The crystal structure of activated protein C-inactivated bovine factor Va: Implications for cofactor function.
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Ceruloplasmin revisited: structural and functional roles of various metal cation-binding sitesCrystal structure of the bovine lactadherin C2 domain, a membrane binding motif, shows similarity to the C2 domains of factor V and factor VIIIThe tertiary structure and domain organization of coagulation factor VIIITrp2313-His2315 of Factor VIII C2 Domain Is Involved in Membrane Binding: STRUCTURE OF A COMPLEX BETWEEN THE C2 DOMAIN AND AN INHIBITOR OF MEMBRANE BINDINGDomain organization of membrane-bound factor VIII.Structure of the Discoidin Domain Receptor 1 Extracellular Region Bound to an Inhibitory Fab Fragment Reveals Features Important for SignalingContribution of Amino Acid Region 659−663 of Factor Va Heavy Chain to the Activity of Factor Xa within Prothrombinase,Computational modeling of laminin N-terminal domains using sparse distance constraints from disulfide bonds and chemical cross-linkingMolecular modeling indicates distinct classes of missense variants with mild and severe XLRS phenotypesA3 domain region 1803-1818 contributes to the stability of activated factor VIII and includes a binding site for activated factor IXMolecular modeling of retinoschisin with functional analysis of pathogenic mutations from human X-linked retinoschisis.The factor VIII C1 domain contributes to platelet bindingStructural investigation of zymogenic and activated forms of human blood coagulation factor VIII: a computational molecular dynamics studyThe domains of a cholesterol-dependent cytolysin undergo a major FRET-detected rearrangement during pore formationTaking the thrombin "fork".Factor VIII lacking the C2 domain retains cofactor activity in vitroModeling of human factor Va inactivation by activated protein C.Procoagulant adaptation of a blood coagulation prothrombinase-like enzyme complex in australian elapid venom.A Glu113Ala mutation within a factor VIII Ca2+-binding site enhances cofactor interactions in factor Xase.Accelerating membrane insertion of peripheral proteins with a novel membrane mimetic model.The co-translational folding and interactions of nascent protein chains: a new approach using fluorescence resonance energy transfer.A bipartite autoinhibitory region within the B-domain suppresses function in factor VThe structure of thrombin, a chameleon-like proteinase.The anticoagulant protein C pathway.Conservative mutations in the C2 domains of factor VIII and factor V alter phospholipid binding and cofactor activity.Inherited defects of coagulation factor V: the hemorrhagic side.Identification of 31 novel mutations in the F8 gene in Spanish hemophilia A patients: structural analysis of 20 missense mutations suggests new intermolecular binding sites.Contribution of A1 subunit residue Q316 in thrombin-activated factor VIII to A2 subunit dissociation.A phosphatidylserine binding site in factor Va C1 domain regulates both assembly and activity of the prothrombinase complex.Location of the multimerin 1 binding site in coagulation factor V: an update.Restoring the procofactor state of factor Va-like variants by complementation with B-domain peptidesAmino acid region 1000-1008 of factor V is a dynamic regulator for the emergence of procoagulant activity.Down-regulation of the clotting cascade by the protein C pathwayThe Dual Regulatory Role of Amino Acids Leu480 and Gln481 of Prothrombin.Mapping of the factor Xa binding site on factor Va by site-directed mutagenesisFactor VIII/V C-domain swaps reveal discrete C-domain roles in factor VIII function and intracellular trafficking.Role of the acidic hirudin-like COOH-terminal amino acid region of factor Va heavy chain in the enhanced function of prothrombinase.Factor VIII C1 domain spikes 2092-2093 and 2158-2159 comprise regions that modulate cofactor function and cellular uptake.Cooperative regulation of the activity of factor Xa within prothrombinase by discrete amino acid regions from factor Va heavy chain.Conformational change path between closed and open forms of C2 domain of coagulation factor V on a two-dimensional free-energy surface.
P2860
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P2860
The crystal structure of activated protein C-inactivated bovine factor Va: Implications for cofactor function.
description
2004 nî lūn-bûn
@nan
2004 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
The crystal structure of activ ...... cations for cofactor function.
@ast
The crystal structure of activ ...... cations for cofactor function.
@en
The crystal structure of activ ...... cations for cofactor function.
@nl
type
label
The crystal structure of activ ...... cations for cofactor function.
@ast
The crystal structure of activ ...... cations for cofactor function.
@en
The crystal structure of activ ...... cations for cofactor function.
@nl
prefLabel
The crystal structure of activ ...... cations for cofactor function.
@ast
The crystal structure of activ ...... cations for cofactor function.
@en
The crystal structure of activ ...... cations for cofactor function.
@nl
P2093
P2860
P356
P1476
The crystal structure of activ ...... cations for cofactor function.
@en
P2093
Kenneth G Mann
Matthew F Hockin
Stephen J Everse
Ty E Adams
P2860
P304
P356
10.1073/PNAS.0403072101
P407
P577
2004-06-07T00:00:00Z