allograft nephropathyADAM-15 inhibits wound healing in human intestinal epithelial cell monolayersThe metalloprotease disintegrin ADAM8. Processing by autocatalysis is required for proteolytic activity and cell adhesionCellular localization of the disintegrin CRII-7/rMDC15 mRNA in rat PNS and CNS and regulated expression in postnatal development and after nerve injuryMeltrin alpha cytoplasmic domain interacts with SH3 domains of Src and Grb2 and is phosphorylated by v-Src.Metalloprotease-disintegrin ADAM 12 binds to the SH3 domain of Src and activates Src tyrosine kinase in C2C12 cells.Sequence-specific interaction between the disintegrin domain of mouse ADAM 2 (fertilin beta) and murine eggs. Role of the alpha(6) integrin subunit.Sequence-specific interaction between the disintegrin domain of mouse ADAM 3 and murine eggs: role of beta1 integrin-associated proteins CD9, CD81, and CD98.Selective modulation of integrin-mediated cell migration by distinct ADAM family membersEvidence that distinct states of the integrin alpha6beta1 interact with laminin and an ADAM.The disulfide bond pattern of catrocollastatin C, a disintegrin-like/cysteine-rich protein isolated from Crotalus atrox venom.Highly enhanced expression of the disintegrin metalloproteinase MDC15 (metargidin) in rheumatoid synovial tissue.The chemokine fractalkine can activate integrins without CX3CR1 through direct binding to a ligand-binding site distinct from the classical RGD-binding site.Urokinase-type plasminogen activator receptor (CD87) is a ligand for integrins and mediates cell-cell interaction.Integrins as "functional hubs" in the regulation of pathological angiogenesisAdamalysins. A family of metzincins including TNF-alpha converting enzyme (TACE).RGD-independent binding of integrin alpha9beta1 to the ADAM-12 and -15 disintegrin domains mediates cell-cell interaction.ADAM15 regulates endothelial permeability and neutrophil migration via Src/ERK1/2 signallingEffect of P to A mutation of the N-terminal residue adjacent to the Rgd motif on rhodostomin: importance of dynamics in integrin recognition.The role of ADAM 15 in glomerular mesangial cell migration.Plasmin-induced migration requires signaling through protease-activated receptor 1 and integrin alpha(9)beta(1).Halting angiogenesis by non-viral somatic gene therapy alleviates psoriasis and murine psoriasiform skin lesions.ADAM and ADAMTS gene expression in native and wound healing human lens epithelial cellsADAM22, expressed in normal brain but not in high-grade gliomas, inhibits cellular proliferation via the disintegrin domain.Identification of inhibitors against interaction between pro-inflammatory sPLA2-IIA protein and integrin αvβ3.The effect of the single substitution of arginine within the RGD tripeptide motif of a modified neurotoxin dendroaspin on its activity of platelet aggregation and cell adhesion.Proinflammatory secreted phospholipase A2 type IIA (sPLA-IIA) induces integrin activation through direct binding to a newly identified binding site (site 2) in integrins αvβ3, α4β1, and α5β1.Potential role for ADAM15 in pathological neovascularization in mice.
P2860
Q22010715-A098CA67-B78F-43FE-B3DD-37451730F25DQ24303582-86A37E36-B2C3-4072-8BF5-9B8F77A29A20Q24303614-98BD1283-1A02-4047-9A29-182BA7B144D4Q24337698-1AAD184A-E56D-4C4D-919E-F9F1B55ECB92Q24548850-C832C48F-C242-473E-8493-94ED42454310Q24669779-78306615-A470-45E5-ACB8-8C4AE6B4C429Q24673136-F4C3BAC9-F570-4CB6-BA30-F2DA5A40B735Q27324447-BB655D1E-1320-4C36-AA21-7ADFB2939BB7Q27674048-41C31C0A-C4C8-4EC9-84CE-AF6143922C4AQ28145371-3327440E-D040-4C24-A705-F0CDDCBBB08CQ28207538-BE2BD0D0-B862-4757-B6DE-7E89CB87304AQ28207811-7AD8698C-C12A-469B-A6B5-0DF4C8C6C4BDQ28250891-8AD165FD-C1DC-4832-BF55-8B4570E69B79Q28281377-8749BE17-702A-4410-ABBE-6AC819E603BDQ28511911-37C89D76-79CA-446D-B689-2B642383C9A0Q28564239-5B9C76E9-0B6E-4B65-8680-F89490C4D0D8Q30168554-B82EA5B5-0DE7-459C-A573-C9B5BB85DFF7Q30168591-4D313971-EC7F-40DF-B59A-BAA5D2AFE170Q30305569-85EC9CA8-D6DC-42BC-8255-D7F6C06D612BQ30307197-6DDCF596-53EF-447E-84C3-F345CD79F55CQ30437660-15E4D690-D669-4925-BA01-617688FEA5CEQ30442078-80ED633F-7657-49B6-81D1-873132F525DEQ30444013-4AF857EE-1435-4897-866E-1C5515D04D66Q30731723-1D54D01F-6EBC-4A1C-826F-FDA4F24CAEBFQ31160040-50A4DF92-669D-4FB0-842C-450F997AD0EAQ31506532-60815083-BC08-49D1-BEBF-9709FA7F65E3Q33591910-78692C40-8A24-41BC-B70D-D1B36DB688D9Q33692956-66C9A5A8-111C-4C08-BF7C-AD6004607621Q33914018-94E78B12-621A-4C49-862A-D53489B1F2A4Q33954946-FD3EF0B2-34E1-435C-A3D7-D4F2C78769D7Q34124981-77D6AD18-1EC2-422F-AA24-DC2EB8E0D0BBQ34136288-B6B3D7EE-4FC5-4C36-AC63-E455272FA0CCQ34332597-58710A45-0608-4CBD-9B0A-1785BC872684Q34428875-15220287-6042-4370-83A4-041859A00B5EQ34434205-065D84D0-A93B-4E9F-B35C-61549081102EQ34480626-6FA36E80-5A59-47C8-9C11-CD08BE5684A4Q34481371-4ADDFB56-C747-4474-A325-2E3108955254Q34541685-8A23286D-04E4-4182-B257-1B2120C67F1EQ34801388-A4D64D65-320B-442B-98DE-C5DB86A0290FQ35169697-15295F9B-C206-45B8-87CC-4831EA771143
P2860
Specific interaction of the recombinant disintegrin-like domain of MDC-15 (metargidin, ADAM-15) with integrin alphavbeta3
description
1998 nî lūn-bûn
@nan
1998 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի մարտին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
Specific interaction of the re ...... -15) with integrin alphavbeta3
@ast
Specific interaction of the re ...... -15) with integrin alphavbeta3
@en
Specific interaction of the re ...... -15) with integrin alphavbeta3
@en-gb
Specific interaction of the re ...... -15) with integrin alphavbeta3
@nl
type
label
Specific interaction of the re ...... -15) with integrin alphavbeta3
@ast
Specific interaction of the re ...... -15) with integrin alphavbeta3
@en
Specific interaction of the re ...... -15) with integrin alphavbeta3
@en-gb
Specific interaction of the re ...... -15) with integrin alphavbeta3
@nl
prefLabel
Specific interaction of the re ...... -15) with integrin alphavbeta3
@ast
Specific interaction of the re ...... -15) with integrin alphavbeta3
@en
Specific interaction of the re ...... -15) with integrin alphavbeta3
@en-gb
Specific interaction of the re ...... -15) with integrin alphavbeta3
@nl
P2093
P2860
P356
P1476
Specific interaction of the re ...... -15) with integrin alphavbeta3
@en
P2093
K Yokoyama
W Puzon-McLaughlin
P2860
P304
P356
10.1074/JBC.273.13.7345
P407
P577
1998-03-27T00:00:00Z