Linked Life Data

19388581

Source:http://linkedlifedata.com/resource/pubmed/id/19388581

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-4
pubmed:dateCreated
2009-4-24
pubmed:abstractText
Biochemistry and pharmacology of snake venoms reveal structural and functional polymorphisms of proteins they contain. These lead their effects by their enzymatic activities (proteases, phospholipases A2, L-amino acid oxydases...) or by binding to membrane receptors. Disintegrin from snake venoms play a role as antagonists of cell adhesion and migration by binding integrins and blocking their function. Characterization of integrin antagonists from snake venom allows us understanding the function of some integrins providing new information to develop new therapeutic agents. In this review, we report classification and therapeutic implications of disintegrins. In particular the structural and the functional characteristics of lebestatin; a short disintegrin isolated from Tunisian Macrovipera lebetina snake venom.
pubmed:language
fre
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0020-2509
pubmed:author
pubmed:issnType
Print
pubmed:volume
84
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
29-37
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
[Snake venom disintegrins: classification and therapeutic potential].
pubmed:affiliation
Laboratoire des Venins et Toxines, Institut Pasteur de Tunis, 13 Place Pasteur, 1002 Tunis Belvédère, Tunisie.
pubmed:publicationType
Journal Article, English Abstract, Review