Cargando…
Slow Escape from a Helical Misfolded State of the Pore-Forming Toxin Cytolysin A
[Image: see text] The pore-forming toxin cytolysin A (ClyA) is expressed as a large α-helical monomer that, upon interaction with membranes, undergoes a major conformational rearrangement into the protomer conformation, which then assembles into a cytolytic pore. Here, we investigate the folding kin...
Autores principales: | Dingfelder, Fabian, Macocco, Iuri, Benke, Stephan, Nettels, Daniel, Faccioli, Pietro, Schuler, Benjamin |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American
Chemical Society
2021
|
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8397351/ https://www.ncbi.nlm.nih.gov/pubmed/34467360 http://dx.doi.org/10.1021/jacsau.1c00175 |
Ejemplares similares
-
The assembly dynamics of the cytolytic pore toxin ClyA
por: Benke, Stephan, et al.
Publicado: (2015) -
Erratum: The assembly dynamics of the cytolytic pore toxin ClyA
por: Benke, Stephan, et al.
Publicado: (2016) -
Curcumin Inhibits Membrane-Damaging Pore-Forming Function of the β-Barrel Pore-Forming Toxin Vibrio cholerae Cytolysin
por: Singh, Mahendra, et al.
Publicado: (2022) -
An oomycete NLP cytolysin forms transient small pores in lipid membranes
por: Pirc, Katja, et al.
Publicado: (2022) -
Glu289 residue in the pore-forming motif of Vibrio cholerae cytolysin is important for efficient β-barrel pore formation
por: Mondal, Anish Kumar, et al.
Publicado: (2022)