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- W2894401039 abstract "Abstract This study aimed to elucidate anticoagulant/antiplatelet mechanisms of two previously purified PLA 2 s from Cerastes cerastes venom, here, termed Cc 1 ‐PLA 2 and Cc 2 ‐PLA 2 . Both PLA 2 s present close molecular weights of 13,534 and 13,430 Da and Isoectric pH (pI) 7.38 and 7.86 respectively, for Cc 1 ‐PLA 2 and Cc 2 ‐PLA 2 . These Ca 2+ ‐dependent enzymes showed a high catalytic activity upon phospholipids, inducing indirect hemolysis, since they conserve the catalytic domain of PLA 2 s 26 CYCGWGGKG 34 . They exhibited dual inhibition of platelet aggregation by targeting P 2 Y 12 and TPα receptors preventing Adenosine diphosphate/arachidonate binding and blood clotting. These effects are due to the interaction of Cc 1 ‐PLA 2 s/Cc 2 ‐PLA 2 s with factor FXa through a noncatalytic PL‐independent mechanism leading to nonreleased thrombin. Both proteins consist of 120 amino acid residues and share similar three‐dimensional structures close to other SV‐PLA 2 s. Structural data of PLA 2 s allowed the relevant residues involved in binding to FXa and platelet receptors. These findings may lead to the design of novel noncompetitive FXa inhibitors." @default.
- W2894401039 created "2018-10-05" @default.
- W2894401039 creator A5003600698 @default.
- W2894401039 creator A5081929184 @default.
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- W2894401039 date "2018-09-21" @default.
- W2894401039 modified "2023-09-25" @default.
- W2894401039 title "Antiplatelet and anticoagulant activities of two phospholipase A2s purified from <i>Cerastes cerastes</i> venom: Structure‐function relationship" @default.
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- W2894401039 doi "https://doi.org/10.1002/jbt.22219" @default.
- W2894401039 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/30239061" @default.
- W2894401039 hasPublicationYear "2018" @default.
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