Snake venom metalloproteinases: structure, function and relationship to the ADAMs family of proteins.
about
Cloning and characterization of ADAMTS11, an aggrecanase from the ADAMTS familyConformation and concerted dynamics of the integrin-binding site and the C-terminal region of echistatin revealed by homonuclear NMRThe cysteine-rich domain of human ADAM 12 supports cell adhesion through syndecans and triggers signaling events that lead to beta1 integrin-dependent cell spreadingAntitumoral activity of snake venom proteins: new trends in cancer therapyFertilin beta and other ADAMs as integrin ligands: insights into cell adhesion and fertilizationInsights into the Evolution of a Snake Venom Multi-Gene Family from the Genomic Organization of Echis ocellatus SVMP GenesEvidence 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.The evolution of the vertebrate metzincins; insights from Ciona intestinalis and Danio rerio.Insights into the venom composition of the ectoparasitoid wasp Nasonia vitripennis from bioinformatic and proteomic studies.Snake venom hemorrhagins.Cloning of a salivary gland metalloprotease and characterization of gelatinase and fibrin(ogen)lytic activities in the saliva of the Lyme disease tick vector Ixodes scapularisThe glycoprotein B disintegrin-like domain binds beta 1 integrin to mediate cytomegalovirus entry.Snake-venom resistance as a mammalian trophic adaptation: lessons from didelphid marsupials.cDNA cloning of a snake venom metalloproteinase from the eastern diamondback rattlesnake (Crotalus adamanteus), and the expression of its disintegrin domain with anti-platelet effects.Crystal structures of VAP1 reveal ADAMs' MDC domain architecture and its unique C-shaped scaffoldAnalysis of the salivary gland transcriptome of Frankliniella occidentalis.Venom proteins of the parasitoid wasp Nasonia vitripennis: recent discovery of an untapped pharmacopee.The venom gland transcriptome of the parasitoid wasp Nasonia vitripennis highlights the importance of novel genes in venom functionSnake venoms and hemostasis.Gene expression profiling of the venom gland from the Venezuelan mapanare (Bothrops colombiensis) using expressed sequence tags (ESTs).The disulphide bond pattern of bitistatin, a disintegrin isolated from the venom of the viper Bitis arietans.Genetic Basis for Variation of Metalloproteinase-Associated Biochemical Activity in Venom of the Mojave Rattlesnake (Crotalus scutulatus scutulatus).Inhibition of neutrophil function by two tick salivary proteinsSnake venom disintegrins and cell migration.Privileged frameworks from snake venom.Immunohistochemical changes in kidney glomerular and tubular proteins caused by rattlesnake (Crotalus vegrandis) venom.A limited role for gene duplications in the evolution of platypus venomAmino acid sequence and homology modeling of obtustatin, a novel non-RGD-containing short disintegrin isolated from the venom of Vipera lebetina obtusa.Cooperation of the metalloprotease, disintegrin, and cysteine-rich domains of ADAM12 during inhibition of myogenic differentiation.Cysteine-rich domain of human ADAM 12 (meltrin alpha) supports tumor cell adhesionSnake venom disintegrins: novel dimeric disintegrins and structural diversification by disulphide bond engineering.Analysis of the roles of RGD-binding integrins, alpha(4)/alpha(9) integrins, alpha(6) integrins, and CD9 in the interaction of the fertilin beta (ADAM2) disintegrin domain with the mouse egg membrane.The reprolysin jararhagin, a snake venom metalloproteinase, functions as a fibrillar collagen agonist involved in fibroblast cell adhesion and signaling.Understanding Biological Roles of Venoms Among the Caenophidia: The Importance of Rear-Fanged Snakes.Insularinase A, a prothrombin activator from Bothrops insularis venom, is a metalloprotease derived from a gene encoding protease and disintegrin domains.Pyrosequencing the salivary transcriptome ofHaemadipsa interrupta(Annelida: Clitellata: Haemadipsidae): anticoagulant diversity and insight into the evolution of anticoagulation capabilities in leeches
P2860
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P2860
Snake venom metalloproteinases: structure, function and relationship to the ADAMs family of proteins.
description
1996 nî lūn-bûn
@nan
1996 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1996 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
name
Snake venom metalloproteinases ...... the ADAMs family of proteins.
@ast
Snake venom metalloproteinases ...... the ADAMs family of proteins.
@en
type
label
Snake venom metalloproteinases ...... the ADAMs family of proteins.
@ast
Snake venom metalloproteinases ...... the ADAMs family of proteins.
@en
prefLabel
Snake venom metalloproteinases ...... the ADAMs family of proteins.
@ast
Snake venom metalloproteinases ...... the ADAMs family of proteins.
@en
P2093
P1433
P1476
Snake venom metalloproteinases ...... the ADAMs family of proteins.
@en
P2093
P304
P356
10.1016/S0041-0101(96)00108-0
P577
1996-11-01T00:00:00Z