VDAC and the bacterial porin PorB of Neisseria gonorrhoeae share mitochondrial import pathways.
about
From evolution to pathogenesis: the link between β-barrel assembly machineries in the outer membrane of mitochondria and gram-negative bacteriaAnaplasma phagocytophilum Ats-1 is imported into host cell mitochondria and interferes with apoptosis inductionStructural 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 PorBEvolutionary conservation in biogenesis of β-barrel proteins allows mitochondria to assemble a functional bacterial trimeric autotransporter protein.Chloroplast β-barrel proteins are assembled into the mitochondrial outer membrane in a process that depends on the TOM and TOB complexes.Targeting of Neisserial PorB to the mitochondrial outer membrane: an insight on the evolution of β-barrel protein assembly machines.Neisserial Omp85 protein is selectively recognized and assembled into functional complexes in the outer membrane of human mitochondria.Porins in prokaryotes and eukaryotes: common themes and variations.Bacterial porin disrupts mitochondrial membrane potential and sensitizes host cells to apoptosis.Biogenesis of beta-barrel membrane proteins in bacteria and eukaryotes: evolutionary conservation and divergence.Signals in bacterial beta-barrel proteins are functional in eukaryotic cells for targeting to and assembly in mitochondria.Gonorrhea - an evolving disease of the new millennium.A translocated bacterial protein protects vascular endothelial cells from apoptosis.A novel inhibitory mechanism of mitochondrion-dependent apoptosis by a herpesviral protein.Neisseria gonorrhoeae-mediated inhibition of apoptotic signalling in polymorphonuclear leukocytes.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.Hijacking mitochondria: bacterial toxins that modulate mitochondrial function.Targeting mitochondria: how intravacuolar bacterial pathogens manipulate mitochondria.Early stages in the biogenesis of eukaryotic β-barrel proteins.Listeriosis downregulates hepatic cytochrome P450 enzymes in sublethal murine infection.Clostridium difficile toxin B causes apoptosis in epithelial cells by thrilling mitochondria. Involvement of ATP-sensitive mitochondrial potassium channels.Neisseria meningitidis Lacking the Major Porins PorA and PorB Is Viable and Modulates Apoptosis and the Oxidative Burst of Neutrophils.Bak and Bax are non-redundant during infection- and DNA damage-induced apoptosis.Outer membrane vesicles from Neisseria gonorrhoeae target PorB to mitochondria and induce apoptosis.Role of Tom5 in Maintaining the Structural Stability of the TOM Complex of Mitochondria
P2860
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P2860
VDAC and the bacterial porin PorB of Neisseria gonorrhoeae share mitochondrial import pathways.
description
2002 nî lūn-bûn
@nan
2002 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
VDAC and the bacterial porin P ...... mitochondrial import pathways.
@ast
VDAC and the bacterial porin P ...... mitochondrial import pathways.
@en
type
label
VDAC and the bacterial porin P ...... mitochondrial import pathways.
@ast
VDAC and the bacterial porin P ...... mitochondrial import pathways.
@en
prefLabel
VDAC and the bacterial porin P ...... mitochondrial import pathways.
@ast
VDAC and the bacterial porin P ...... mitochondrial import pathways.
@en
P2093
P2860
P356
P1433
P1476
VDAC and the bacterial porin P ...... mitochondrial import pathways.
@en
P2093
Anne Müller
Joachim Rassow
Nikolaus Machuy
Thomas F Meyer
Thomas Rudel
P2860
P304
P356
10.1093/EMBOJ/21.8.1916
P407
P577
2002-04-01T00:00:00Z