Apparent molecular weights of a heat-modifiable protein from the outer membrane of Escherichia coli in gels with different acrylamide concentrations.
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A growing toolbox of techniques for studying β-barrel outer membrane protein folding and biogenesisStructural investigations of the active-site mutant Asn156Ala of outer membrane phospholipase A: Function of the Asn-His interaction in the catalytic triadThe β-barrel assembly machinery in motion.Dissecting the effects of periplasmic chaperones on the in vitro folding of the outer membrane protein PagPSurface topology of the Escherichia coli K-12 ferric enterobactin receptorResolution of basic gonococcal outer membrane proteins by nonequilibrium pH gradient electrophoresis.Molecular cloning of the Pasteurella haemolytica pomA gene and identification of bovine antibodies against PomA surface domains.Characterization of an OmpA-like outer membrane protein of the acidophilic iron-oxidizing bacterium, Acidithiobacillus ferrooxidansStructure and electrophysiological properties of the YscC secretin from the type III secretion system of Yersinia enterocolitica.Structural and functional analyses of the major outer membrane protein of Chlamydia trachomatis.Identification of Francisella tularensis outer membrane protein A (FopA) as a protective antigen for tularemia.Primary structure of major outer membrane protein II (ompA protein) of Escherichia coli K-12.Heat Modifiability of Outer Membrane Proteins from Gram-Negative BacteriaMechanistic studies of the biogenesis and folding of outer membrane proteins in vitro and in vivo: what have we learned to date?Skp is a multivalent chaperone of outer-membrane proteinsMolecular characterization of pldA, the structural gene for a phospholipase A from Campylobacter coli, and its contribution to cell-associated hemolysis.Demonstration of a folded monomeric form of porin PhoE of Escherichia coli in vivo.Topology of the outer membrane phospholipase A of Salmonella typhimurium.Outer membrane of Serratia marcescens: apparent molecular weights of heat-modifiable proteins in gels with different acrylamide concentrations.Proteolytic processing is not essential for multiple functions of the Escherichia coli autotransporter adhesin involved in diffuse adherence (AIDA-I).An alternative topological model for Escherichia coli OmpA.
P2860
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P2860
Apparent molecular weights of a heat-modifiable protein from the outer membrane of Escherichia coli in gels with different acrylamide concentrations.
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name
Apparent molecular weights of ...... ent acrylamide concentrations.
@en
Apparent molecular weights of ...... ent acrylamide concentrations.
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type
label
Apparent molecular weights of ...... ent acrylamide concentrations.
@en
Apparent molecular weights of ...... ent acrylamide concentrations.
@nl
prefLabel
Apparent molecular weights of ...... ent acrylamide concentrations.
@en
Apparent molecular weights of ...... ent acrylamide concentrations.
@nl
P2860
P1476
Apparent molecular weights of ...... ent acrylamide concentrations.
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P2093
P2860
P304
P577
1978-06-01T00:00:00Z