Cargando…
Assembly and routing of von Willebrand factor variants: the requirements for disulfide-linked dimerization reside within the carboxy-terminal 151 amino acids
The precursor protein of von Willebrand factor (pro-vWF) consists of four different repeated domains, denoted D1-D2-D'-D3-A1-A2-A3-D4-B1-B2- B3-C1-C2, followed by a carboxy-terminal region of 151 amino acids without obvious internal homology. Previously, we have shown the requirement of the dom...
Formato: | Texto |
---|---|
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
1991
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2288914/ https://www.ncbi.nlm.nih.gov/pubmed/2007623 |
Ejemplares similares
-
The disulfide bond Cys2724-Cys2774 in the C-terminal cystine knot domain of von Willebrand factor is critical for its dimerization and secretion
por: Zhang, Yuxin, et al.
Publicado: (2021) -
Autoregulation of von Willebrand factor function by a disulfide bond switch
por: Butera, Diego, et al.
Publicado: (2018) -
Terminal Platelet Production is Regulated by Von Willebrand Factor
por: Poirault-Chassac, Sonia, et al.
Publicado: (2013) -
Assembly Mechanism of Mucin and von Willebrand Factor Polymers
por: Javitt, Gabriel, et al.
Publicado: (2020) -
Inhibition of disulfide bonding of von Willebrand protein by monensin results in small, functionally defective multimers
Publicado: (1985)