Gonococcal invasion of epithelial cells driven by P.IA, a bacterial ion channel with GTP binding properties.
about
Expression capable library for studies of Neisseria gonorrhoeae, version 1.0.Rho GTPases as pathogen targets: Focus on curable sexually transmitted infectionsStructure and function of the PorB porin from disseminating Neisseria gonorrhoeaeNeisseriae internalization by epithelial cells is enhanced by TLR2 stimulationIsolation of Neisseria gonorrhoeae mutants that show enhanced trafficking across polarized T84 epithelial monolayersInteractions of pathogenic Neisseria with host cells. Is it possible to assemble the puzzle?Host iron binding proteins acting as niche indicators for Neisseria meningitidisSequence polymorphism, predicted secondary structures, and surface-exposed conformational epitopes of Campylobacter major outer membrane protein.Role of ribosomal protein L12 in gonococcal invasion of Hec1B cells.Trends of the major porin gene (ompF) evolution: insight from the genus Yersinia.Genetic diversity and mosaicism at the por locus of Neisseria gonorrhoeae.Comparison of immune responses to gonococcal PorB delivered as outer membrane vesicles, recombinant protein, or Venezuelan equine encephalitis virus replicon particles.Meningococcal internalization into human endothelial and epithelial cells is triggered by the influx of extracellular L-glutamate via GltT L-glutamate ABC transporter in Neisseria meningitidisPilus phase variation switches gonococcal adherence to invasion by caveolin-1-dependent host cell signaling.The Pathobiology of Neisseria gonorrhoeae Lower Female Genital Tract Infection.Estradiol-Treated Female Mice as Surrogate Hosts for Neisseria gonorrhoeae Genital Tract Infections.Neisseria meningitidis porin PorB interacts with mitochondria and protects cells from apoptosisRole of lipooligosaccharide in Opa-independent invasion of Neisseria gonorrhoeae into human epithelial cells.Role of FNR and FNR-regulated, sugar fermentation genes in Neisseria meningitidis infectionPhosphoethanolamine residues on the lipid A moiety of Neisseria gonorrhoeae lipooligosaccharide modulate binding of complement inhibitors and resistance to complement killing.Inhibition of Neisseria gonorrhoeae epithelial cell interactions by vaginal Lactobacillus species.Innate recognition by neutrophil granulocytes differs between Neisseria gonorrhoeae strains causing local or disseminating infections.Structure-function studies of the Neisseria gonorrhoeae major outer membrane porinSaturating mutagenesis of an essential gene: a majority of the Neisseria gonorrhoeae major outer membrane porin (PorB) is mutable.The biology of Neisseria adhesins.Both MisR (CpxR) and MisS (CpxA) Are Required for Neisseria gonorrhoeae Infection in a Murine Model of Lower Genital Tract Infection.Neisseria gonorrhoeae porin P1.B induces endosome exocytosis and a redistribution of Lamp1 to the plasma membrane.Typing and surface charges of the variable loop regions of PorB from Neisseria meningitidis.Low-phosphate-dependent invasion resembles a general way for Neisseria gonorrhoeae to enter host cells.CEACAM is not necessary for Neisseria gonorrhoeae to adhere to and invade female genital epithelial cells.The pilus-induced Ca2+ flux triggers lysosome exocytosis and increases the amount of Lamp1 accessible to Neisseria IgA1 protease.Cholera toxin and extracellular Ca2+ induce adherence of non-piliated Neisseria: evidence for an important role of G-proteins and Rho in the bacteria-cell interaction.Fibronectin-binding protein acts as Staphylococcus aureus invasin via fibronectin bridging to integrin alpha5beta1.Neisserial porin (PorB) causes rapid calcium influx in target cells and induces apoptosis by the activation of cysteine proteasesMutagenesis of the Neisseria gonorrhoeae porin reduces invasion in epithelial cells and enhances phagocyte responsiveness.Neisserial PorB is translocated to the mitochondria of HeLa cells infected with Neisseria meningitidis and protects cells from apoptosis.
P2860
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P2860
Gonococcal invasion of epithelial cells driven by P.IA, a bacterial ion channel with GTP binding properties.
description
1998 nî lūn-bûn
@nan
1998年の論文
@ja
1998年学术文章
@wuu
1998年学术文章
@zh-cn
1998年学术文章
@zh-hans
1998年学术文章
@zh-my
1998年学术文章
@zh-sg
1998年學術文章
@yue
1998年學術文章
@zh
1998年學術文章
@zh-hant
name
Gonococcal invasion of epithel ...... l with GTP binding properties.
@ast
Gonococcal invasion of epithel ...... l with GTP binding properties.
@en
type
label
Gonococcal invasion of epithel ...... l with GTP binding properties.
@ast
Gonococcal invasion of epithel ...... l with GTP binding properties.
@en
prefLabel
Gonococcal invasion of epithel ...... l with GTP binding properties.
@ast
Gonococcal invasion of epithel ...... l with GTP binding properties.
@en
P2860
P356
P1476
Gonococcal invasion of epithel ...... el with GTP binding properties
@en
P2093
T D Duensing
P2860
P304
P356
10.1084/JEM.188.5.941
P407
P577
1998-09-01T00:00:00Z