Catalysis of protein folding by chaperones in pathogenic bacteria
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Fiber formation across the bacterial outer membrane by the chaperone/usher pathwayInsights into pilus assembly and secretion from the structure and functional characterization of usher PapCDesign and Synthesis of C-2 Substituted Thiazolo and Dihydrothiazolo Ring-Fused 2-Pyridones: Pilicides with Increased Antivirulence ActivityStructural and Functional Characterization of Pseudomonas aeruginosa CupB ChaperonesThe Structure of the PapD-PapGII Pilin Complex Reveals an Open and Flexible P5 PocketQuality control of disulfide bond formation in pilus subunits by the chaperone FimCPeriplasmic peptidyl prolyl cis-trans isomerases are not essential for viability, but SurA is required for pilus biogenesis in Escherichia coliThe extracytoplasmic adaptor protein CpxP is degraded with substrate by DegP.Protein secretion in the absence of ATP: the autotransporter, two-partner secretion and chaperone/usher pathways of gram-negative bacteria (review).Structural biology of the chaperone-usher pathway of pilus biogenesisRationally designed small compounds inhibit pilus biogenesis in uropathogenic bacteria.Structural Insight into Archaic and Alternative Chaperone-Usher Pathways Reveals a Novel Mechanism of Pilus Biogenesis.FGL chaperone-assembled fimbrial polyadhesins: anti-immune armament of Gram-negative bacterial pathogens.A tale of two pili: assembly and function of pili in bacteria.Two-step and one-step secretion mechanisms in Gram-negative bacteria: contrasting the type IV secretion system and the chaperone-usher pathway of pilus biogenesis.Adhesive organelles of Gram-negative pathogens assembled with the classical chaperone/usher machinery: structure and function from a clinical standpoint.Bacterial surface appendages as targets for novel antibacterial therapeutics.Development of antivirulence compounds: a biochemical review.Impairment of the biomechanical compliance of P pili: a novel means of inhibiting uropathogenic bacterial infections?Off-pathway assembly of fimbria subunits is prevented by chaperone CfaA of CFA/I fimbriae from enterotoxigenic E. coli.Carboxylic acid isosteres improve the activity of ring-fused 2-pyridones that inhibit pilus biogenesis in E. coli.Synthesis and application of a bromomethyl substituted scaffold to be used for efficient optimization of anti-virulence activity.
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P2860
Catalysis of protein folding by chaperones in pathogenic bacteria
description
article científic
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article scientifique
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articolo scientifico
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artigo científico
@pt
bilimsel makale
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scientific article published on 06 December 2004
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Catalysis of protein folding by chaperones in pathogenic bacteria
@en
Catalysis of protein folding by chaperones in pathogenic bacteria.
@nl
type
label
Catalysis of protein folding by chaperones in pathogenic bacteria
@en
Catalysis of protein folding by chaperones in pathogenic bacteria.
@nl
prefLabel
Catalysis of protein folding by chaperones in pathogenic bacteria
@en
Catalysis of protein folding by chaperones in pathogenic bacteria.
@nl
P2093
P2860
P356
P1476
Catalysis of protein folding by chaperones in pathogenic bacteria
@en
P2093
Carl Frieden
James G Bann
Jerome S Pinkner
Scott J Hultgren
P2860
P304
17389-17393
P356
10.1073/PNAS.0408072101
P407
P577
2004-12-06T00:00:00Z