The factor VII zymogen structure reveals reregistration of beta strands during activation
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The 2.2-A crystal structure of human pro-granzyme K reveals a rigid zymogen with unusual featuresARNT PAS-B has a fragile native state structure with an alternative -sheet register nearby in sequence spaceCrystal structure of prethrombin-1Crystallographic and Kinetic Evidence of Allostery in a Trypsin-like ProteaseCrystal Structures of Prethrombin-2 Reveal Alternative Conformations under Identical Solution Conditions and the Mechanism of Zymogen ActivationCrystal Structure of aSchistosoma mansoniSeptin Reveals the Phenomenon of Strand Slippage in Septins Dependent on the Nature of the Bound NucleotideGenetic, molecular and functional analyses of complement factor I deficiencyConformational Changes of Congenital FVII Variants with Defective Binding to Tissue Factor ARG304GLN (FVII Padua), ARG 304TRP (FVII Nagoya) and ARG79GLN (FVII Shinjo or Tondabayashi).Engineering exosite peptides for complete inhibition of factor VIIa using a protease switch with substrate phage.Disulfide locked variants of factor VIIa with a restricted beta-strand conformation have enhanced enzymatic activityDirect observations of shifts in the β-sheet register of a protein-peptide complex using explicit solvent simulationsDiscovery methodology for the development of direct factor VIIa inhibitors.Allostery in trypsin-like proteases suggests new therapeutic strategies.Conformational selection in trypsin-like proteases.Exosites in the substrate specificity of blood coagulation reactions.Loop dynamics of the extracellular domain of human tissue factor and activation of factor VIIa.Protein anticoagulants targeting factor VIIa-tissue factor complex: a comprehensive review.The conformational switch from the factor X zymogen to protease state mediates exosite expression and prothrombinase assembly.The P303T mutation in the human factor VII (FVII) gene alters the conformational state of the enzyme and causes a severe functional deficiency.Prothrombinase assembly and S1 site occupation restore the catalytic activity of FXa impaired by mutation at the sodium-binding site.Coagulation factor binding orientation and dimerization may influence infectivity of adenovirus-coagulation factor complexes.Augmented intrinsic activity of Factor VIIa by replacement of residues 305, 314, 337 and 374: evidence of two unique mutational mechanisms of activity enhancement.A combined structural dynamics approach identifies a putative switch in factor VIIa employed by tissue factor to initiate blood coagulation.Antibody-induced enhancement of factor VIIa activity through distinct allosteric pathways.Fusion of two distinct peptide exosite inhibitors of Factor VIIa.A frequent human coagulation Factor VII mutation (A294V, c152) in loop 140s affects the interaction with activators, tissue factor and substrates.Assignment of molecular properties of a superactive coagulation factor VIIa variant to individual amino acid changes.Two new double mutant alleles of the F7 gene and a literature review on alleles with two mutations in FVII deficiency.Severe FVII deficiency caused by a new point mutation combined with a previously undetected gene deletion
P2860
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P2860
The factor VII zymogen structure reveals reregistration of beta strands during activation
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2001 nî lūn-bûn
@nan
2001 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
The factor VII zymogen structure reveals reregistration of beta strands during activation
@ast
The factor VII zymogen structure reveals reregistration of beta strands during activation
@en
The factor VII zymogen structure reveals reregistration of beta strands during activation
@nl
type
label
The factor VII zymogen structure reveals reregistration of beta strands during activation
@ast
The factor VII zymogen structure reveals reregistration of beta strands during activation
@en
The factor VII zymogen structure reveals reregistration of beta strands during activation
@nl
prefLabel
The factor VII zymogen structure reveals reregistration of beta strands during activation
@ast
The factor VII zymogen structure reveals reregistration of beta strands during activation
@en
The factor VII zymogen structure reveals reregistration of beta strands during activation
@nl
P2093
P1433
P1476
The factor VII zymogen structure reveals reregistration of beta strands during activation
@en
P2093
C Eigenbrot
D Kirchhofer
M H Ultsch
M S Dennis
R A Lazarus
P304
P356
10.1016/S0969-2126(01)00624-4
P577
2001-07-03T00:00:00Z