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Literature summary for 3.4.24.73 extracted from

  • Tanjoni, I.; Evangelista, K.; Della-Casa, M.S.; Butera, D.; Magalhaes, G.S.; Baldo, C.; Clissa, P.B.; Fernandes, I.; Eble, J.; Moura-da-Silva, A.M.
    Different regions of the class P-III snake venom metalloproteinase jararhagin are involved in binding to alpha2beta1 integrin and collagen (2010), Toxicon, 55, 1093-1099.
    View publication on PubMed

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular the enzyme is secreted Bothrops jararaca
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Bothrops jararaca jararhagin toxin binding to collagen appears to be sufficient to inhibit collagen-induced platelet aggregation in the human host ?
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?

Organism

Organism UniProt Comment Textmining
Bothrops jararaca
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Source Tissue

Source Tissue Comment Organism Textmining
venom
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Bothrops jararaca
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information jararhagin toxin binding to collagen appears to be sufficient to inhibit collagen-induced platelet aggregation in the human host Bothrops jararaca ?
-
?
additional information different regions of the class P-III snake venom metalloproteinase jararhagin are involved in binding to alpha2beta1 integrin, a collagen receptor, and collagen from host K-562 cells, analysis using monoclonal antibodies and recombinant jararhagin fragments, jararhagin binding to collagen and alpha2beta1 integrin occurs by two independent motifs located on disintegrin-like and cysteine-rich domains, respectively, detailed overview Bothrops jararaca ?
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?

General Information

General Information Comment Organism
additional information jararhagin toxin binding to collagen appears to be sufficient to inhibit collagen-induced platelet aggregation in the human host Bothrops jararaca