About: Activated protein C cleavage of factor Va leads to dissociation of the A2 domain

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About: Activated protein C cleavage of factor Va leads to dissociation of the A2 domain Goto Sponge NotDistinct Permalink

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scientific article published on 01 August 1997

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в серпні 1997 (uk) article scientifique publié en 1997 (fr) im August 1997 veröffentlichter wissenschaftlicher Artikel (de) artículu científicu espublizáu n'agostu de 1997 (ast) scientific article published on 01 August 1997 (en)
publication date	wds:Q73575454-642D8B24-23AA-4CA3-9053-8F5BBEEA0F17
publication date	1997-08-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q73575454-874101A6-CAB9-4C8D-BA64-0279A49B0F17
language of work or name	English
cites work	wds:Q73575454-06B911F1-4FE4-4A39-BB91-C176FFDE7D42 wds:Q73575454-0DC32EC0-A594-4F77-B084-B86CFDA8DF87 wds:Q73575454-851CEB83-064D-4EC5-AE9C-EB59A6F0F72E wds:Q73575454-89562776-45FC-4080-AD3E-2EE898A9CE2F wds:Q73575454-A01992AC-EFB2-4BCB-9862-1AA4F4E08EAF wds:Q73575454-A8708753-707D-495B-890C-3E5D99B8C554 wds:Q73575454-A8C829C2-8BDE-427E-AAFC-4A8F106F330F wds:Q73575454-BA66E7F7-6561-4AC1-89F5-C8053EC67BBC wds:Q73575454-D9AA7778-B8D4-4236-AADF-0637720FA90C wds:Q73575454-E2EB0FC9-4D93-46CB-AFF4-E5373CA99A56 wds:Q73575454-E46EF7C3-1700-4803-ABA7-6BC2C7A37185 wds:Q73575454-EC9D320D-7912-4E0E-8A4F-EBC586BB0B11 wds:Q73575454-EFA39097-3D32-4D24-9841-7F9013B5B0F6 wds:Q73575454-F48ACC53-D1CA-469B-8FED-ADBCFC012A8D wds:Q73575454-F9242BAD-2EF2-4A5F-B4D9-99313529B251
cites work	The inhibition of blood coagulation by activated protein C through the selective inactivation of activated factor V Molecular cloning of a cDNA encoding human antihaemophilic factor Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4 EQUILIBRIUM ULTRACENTRIFUGATION OF DILUTE SOLUTIONS Factor V Interactions of a fluorescent active-site-directed inhibitor of thrombin: dansylarginine N-(3-ethyl-1,5-pentanediyl)amide Interaction of clotting factor V heavy chain with prothrombin and prethrombin 1 and role of activated protein C in regulating this interaction: analysis by analytical ultracentrifugation A simple method for the preparation of homogeneous phospholipid vesicles Human plasma protein C: isolation, characterization, and mechanism of activation by alpha-thrombin Isolation of functional human coagulation factor V by using a hybridoma antibody Boundary analysis in sedimentation transport experiments: a procedure for obtaining sedimentation coefficient distributions using the time derivative of the concentration profile Peptide bond cleavages and loss of functional activity during inactivation of factor Va and factor VaR506Q by activated protein C. Effects of protein S and factor Xa on peptide bond cleavages during inactivation of factor Va and factor VaR506Q by activated protein C Structure of bovine blood coagulation factor Va. Determination of the subunit associations, molecular weights, and asymmetries by analytical ultracentrifugation Determination of the disulfide bridges in factor Va light chain
author name string	wds:Q73575454-8F8D0672-6264-4F6C-B715-0F4D0E029308 wds:Q73575454-98646B96-BC6C-455C-A366-AF08AD165802 wds:Q73575454-F2971663-4533-456A-9E75-204FCE34D33C wds:Q73575454-F63DB474-482F-41E3-A38F-40BBDFD15975
author name string	K G Mann M Kalafatis K J Begin M F Hockin
rdfs:label	Activated protein C cleavage of factor Va leads to dissociation of the A2 domain (en) Activated protein C cleavage of factor Va leads to dissociation of the A2 domain (nl)
skos:prefLabel	Activated protein C cleavage of factor Va leads to dissociation of the A2 domain (en) Activated protein C cleavage of factor Va leads to dissociation of the A2 domain (nl)
name	Activated protein C cleavage of factor Va leads to dissociation of the A2 domain (en) Activated protein C cleavage of factor Va leads to dissociation of the A2 domain (nl)
title	wds:Q73575454-69082849-C207-4A22-A451-3452E89E67EF
title	Activated protein C cleavage of factor Va leads to dissociation of the A2 domain (en)
page(s)	wds:Q73575454-DE23E5EA-46A6-4C87-9AE0-62F6E3781C2A
page(s)	20678-20683
instance of	wds:Q73575454-736DB851-C28D-4B51-99F0-C608CA6EADBA
instance of	scholarly article
main subject	wds:Q73575454-074F83DF-78E9-4F01-8205-822EBBC0A8ED
main subject	drotrecogin alfa
PubMed ID	wds:Q73575454-925339BE-2003-4F39-967B-EA498803AA81
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/9252387
PubMed ID	9252387
published in	wds:Q73575454-9478790E-F642-470C-9119-723F9FE0FE6C
published in	Journal of Biological Chemistry
issue	wds:Q73575454-F8A8BC36-4D00-4EB5-BC3F-9ED81BECFE26
volume	wds:Q73575454-021E1D4D-6AD2-403E-89A0-5735E6364C7E
issue	33
volume	272
number of pages	wds:Q73575454-D696B2DF-B845-4E8C-9385-4E9A9E9576BE
number of pages	6 (xsd:decimal)
DOI	wds:Q73575454-BFFBBA3D-7E10-4095-9EE1-57DB11033239
DOI	http://dx.doi.org/10.1074/JBC.272.33.20678
DOI	10.1074/JBC.272.33.20678
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q73575454
is cites work of	Regulation of blood coagulation Systemic blood coagulation activation in acute coronary syndromes The Contribution of Amino Acid Region Asp695-Tyr698 of Factor V to Procofactor Activation and Factor Va Function Amino Acids Glu323, Tyr324, Glu330, and Val331 of Factor Va Heavy Chain Are Essential for Expression of Cofactor Activity Structural requirements for expression of factor Va activity A chimeric protein C containing the prothrombin Gla domain exhibits increased anticoagulant activity and altered phospholipid specificity. Crystal structure of the prothrombinase complex from the venom of Pseudonaja textilis Importance of protein S and phospholipid for activated protein C-mediated cleavages in factor Va. Cellular regulation of blood coagulation: a model for venous stasis Interdomain engineered disulfide bond permitting elucidation of mechanisms of inactivation of coagulation factor Va by activated protein C Factor Va is inactivated by activated protein C in the absence of cleavage sites at Arg-306, Arg-506, and Arg-679. Binding site for blood coagulation factor Xa involving residues 311-325 in factor Va. Modeling of human factor Va inactivation by activated protein C. Mechanism of factor Va inactivation by plasmin. Loss of A2 and A3 domains from a Ca2+-dependent complex of fragments bound to phospholipid Down regulation of prothrombinase by activated protein C during prothrombin activation Activated protein C cofactor function of protein S: a critical role for Asp95 in the EGF1-like domain Venom factor V from the common brown snake escapes hemostatic regulation through procoagulant adaptations. Cleavage at both Arg306 and Arg506 is required and sufficient for timely and efficient inactivation of factor Va by activated protein C. Blood coagulation factor Va's key interactive residues and regions for prothrombinase assembly and prothrombin binding
is cites work of	wds:Q44467155-C6101273-A4E1-45DA-A3F0-DC4AA440921A wds:Q44683596-A116FA2A-022F-4C4D-B260-432B91735A7B wds:Q37116951-15BE733B-9EC3-42DD-A24A-A790FCFE3255

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