Membrane targeting of a bacterial virulence factor harbouring an extended signal peptide. - Wikidata - awgldk - TriplyDB

Membrane targeting of a bacterial virulence factor harbouring an extended signal peptide.

Membrane targeting of a bacterial virulence factor harbouring an extended signal peptide.

http://www.wikidata.org/entity/Q54490543

about

Structure of the secretion domain of HxuA fromHaemophilus influenzae Pseudomonas aeruginosa uses a cyclic-di-GMP-regulated adhesin to reinforce the biofilm extracellular matrix Translocation path of a substrate protein through its Omp85 transporter.Conformational dynamics of protein transporter FhaC: large-scale motions of plug helix.The prodomain of the Bordetella two-partner secretion pathway protein FhaB remains intracellular yet affects the conformation of the mature C-terminal domain.Two-partner secretion of gram-negative bacteria: a single β-barrel protein enables transport across the outer membrane Type V Secretion: the Autotransporter and Two-Partner Secretion Pathways Topology and maturation of filamentous haemagglutinin suggest a new model for two-partner secretion.Virulence determinants involved in differential host niche adaptation of Neisseria meningitidis and Neisseria gonorrhoeae.Two-Partner Secretion: Combining Efficiency and Simplicity in the Secretion of Large Proteins for Bacteria-Host and Bacteria-Bacteria Interactions A novel sensor kinase is required for Bordetella bronchiseptica to colonize the lower respiratory tract New Insight into Filamentous Hemagglutinin Secretion Reveals a Role for Full-Length FhaB in Bordetella Virulence DegP Chaperone Suppresses Toxic Inner Membrane Translocation Intermediates.Natural-host animal models indicate functional interchangeability between the filamentous haemagglutinins of Bordetella pertussis and Bordetella bronchiseptica and reveal a role for the mature C-terminal domain, but not the RGD motif, during infecti Bordetella filamentous hemagglutinin and fimbriae: critical adhesins with unrealized vaccine potential.A functional two-partner secretion system contributes to adhesion of Neisseria meningitidis to epithelial cells.Meningococcal Two-Partner Secretion Systems and Their Association with Outcome in Patients with Meningitis Filamentous hemagglutinin of Bordetella pertussis: a key adhesin with immunomodulatory properties?YidC is involved in the biogenesis of the secreted autotransporter hemoglobin protease.Multiple signals direct the assembly and function of a type 1 secretion system An unusual signal peptide extension inhibits the binding of bacterial presecretory proteins to the signal recognition particle, trigger factor, and the SecYEG complex.Job contenders: roles of the β-barrel assembly machinery and the translocation and assembly module in autotransporter secretion.

P2860

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P2860

Membrane targeting of a bacterial virulence factor harbouring an extended signal peptide.

http://www.wikidata.org/entity/Q54490543

description

2004 nî lūn-bûn

@nan

2004年の論文

@ja

2004年学术文章

@wuu

2004年学术文章

@zh-cn

2004年学术文章

@zh-hans

2004年学术文章

@zh-my

2004年学术文章

@zh-sg

2004年學術文章

@yue

2004年學術文章

@zh

2004年學術文章

@zh-hant

name

Membrane targeting of a bacterial virulence factor harbouring an extended signal peptide.

@en

Membrane targeting of a bacterial virulence factor harbouring an extended signal peptide.

@nl

type

label

Membrane targeting of a bacterial virulence factor harbouring an extended signal peptide.

@en

Membrane targeting of a bacterial virulence factor harbouring an extended signal peptide.

@nl

prefLabel

Membrane targeting of a bacterial virulence factor harbouring an extended signal peptide.

@en

Membrane targeting of a bacterial virulence factor harbouring an extended signal peptide.

@nl

P1433

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P1476

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P2860

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P356

P1433

Journal of Molecular Microbiology and Biotechnology

P1476

Membrane targeting of a bacterial virulence factor harbouring an extended signal peptide.

@en

P2093

Eve Willery

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

Hans-Georg Koch

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

Karl-Ludwig Schimz

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

Matthias Müller

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

Michael Moser

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

Nina Chevalier

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

P2860

Crystal structure of the ribonucleoprotein core of the signal recognition particle

Subtilisin-like autotransporter serves as maturation protease in a bacterial secretion pathway.

Two-partner secretion in Gram-negative bacteria: a thrifty, specific pathway for large virulence proteins.

The great escape: structure and function of the autotransporter proteins.

Binding specificity of Escherichia coli trigger factor.

Escherichia coli translocase: the unravelling of a molecular machine.

Role of ADP-ribosyltransferase activity of pertussis toxin in toxin-adhesin redundancy with filamentous hemagglutinin during Bordetella pertussis infection

Biogenesis of inner membrane proteins in Escherichia coli.

The structural basis of protein targeting and translocation in bacteria.

Functional analysis of the signal recognition particle in Escherichia coli by characterization of a temperature-sensitive ffh mutant.

P304

7-18

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scholarly article

P356

10.1159/000082076

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P433

1

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8

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Françoise Jacob-Dubuisson

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2004-01-01T00:00:00Z

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P698

15741736

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