Results 91 to 100 of about 5,195,858 (198)

Plasmid-Encoded Outer Membrane Protein YadA Mediates Specific Binding of Enteropathogenic Yersiniae to Various Types of Collagen [PDF]

open access: yes, 1992
The plasmid-encoded outer membrane protein YadA of enteropathogenic yersiniae is associated with pathogenicity. Recently, collagen binding of YadA-positive yersiniae was reported without detailed characterization (L. Emödy, J. Heesemann, H. Wolf-Watz, M.
Emmerich, F.   +4 more
core   +1 more source

Exploring bacterial outer membrane barrier to combat bad bugs

open access: yesInfection and Drug Resistance, 2017
Ishan Ghai,1 Shashank Ghai2 1School of Engineering and Life Sciences, Jacobs University, Bremen, 2Leibniz University, Hannover, Germany Abstract: One of the main fundamental mechanisms of antibiotic resistance in Gram-negative bacteria comprises an ...
Ghai I, Ghai S
doaj  

Lifting the lid on pilus assembly

open access: yeseLife, 2014
A combination of computer simulations, evolutionary analysis and graph theory has provided new insights into the assembly of pili on the surface of bacteria.
Han Remaut, Nir Ben-Tal
doaj   +1 more source

Single-channel measurements of an N-acetylneuraminic acid-inducible outer membrane channel in Escherichia coli [PDF]

open access: yes, 2012
NanC is an Escherichia coli outer membrane protein involved in sialic acid (Neu5Ac, i.e., N-acetylneuraminic acid) uptake. Expression of the NanC gene is induced and controlled by Neu5Ac. The transport mechanism of Neu5Ac is not known.
Peneff, Caroline M.   +4 more
core   +1 more source

Allosteric signalling in the outer membrane translocation domain of PapC usher

open access: yeseLife, 2014
PapC ushers are outer-membrane proteins enabling assembly and secretion of P pili in uropathogenic E. coli. Their translocation domain is a large β-barrel occluded by a plug domain, which is displaced to allow the translocation of pilus subunits across ...
Irene Farabella   +8 more
doaj   +1 more source

Bacterial Outer Membranes and Interactions with Membrane Proteins [PDF]

open access: yesBiophysical Journal, 2015
Because the bacteria's outer membrane (OM) acts as an effective barrier against the permeation of both hydrophobic and hydrophilic compounds, gram-negative cell permeation is one of the biggest challenges to the discovery of novel antibiotics for bacterial infections and antibiotic resistance worldwide.
openaire   +1 more source

Soluble versions of outer membrane cytochromes function as exporters for heterologously produced cargo proteins

open access: yesMicrobial Cell Factories, 2019
This study reveals that it is possible to secrete truncated versions of outer membrane cytochromes into the culture supernatant and that these proteins can provide a basis for the export of heterologously produced proteins.
Helge M. Dietrich   +5 more
doaj   +1 more source

Pseudomonas aeruginosa outer membrane proteins: Profile analysis and immunogenicity in relation to the antibiotic resistance

open access: yesJournal of Veterinary Medical Research, 2005
To analyze the major outer membrane proteins (OMPs) of the sensitive or resistant Pseudomonas aeruginosa strains, the OMPs were separated from the cellular elements by sarcosyl extraction method.
Mona I. El-Enbaawy, Ansam M. Salam
doaj  

Commensal bacterial outer membrane protein A induces interleukin-22 production

open access: yesCell Reports
Summary: Interleukin (IL)-22 promotes host-microbiota homeostasis. We sought to identify microbiota metabolite(s) that drive intestinal IL-22 production.
Yanling Wang   +3 more
doaj   +1 more source

Isolation and characterisation of the intermembrane space components of the mitochondrial TIM22 protein import machinery of Neurospora crassa [PDF]

open access: yes, 2004
Mitochondria are essential cellular organelles of eukaryotic organisms, which import most of their proteinaceous constituents from the cytoplasm. Two mitochondrial membranes contain different translocation machineries which are involved in the import and
Vasiljev, Andreja
core  

Home - About - Disclaimer - Privacy