Structure and function of the PorB porin from disseminating Neisseria gonorrhoeae (Q27683044)

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Oliver Kepp

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Martin Fraunholz

object named as

Martin Fraunholz

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Vera Kozjak-Pavlovic

object named as

Vera Kozjak-Pavlovic

2

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Thomas Rudel

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object named as

Thomas Rudel

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author name string

Michaela Faulstich

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Robert Hurwitz

Structure of the head of the Bartonella adhesin BadA

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language of work or name

English

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publication date

1 February 2013

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published in

Biochemical Journal

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volume

449

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issue

3

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page(s)

631-42

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cites work

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Structure of the OmpA-like domain of RmpM from Neisseria meningitidis

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Structural basis for solute transport, nucleotide regulation, and immunological recognition of Neisseria meningitidis PorB

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An arginine ladder in OprP mediates phosphate-specific transfer across the outer membrane

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Bim and Bmf synergize to induce apoptosis in Neisseria gonorrhoeae infection

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Transmembrane passage of hydrophobic compounds through a protein channel wall

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Low-phosphate-dependent invasion resembles a general way for Neisseria gonorrhoeae to enter host cells.

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Targeting of the pro-apoptotic VDAC-like porin (PorB) of Neisseria gonorrhoeae to mitochondria of infected cells

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VDAC and the bacterial porin PorB of Neisseria gonorrhoeae share mitochondrial import pathways

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Bacterial porin disrupts mitochondrial membrane potential and sensitizes host cells to apoptosis

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Neisserial PorB is translocated to the mitochondria of HeLa cells infected with Neisseria meningitidis and protects cells from apoptosis.

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Meningococcal porin PorB prevents cellular apoptosis in a toll-like receptor 2- and NF-kappaB-independent manner

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Nonlinear and asymmetric open channel characteristics of an ion-selective porin in planar membranes

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Mutagenesis of the Neisseria gonorrhoeae porin reduces invasion in epithelial cells and enhances phagocyte responsiveness.

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Successful recovery of the normal electrophysiological properties of PorB (class 3) porin from Neisseria meningitidis after expression in Escherichia coli and renaturation.

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Molecular Architecture and Electrostatic Properties of a Bacterial Porin

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Host glycoprotein Gp96 and scavenger receptor SREC interact with PorB of disseminating Neisseria gonorrhoeae in an epithelial invasion pathway

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Serovars and serum resistance of Neisseria gonorrhoeae from disseminated and uncomplicated infections.

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Naturally occurring isolates of Neisseria gonorrhoeae, which display anomalous serovar properties, express PIA/PIB hybrid porins, deletions in PIB or novel PIA molecules

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S-layer protein from Thermus thermophilus HB8 assembles into porin-like structures

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Identifiers

DOI

10.1042/BJ20121025

1 reference

Consolidated OpenCitations Corpus – April 2017

1 reference

Consolidated OpenCitations Corpus – April 2017

PubMed publication ID

23095086

1 reference

Consolidated OpenCitations Corpus – April 2017