Venom factor V from the common brown snake escapes hemostatic regulation through procoagulant adaptations.
about
Crystal structure of the prothrombinase complex from the venom of Pseudonaja textilisThe molecular basis of factor V and VIII procofactor activationProcoagulant adaptation of a blood coagulation prothrombinase-like enzyme complex in australian elapid venom.Blood coagulation factors V and VIII: Molecular Mechanisms of Procofactor Activation.A bipartite autoinhibitory region within the B-domain suppresses function in factor VConservative mutations in the C2 domains of factor VIII and factor V alter phospholipid binding and cofactor activity.Engineered factor Xa variants retain procoagulant activity independent of direct factor Xa inhibitors.Venom down under: dynamic evolution of Australian elapid snake toxins.Factor deficiencies in venom-induced consumption coagulopathy resulting from Australian elapid envenomation: Australian Snakebite Project (ASP-10).
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P2860
Venom factor V from the common brown snake escapes hemostatic regulation through procoagulant adaptations.
description
article científic
@ca
article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on 13 April 2009
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
@cs
name
Venom factor V from the common ...... ough procoagulant adaptations.
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Venom factor V from the common ...... ough procoagulant adaptations.
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type
label
Venom factor V from the common ...... ough procoagulant adaptations.
@en
Venom factor V from the common ...... ough procoagulant adaptations.
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prefLabel
Venom factor V from the common ...... ough procoagulant adaptations.
@en
Venom factor V from the common ...... ough procoagulant adaptations.
@nl
P2093
P2860
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Venom factor V from the common ...... rough procoagulant adaptations
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John de Jersey
Liam St Pierre
Martin F Lavin
Michael Boltz
Paul P Masci
Rodney M Camire
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P304
P356
10.1182/BLOOD-2009-02-202663
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P50
P577
2009-04-13T00:00:00Z