Bacterial Chaperones CsgE and CsgC Differentially Modulate Human α-Synuclein Amyloid Formation via Transient Contacts.
Amyloid formation is historically associated with cytotoxicity, but many organisms produce functional amyloid fibers (e.g., curli) as a normal part of cell biology. Two E. coli genes in the curli operon encode the chaperone-like proteins CsgC and CsgE that both can reduce in vitro amyloid formation...
Main Authors: | Erik Chorell, Emma Andersson, Margery L Evans, Neha Jain, Anna Götheson, Jörgen Åden, Matthew R Chapman, Fredrik Almqvist, Pernilla Wittung-Stafshede |
---|---|
Format: | Article |
Language: | English |
Published: |
Public Library of Science (PLoS)
2015-01-01
|
Series: | PLoS ONE |
Online Access: | http://europepmc.org/articles/PMC4605646?pdf=render |
Similar Items
-
Structure-Function Analysis of the Curli Accessory Protein CsgE Defines Surfaces Essential for Coordinating Amyloid Fiber Formation
by: Roger D. Klein, et al.
Published: (2018-07-01) -
csg2csg: A TOOL TO ASSIST VALIDATION & VERIFICATION
by: Davis Andrew, et al.
Published: (2021-01-01) -
The direct rendering of CSG objects
by: HUANG, WEN-ZHE, et al.
Published: (1992) -
Adaptive polygonization of CSG-Solid
by: cheng, chi-hong, et al.
Published: (1996) -
Efficient Polygonization of CSG Solids
by: Chung-Wen Chung, et al.
Published: (1995)