Modulation of Neisseria porin (PorB) by cytosolic ATP/GTP of target cells: parallels between pathogen accommodation and mitochondrial endosymbiosis.
about
From evolution to pathogenesis: the link between β-barrel assembly machineries in the outer membrane of mitochondria and gram-negative bacteriaA novel approach for purification and selective capture of membrane vesicles of the periodontopathic bacterium, Porphyromonas gingivalis: membrane vesicles bind to magnetic beads coated with epoxy groups in a noncovalent, species-specific mannerStructural basis for solute transport, nucleotide regulation, and immunological recognition of Neisseria meningitidis PorBStructure and function of the PorB porin from disseminating Neisseria gonorrhoeaeIdentification of a cation transport pathway in Neisseria meningitidis PorBRv1698 of Mycobacterium tuberculosis represents a new class of channel-forming outer membrane proteinsMolecular basis for the differential interaction of plant mitochondrial VDAC proteins with tRNAs.Bacterial porin disrupts mitochondrial membrane potential and sensitizes host cells to apoptosis.VDAC and the bacterial porin PorB of Neisseria gonorrhoeae share mitochondrial import pathways.Structural and evolutionary inference from molecular variation in Neisseria porinsVoltage gating is a fundamental feature of porin and toxin beta-barrel membrane channels.Gonorrhea - an evolving disease of the new millennium.The evolutionary history of mitochondrial porins.Nucleotide-binding sites in the voltage-dependent anion channel: characterization and localization.por Variable-region typing by DNA probe hybridization is broadly applicable to epidemiologic studies of Neisseria gonorrhoeae.Update on meningococcal disease with emphasis on pathogenesis and clinical managementVariation in the Neisseria lactamica porin, and its relationship to meningococcal PorBStaphylococcus aureus Panton-Valentine leukocidin directly targets mitochondria and induces Bax-independent apoptosis of human neutrophils.Ion channels in the outer membranes of chloroplasts and mitochondria: open doors or regulated gates?Elimination of channel-forming activity by insertional inactivation of the p13 gene in Borrelia burgdorferiNeisseria meningitidis porin PorB interacts with mitochondria and protects cells from apoptosisPyrophosphate-mediated iron acquisition from transferrin in Neisseria meningitidis does not require TonB activity.Calcium, ATP and nuclear pore channel gatingThe Oms66 (p66) protein is a Borrelia burgdorferi porin.Outer mitochondrial membrane permeability can regulate coupled respiration and cell survival.Outer membrane proteins of pathogenic spirochetes.The molecular mechanisms used by Neisseria gonorrhoeae to initiate infection differ between men and women.Gonococcal invasion of epithelial cells driven by P.IA, a bacterial ion channel with GTP binding properties.Structure-function studies of the Neisseria gonorrhoeae major outer membrane porinExpression, purification and preliminary X-ray analysis of the Neisseria meningitidis outer membrane protein PorB.Saturating mutagenesis of an essential gene: a majority of the Neisseria gonorrhoeae major outer membrane porin (PorB) is mutable.Characterization and intracellular trafficking pattern of vacuoles containing Chlamydia pneumoniae in human epithelial cells.Emerging roles of pathogens in Alzheimer disease.The first suicides: a legacy inherited by parasitic protozoans from prokaryote ancestors.Neisseria gonorrhoeae porin P1.B induces endosome exocytosis and a redistribution of Lamp1 to the plasma membrane.Gonococcal porin IB activates NF-kappaB in human urethral epithelium and increases the expression of host antiapoptotic factors.Targeting of the pro-apoptotic VDAC-like porin (PorB) of Neisseria gonorrhoeae to mitochondria of infected cellsNeisseria meningitidis Lacking the Major Porins PorA and PorB Is Viable and Modulates Apoptosis and the Oxidative Burst of Neutrophils.Neisserial porin (PorB) causes rapid calcium influx in target cells and induces apoptosis by the activation of cysteine proteasesPurification, characterization and sequence analysis of Omp50,a new porin isolated from Campylobacter jejuni.
P2860
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P2860
Modulation of Neisseria porin (PorB) by cytosolic ATP/GTP of target cells: parallels between pathogen accommodation and mitochondrial endosymbiosis.
description
1996 nî lūn-bûn
@nan
1996年の論文
@ja
1996年学术文章
@wuu
1996年学术文章
@zh
1996年学术文章
@zh-cn
1996年学术文章
@zh-hans
1996年学术文章
@zh-my
1996年学术文章
@zh-sg
1996年學術文章
@yue
1996年學術文章
@zh-hant
name
Modulation of Neisseria porin ...... d mitochondrial endosymbiosis.
@en
Modulation of Neisseria porin
@nl
type
label
Modulation of Neisseria porin ...... d mitochondrial endosymbiosis.
@en
Modulation of Neisseria porin
@nl
prefLabel
Modulation of Neisseria porin ...... d mitochondrial endosymbiosis.
@en
Modulation of Neisseria porin
@nl
P2093
P1433
P1476
Modulation of Neisseria porin ...... d mitochondrial endosymbiosis.
@en
P2093
P304
P356
10.1016/S0092-8674(00)81117-4
P407
P50
P577
1996-05-01T00:00:00Z