Cargando…
Polylysine-Mediated Translocation of the Diphtheria Toxin Catalytic Domain through the Anthrax Protective Antigen Pore
[Image: see text] The protective antigen (PA) moiety of anthrax toxin forms oligomeric pores in the endosomal membrane, which translocate the effector proteins of the toxin to the cytosol. Effector proteins bind to oligomeric PA via their respective N-terminal domains and undergo N- to C-terminal tr...
Autores principales: | Sharma, Onkar, Collier, R. John |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American
Chemical Society
2014
|
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4230326/ https://www.ncbi.nlm.nih.gov/pubmed/25317832 http://dx.doi.org/10.1021/bi500985v |
Ejemplares similares
-
Atomic structure of anthrax PA pore elucidates toxin translocation
por: Jiang, Jiansen, et al.
Publicado: (2015) -
DARPins bind their cytosolic targets after having been translocated through the protective antigen pore of anthrax toxin
por: Becker, Lukas, et al.
Publicado: (2023) -
Disulfide Bonds in the Ectodomain of Anthrax Toxin Receptor 2 Are Required for the Receptor-Bound Protective-Antigen Pore to Function
por: Sun, Jianjun, et al.
Publicado: (2010) -
Electrostatic Ratchet in the Protective Antigen Channel Promotes Anthrax Toxin Translocation
por: Wynia-Smith, Sarah L., et al.
Publicado: (2012) -
Cellular Entry of the Diphtheria Toxin Does Not Require the Formation of the Open-Channel State by Its Translocation Domain
por: Ladokhin, Alexey S., et al.
Publicado: (2017)