von Willebrand factor: the complex molecular genetics of a multidomain and multifunctional protein.
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von Willebrand factor: the complex molecular genetics of a multidomain and multifunctional protein. / Schneppenheim, Reinhard; Budde, U.
in: J THROMB HAEMOST, Jahrgang 9 Suppl 1, 2011, S. 209-215.Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung
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TY - JOUR
T1 - von Willebrand factor: the complex molecular genetics of a multidomain and multifunctional protein.
AU - Schneppenheim, Reinhard
AU - Budde, U
PY - 2011
Y1 - 2011
N2 - von Willebrand disease (VWD), the most common inherited bleeding disorder in humans, is characterised by a prolonged bleeding time due to quantitative and/or functional deficits of von Willebrand factor (VWF), a huge multimeric protein. Given the large size and complexity of the protein, the many functions of VWF, for example, binding to collagen, to platelet GPIb, and to FVIII, the localisation of these binding sites in different VWF domains, as well as the dependence on a high molecular weight multimer structure for proper function, VWF is prone to quantitative and very heterogeneous structural and functional defects. Comprehensive clinical and laboratory phenotypic description of patients with VWD in correlation to the genotype has considerably increased our knowledge on this disorder and the physiology and pathophysiology of VWF. This article focuses on the phenotype/genotype relationship in VWD and the context of VWD types and subtypes with particular VWF domains.
AB - von Willebrand disease (VWD), the most common inherited bleeding disorder in humans, is characterised by a prolonged bleeding time due to quantitative and/or functional deficits of von Willebrand factor (VWF), a huge multimeric protein. Given the large size and complexity of the protein, the many functions of VWF, for example, binding to collagen, to platelet GPIb, and to FVIII, the localisation of these binding sites in different VWF domains, as well as the dependence on a high molecular weight multimer structure for proper function, VWF is prone to quantitative and very heterogeneous structural and functional defects. Comprehensive clinical and laboratory phenotypic description of patients with VWD in correlation to the genotype has considerably increased our knowledge on this disorder and the physiology and pathophysiology of VWF. This article focuses on the phenotype/genotype relationship in VWD and the context of VWD types and subtypes with particular VWF domains.
KW - Humans
KW - Mutation
KW - Genetic Testing
KW - Protein Conformation
KW - von Willebrand Diseases/diagnosis
KW - von Willebrand Factor/chemistry/genetics/physiology
KW - Humans
KW - Mutation
KW - Genetic Testing
KW - Protein Conformation
KW - von Willebrand Diseases/diagnosis
KW - von Willebrand Factor/chemistry/genetics/physiology
M3 - SCORING: Journal article
VL - 9 Suppl 1
SP - 209
EP - 215
JO - J THROMB HAEMOST
JF - J THROMB HAEMOST
SN - 1538-7933
ER -
