PapD-like chaperones provide the missing information for folding of pilin proteins. - Wikidata - wikimedia - TriplyDB

PapD-like chaperones provide the missing information for folding of pilin proteins.

PapD-like chaperones provide the missing information for folding of pilin proteins.

http://www.wikidata.org/entity/Q35166061

about

Crystal structure of the FimD usher bound to its cognate FimC-FimH substrate SipA is required for pilus formation in Streptococcus pyogenes serotype M3 Protein quality control in the bacterial periplasm Adhesive Pili in UTI Pathogenesis and Drug Development Structural basis of tropism of Escherichia coli to the bladder during urinary tract infection Crystal Structure of the P Pilus Rod Subunit PapA Fiber formation across the bacterial outer membrane by the chaperone/usher pathway Insights into pilus assembly and secretion from the structure and functional characterization of usher PapC Structure of CFA/I fimbriae from enterotoxigenic Escherichia coli The Structure of the PapD-PapGII Pilin Complex Reveals an Open and Flexible P5 Pocket The structure of the CS1 pilus of enterotoxigenic Escherichia coli reveals structural polymorphism.The Vibrio cholerae Colonization Factor GbpA Possesses a Modular Structure that Governs Binding to Different Host Surfaces Quality control of disulfide bond formation in pilus subunits by the chaperone FimC Crystal structure of enterotoxigenic Escherichia coli colonization factor CS6 reveals a novel type of functional assembly Structural and adhesive properties of the long polar fimbriae protein LpfD from adherent-invasive Escherichia coli Hybrid Structure of the Type 1 Pilus of Uropathogenic Escherichia coli Structural basis for Myf and Psa fimbriae-mediated tropism of pathogenic strains of Yersinia for host tissues Cpx signaling pathway monitors biogenesis and affects assembly and expression of P pili The chaperone/usher pathways of Pseudomonas aeruginosa: identification of fimbrial gene clusters (cup) and their involvement in biofilm formation Structural insight into host recognition by aggregative adherence fimbriae of enteroaggregative Escherichia coli Analysis of the unique structural and physicochemical properties of the DraD/AfaD invasin in the context of its belonging to the family of chaperone/usher type fimbrial subunits.Topology of the outer membrane usher PapC determined by site-directed fluorescence labeling.Bacterial outer membrane ushers contain distinct targeting and assembly domains for pilus biogenesis.Structure of a Chaperone-Usher Pilus Reveals the Molecular Basis of Rod Uncoiling.Chaperone function of FkpA, a heat shock prolyl isomerase, in the periplasm of Escherichia coli.Construction, analysis, and beta-glucanase screening of a bacterial artificial chromosome library from the large-bowel microbiota of mice.FimH adhesin of type 1 fimbriae is a potent inducer of innate antimicrobial responses which requires TLR4 and type 1 interferon signalling.Real-time and equilibrium (19)F-NMR studies reveal the role of domain-domain interactions in the folding of the chaperone PapD.Periplasmic peptidyl prolyl cis-trans isomerases are not essential for viability, but SurA is required for pilus biogenesis in Escherichia coli Structure and function of Escherichia coli type 1 pili: new insight into the pathogenesis of urinary tract infections.Molecular strategies for fimbrial expression and assembly.Transcription elongation factor GreA has functional chaperone activity The minor pilin subunit Sgp2 is necessary for assembly of the pilus encoded by the srtG cluster of Streptococcus suis.Pilicides inhibit the FGL chaperone/usher assisted biogenesis of the Dr fimbrial polyadhesin from uropathogenic Escherichia coli Contributions of chaperone/usher systems to cell binding, biofilm formation and Yersinia pestis virulence.Structural biology of the chaperone-usher pathway of pilus biogenesis Snapshots of usher-mediated protein secretion and ordered pilus assembly.Rationally designed small compounds inhibit pilus biogenesis in uropathogenic bacteria.Molecular mechanism of P pilus termination in uropathogenic Escherichia coli Lipase-specific foldases.

P2860

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P2860

PapD-like chaperones provide the missing information for folding of pilin proteins.

http://www.wikidata.org/entity/Q35166061

description

2000 nî lūn-bûn

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2000 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

2000 թվականի հուլիսին հրատարակված գիտական հոդված

@hy

2000年の論文

@ja

2000年論文

@yue

2000年論文

@zh-hant

2000年論文

@zh-hk

2000年論文

@zh-mo

2000年論文

@zh-tw

2000年论文

@wuu

name

PapD-like chaperones provide the missing information for folding of pilin proteins.

@ast

PapD-like chaperones provide the missing information for folding of pilin proteins.

@en

type

label

PapD-like chaperones provide the missing information for folding of pilin proteins.

@ast

PapD-like chaperones provide the missing information for folding of pilin proteins.

@en

prefLabel

PapD-like chaperones provide the missing information for folding of pilin proteins.

@ast

PapD-like chaperones provide the missing information for folding of pilin proteins.

@en

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P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

PapD-like chaperones provide the missing information for folding of pilin proteins.

@en

P2093

C Frieden

http://www.w3.org/2001/XMLSchema#string

F G Sauer

http://www.w3.org/2001/XMLSchema#string

G E Soto

http://www.w3.org/2001/XMLSchema#string

G Waksman

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J S Pinkner

http://www.w3.org/2001/XMLSchema#string

M M Barnhart

http://www.w3.org/2001/XMLSchema#string

S J Hultgren

http://www.w3.org/2001/XMLSchema#string

S Langermann

http://www.w3.org/2001/XMLSchema#string

P2860

Type 1 fimbrial expression enhances Escherichia coli virulence for the urinary tract

Structural basis of chaperone function and pilus biogenesis

X-ray structure of the FimC-FimH chaperone-adhesin complex from uropathogenic Escherichia coli

Crystal structure of chaperone protein PapD reveals an immunoglobulin fold

The crystal structure of the bacterial chaperonin GroEL at 2.8 A

NMR solution structure of the periplasmic chaperone FimC

Structure of alpha-lytic protease complexed with its pro region

Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter

Vaccination with FimH adhesin protects cynomolgus monkeys from colonization and infection by uropathogenic Escherichia coli

Prevention of mucosal Escherichia coli infection by FimH-adhesin-based systemic vaccination

P304

7709-7714

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P31

scholarly article

P356

10.1073/PNAS.130183897

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P407

P433

14

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P478

97

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P577

2000-07-01T00:00:00Z

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12460020

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P698

10859353

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P921

molecular chaperones

protein folding

P932

16609

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