Cargando…
Disulfide bond formation during the folding of influenza virus hemagglutinin
To study the importance of individual sulfhydryl residues during the folding and assembly in vivo of influenza virus hemagglutinin (HA), we have constructed and expressed a series of mutant HA proteins in which cysteines involved in three disulfide bonds have been substituted by serine residues. Inv...
Formato: | Texto |
---|---|
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
1992
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2290053/ https://www.ncbi.nlm.nih.gov/pubmed/1321156 |
Ejemplares similares
-
Folding of influenza hemagglutinin in the endoplasmic reticulum
Publicado: (1991) -
PDI-Regulated Disulfide Bond Formation in Protein Folding and Biomolecular Assembly
por: Fu, Jiahui, et al.
Publicado: (2020) -
Conformational folding and disulfide bonding drive distinct stages of protein structure formation
por: Lv, Jian-Min, et al.
Publicado: (2018) -
Role of disulfide bond formation in the folding and assembly of the envelope glycoproteins of a pestivirus
por: Branza-Nichita, Norica, et al.
Publicado: (2002) -
Imbalance of heterologous protein folding and disulfide bond formation rates yields runaway oxidative stress
por: Tyo, Keith EJ, et al.
Publicado: (2012)