Examining thrombin hydrolysis of the factor XIII activation peptide segment leads to a proposal for explaining the cardioprotective effects observed with the factor XIII V34L mutation

Examining thrombin hydrolysis of the factor XIII activation peptide segment leads to a proposal for explaining the cardioprotective effects observed with the factor XIII V34L mutation

Item
http://www.wikidata.org/entity/Q28115016
Interaction of the factor XIII activation peptide with alpha -thrombin. Crystal structure of its enzyme-substrate analog complexBiophysical investigation of GpIbalpha binding to thrombin anion binding exosite II.Structure-based predictive models for allosteric hot spots.Gene polymorphisms of the haemostatic system and the risk of arterial thrombotic disease.Molecular mechanisms affecting fibrin structure and stability.Factor XIIIA-V34L and factor XIIIB-H95R gene variants: effects on survival in myocardial infarction patients.Genetic markers of cardiovascular disease in rheumatoid arthritis.Associations of the beta-fibrinogen Hae III and factor XIII Val34Leu gene variants with venous thrombosis.Ligand binding to anion-binding exosites regulates conformational properties of thrombin.Design of Factor XIII V34X activation peptides to control ability to interact with thrombin mutants.Genetic predictors of response to photodynamictherapy.A quantitative systems pharmacology model of blood coagulation network describes in vivo biomarker changes in non-bleeding subjects.Effects of introducing fibrinogen Aalpha character into the factor XIII activation peptide segment.Probing thrombin's ability to accommodate a V34F substitution within the factor XIII activation peptide segment (28-41).The protective effect of the factor XIII Val34Leu mutation on the risk of deep venous thrombosis is dependent on the fibrinogen level.Coagulation F13A1 V34L, fibrinogen and homocysteine versus conventional risk factors in the pathogenesis of MI in young persons.Screening cleavage of Factor XIII V34X Activation Peptides by thrombin mutants: A strategy for controlling fibrin architecture.
P2860

Examining thrombin hydrolysis of the factor XIII activation peptide segment leads to a proposal for explaining the cardioprotective effects observed with the factor XIII V34L mutation

Item
http://www.wikidata.org/entity/Q28115016
description
2000 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
article publié dans la revue scientifique Journal of Biological Chemistry
@fr
artículu científicu espublizáu en 2000
@ast
im Juli 2000 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2000/07/07)
@sk
vědecký článek publikovaný v roce 2000
@cs
wetenschappelijk artikel (gepubliceerd op 2000/07/07)
@nl
наукова стаття, опублікована в липні 2000
@uk
name
Examining thrombin hydrolysis ...... the factor XIII V34L mutation
@ast
Examining thrombin hydrolysis ...... the factor XIII V34L mutation
@en
Examining thrombin hydrolysis ...... the factor XIII V34L mutation
@nl
type
label
Examining thrombin hydrolysis ...... the factor XIII V34L mutation
@ast
Examining thrombin hydrolysis ...... the factor XIII V34L mutation
@en
Examining thrombin hydrolysis ...... the factor XIII V34L mutation
@nl
prefLabel
Examining thrombin hydrolysis ...... the factor XIII V34L mutation
@ast
Examining thrombin hydrolysis ...... the factor XIII V34L mutation
@en
Examining thrombin hydrolysis ...... the factor XIII V34L mutation
@nl
P1433
P1476
P2093
P2860
P304
P31
P356
P407
P433
P478
P577
P5875
P698
P356
P1433
P1476
Examining thrombin hydrolysis ...... the factor XIII V34L mutation
@en
P2093
P2860
P304
P31
P356
P407
P433
P478
P577
P5875
P698