The E. coli CsgB nucleator of curli assembles to β-sheet oligomers that alter the CsgA fibrillization mechanism.
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Bacterial amyloid formation: structural insights into curli biogensisLegal but lethal: functional protein aggregation at the verge of toxicityTemperature-dependent structural changes of Parkinson's alpha-synuclein reveal the role of pre-existing oligomers in alpha-synuclein fibrillizationModulation of curli assembly and pellicle biofilm formation by chemical and protein chaperones.Promiscuous cross-seeding between bacterial amyloids promotes interspecies biofilms.CD14 protein acts as an adaptor molecule for the immune recognition of Salmonella curli fibers.Isolation, characterization, and aggregation of a structured bacterial matrix precursor.Solution NMR structure of CsgE: Structural insights into a chaperone and regulator protein important for functional amyloid formationCurli mediate bacterial adhesion to fibronectin via tensile multiple bondsThe bacterial amyloid curli is associated with urinary source bloodstream infection.The propensity of the bacterial rodlin protein RdlB to form amyloid fibrils determines its function in Streptomyces coelicolorGiving structure to the biofilm matrix: an overview of individual strategies and emerging common themes.Functional analysis of the accessory protein TapA in Bacillus subtilis amyloid fiber assembly.Protein folding in the cell envelope of Escherichia coli.Full-length TDP-43 forms toxic amyloid oligomers that are present in frontotemporal lobar dementia-TDP patients.A genomic region involved in the formation of adhesin fibers in Bacillus cereus biofilms.Understanding Curli Amyloid-Protein Aggregation by Hydrogen-Deuterium Exchange and Mass Spectrometry.Functional amyloids: interrelationship with other amyloids and therapeutic assessment to treat neurodegenerative diseases.Electrostatic lipid-protein interactions sequester the curli amyloid fold on the lipopolysaccharide membrane surface.Deamidation Slows Curli Amyloid-Protein Aggregation.Structure-Function Analysis of the Curli Accessory Protein CsgE Defines Surfaces Essential for Coordinating Amyloid Fiber FormationMultitasking of Hsp70 chaperone in the biogenesis of bacterial functional amyloidsProtein Co-Aggregation Related to Amyloids: Methods of Investigation, Diversity, and Classification
P2860
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P2860
The E. coli CsgB nucleator of curli assembles to β-sheet oligomers that alter the CsgA fibrillization mechanism.
description
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name
The E. coli CsgB nucleator of ...... CsgA fibrillization mechanism.
@ast
The E. coli CsgB nucleator of ...... CsgA fibrillization mechanism.
@en
type
label
The E. coli CsgB nucleator of ...... CsgA fibrillization mechanism.
@ast
The E. coli CsgB nucleator of ...... CsgA fibrillization mechanism.
@en
prefLabel
The E. coli CsgB nucleator of ...... CsgA fibrillization mechanism.
@ast
The E. coli CsgB nucleator of ...... CsgA fibrillization mechanism.
@en
P2093
P2860
P356
P1476
The E. coli CsgB nucleator of ...... CsgA fibrillization mechanism.
@en
P2093
Bradley Ford
Carl Frieden
Jerome S Pinkner
Scott J Hultgren
Scott L Crick
P2860
P304
P356
10.1073/PNAS.1204161109
P407
P577
2012-04-09T00:00:00Z