Results 291 to 300 of about 358,692 (311)

Bacterial ß-Barrel Outer Membrane Proteins

2009
ß-barrel outer membrane proteins constitute the second and less well-studied class of transmembrane proteins. They are present exclusively in the outer membrane of Gram-negative bacteria and presumably in the outer membrane of mitochondria and chloroplasts.
Pantelis G. Bagos, Stavros J. Hamodrakas
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Bacterial outer membrane vesicles as a platform for biomedical applications: An update.

Journal of Controlled Release, 2020
Outer membrane vesicles (OMVs) are produced by Gram-negative bacteria both in vitro and in vivo. OMVs are nano-sized spherical vehicles formed by lipid bilayer membranes and contain multiple parent bacteria-derived components.
Min Li, Han Zhou, Chen Yang, Yi Wu, Xuechang Zhou, Hang Liu, Yucai Wang   +6 more
semanticscholar   +1 more source

Multiple pathways allow protein secretion across the bacterial outer membrane

Current Opinion in Cell Biology, 2000
Secretion of proteins across the bacterial outer membrane takes place via a variety of mechanisms from simple one-component systems to complex multicomponent pathways. Secretion pathways can be organized into evolutionarily and functionally related groups, which highlight their relationship with organelle biogenesis.
D G, Thanassi, S J, Hultgren
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Bacterial outer membrane protein analysis by electrophoresis and microchip technology

Expert Review of Proteomics, 2007
Outer membrane proteins are indispensable components of bacterial cells and participate in several relevant functions of the microorganisms. Changes in the outer membrane protein composition might alter antibiotic sensitivity and pathogenicity. Furthermore, the effects of various factors on outer membrane protein expression, such as antibiotic ...
Ildikó, Kustos, Béla, Kocsis, Ferenc, Kilár   +2 more
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Biogenesis of β-barrel integral proteins of bacterial outer membrane

Biochemistry (Moscow), 2012
Gram-negative bacteria are enveloped by two membranes, the inner (cytoplasmic) (CM) and the outer (OM). The majority of integral outer membrane proteins are arranged in β-barrels of cylindrical shape composed of amphipathic antiparallel β-strands. In bacteria, β-barrel proteins function as water-filled pores, active transporters, enzymes, receptors ...
T F, Solov'eva, O D, Novikova, O Yu, Portnyagina   +2 more
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In vitro synthesized bacterial outer membrane protein is integrated into bacterial inner membranes but translocated across microsomal membranes

Nature, 1986
The LamB protein is an integral membrane protein of the outer membrane of Escherichia coli. We have now found that, when synthesized in an E. coli cell-free translation system supplemented with inverted vesicles derived from the E. coli inner membrane, LamB protein is integrated into the vesicle membrane as assayed by its resistance to extraction at ...
M, Watanabe, J F, Hunt, G, Blobel
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Omp85, an evolutionarily conserved bacterial protein involved in outer-membrane-protein assembly

Research in Microbiology, 2004
The insertion of proteins into membranes generally requires the assistance of membrane proteins. A protein, designated Omp85 in Neisseria meningitidis, was shown to be required for the assembly of bacterial outer-membrane proteins. The protein is essential for the viability of the bacteria and is ubiquitous among Gram-negative bacteria. Omp85 depletion
Voulhoux, J.R., Tommassen, J.P.M.
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Not all Bacterial Outer Membrane Proteins are β-Barrels

2023
AbstractThe discovery of WzA, an octomeric helical barrel integral bacterial outer membrane protein, has challenged the widely held understanding that all integral outer membrane proteins of gram-negative bacteria are closed β-barrels composed of transmembrane β-strands.
John Heido, Simon Keng, Pream Kadevari, Hulya Poyrazoglu, Ekta Priyam, Sajith Jayasinghe   +5 more
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Role of a Highly Conserved Bacterial Protein in Outer Membrane Protein Assembly

Science, 2003
After transport across the cytoplasmic membrane, bacterial outer membrane proteins are assembled into the outer membrane. Meningococcal Omp85 is a highly conserved protein in Gram-negative bacteria, and its homolog Toc75 is a component of the chloroplast protein-import machinery.
Voulhoux, J.R., Bos, M.P., Geurtsen, J.J.G., Mols, M., Tommassen, J.P.M.   +4 more
openaire   +3 more sources

Protein oligomerization in the bacterial outer membrane

2009
The formation of homo-oligomeric assemblies is a well-established characteristic of many soluble proteins and enzymes. Oligomerization has been shown to increase protein stability, allow allosteric cooperativity, shape reaction compartments and provide multivalent interaction sites in soluble proteins. In comparison, our understanding of the prevalence
Guoyu, Meng, Chandran, Vidya, Remaut, Han Karel, Waksman, G.   +3 more
openaire   +1 more source