Cargando…
High affinity binding of hydrophobic and autoantigenic regions of proinsulin to the 70 kDa chaperone DnaK
BACKGROUND: Chaperones facilitate proper folding of peptides and bind to misfolded proteins as occurring during periods of cell stress. Complexes of peptides with chaperones induce peptide-directed immunity. Here we analyzed the interaction of (pre)proinsulin with the best characterized chaperone of...
Autores principales: | Burkart, Volker, Siegenthaler, Rahel K, Blasius, Elias, Vandenbroeck, Koen, Alloza, Iraide, Fingberg, Waltraud, Schloot, Nanette C, Christen, Philipp, Kolb, Hubert |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2010
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2994776/ https://www.ncbi.nlm.nih.gov/pubmed/21059249 http://dx.doi.org/10.1186/1471-2091-11-44 |
Ejemplares similares
-
The Autoantigenic Proinsulin B-Chain Peptide B11-23 Synergises with the 70 kDa Heat Shock Protein DnaK in Macrophage Stimulation
por: Blasius, Elias, et al.
Publicado: (2018) -
Role of Mycoplasma Chaperone DnaK in Cellular Transformation
por: Benedetti, Francesca, et al.
Publicado: (2020) -
Influence of Escherichia coli chaperone DnaK on protein immunogenicity
por: Ratanji, Kirsty D., et al.
Publicado: (2016) -
The Molecular Chaperone DnaK Is a Source of Mutational Robustness
por: Aguilar-Rodríguez, José, et al.
Publicado: (2016) -
Reinkarnál dnak a részecskegyorsít k
Publicado: (2009)