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Protein oligomerization in the bacterial outer membrane (Review)

Molecular Membrane Biology, 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, Remi Fronzes, Han Remaut
exaly   +3 more sources

Protein import and export across the bacterial outer membrane

Current Opinion in Structural Biology, 2021
The bacterial outer membrane forms an impermeable barrier to the environment, but a wide variety of substances must cross it without compromising the membrane. Perhaps, the most fascinating transport phenomenon is the import and export of very large protein toxins using relatively small β-barrel proteins residing in the outer membrane.
Jérémy, Guérin, Susan K, Buchanan
openaire   +2 more sources

Assembly of Bacterial Outer Membrane Proteins

2012
Various methods that are routinely used to study the subcellular localization of membrane proteins in wild-type Gram-negative bacteria fall short in genetic studies addressing the biogenesis of outer membrane proteins (OMPs). Here, we describe three biochemical methods that can be used in such studies to evaluate the proper assembly of OMPs into the ...
Grijpstra, J.   +2 more
openaire   +3 more sources

Modeling and simulation of bacterial outer membranes and interactions with membrane proteins

Current Opinion in Structural Biology, 2017
The outer membrane (OM) of Gram-negative bacteria is composed of phospholipids in the periplasmic leaflet and lipopolysaccharides (LPS) in the external leaflet, along with β-barrel OM proteins (OMPs) and lipidated periplasmic lipoproteins. As a defensive barrier to toxic compounds, an LPS molecule has high antigenic diversity and unique combination of ...
Dhilon S Patel, Yifei Qi, Wonpil Im
openaire   +2 more sources

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.   +4 more
openaire   +3 more sources

Structural Aspects of Bacterial Outer Membrane Protein Assembly

2015
The outer membrane of Gram-negative bacteria is predominantly populated by β-Barrel proteins and lipid anchored proteins that serve a variety of biological functions. The proper folding and assembly of these proteins is essential for bacterial viability and often plays a critical role in virulence and pathogenesis. The β-barrel assembly machinery (Bam)
Charles, Calmettes   +2 more
openaire   +2 more sources

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   +2 more
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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   +2 more
openaire   +2 more sources

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
openaire   +1 more source

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
openaire   +2 more sources

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