Breaking on through to the other side: protein export through the bacterial Sec system.
about
How Listeria monocytogenes organizes its surface for virulenceAntibody-mediated immunity induced by engineered Escherichia coli OMVs carrying heterologous antigens in their lumen.Proteome-wide subcellular topologies of E. coli polypeptides database (STEPdb).Multitasking SecB chaperones in bacteriaImaging and quantification of trans-membrane protein diffusion in living bacteria.Large-scale evolutionary analyses on SecB subunits of bacterial sec system.Function and evolution of two forms of SecDF homologs in Streptomyces coelicolor.Bacillus anthracis SlaQ Promotes S-Layer Protein Assembly.DegP Chaperone Suppresses Toxic Inner Membrane Translocation Intermediates.Evolutionary evidence on suitability of SecD as a target for development of antibacterial agents against Staphylococcus aureusThe Escherichia coli peripheral inner membrane proteome.Secretion of atypical protein substrates by the ESAT-6 secretion system of Staphylococcus aureusSelective transport by SecA2: an expanding family of customized motor proteins.Identification of a Large Family of Slam-Dependent Surface Lipoproteins in Gram-Negative Bacteria.MatureP: prediction of secreted proteins with exclusive information from their mature regions.Protein folding in the cell envelope of Escherichia coli.Neisserial surface lipoproteins: structure, function and biogenesis.Type IX secretion: the generation of bacterial cell surface coatings involved in virulence, gliding motility and the degradation of complex biopolymers.Folding while bound to chaperones.Rapid label-free quantitative analysis of the E. coli BL21(DE3) inner membrane proteome.The TatC component of the twin-arginine protein translocase functions as an obligate oligomer.Crystallization and preliminary X-ray crystallographic analysis of the curli transporter CsgGChaperone addiction of toxin-antitoxin systems.Preprotein mature domains contain translocase targeting signals that are essential for secretion.Xyn11E from Paenibacillus barcinonensis BP-23: a LppX-chaperone-dependent xylanase with potential for upgrading paper pulps.Site-saturation mutagenesis of mutant L-asparaginase II signal peptide hydrophobic region for improved excretion of cyclodextrin glucanotransferase.Protein Secretion in Gram-Positive Bacteria: From Multiple Pathways to Biotechnology.Sec pathway influences the growth of Deinococcus radiodurans.Recombinant protein expression in Lactococcus lactis using the P170 expression system.The way is the goal: how SecA transports proteins across the cytoplasmic membrane in bacteria.Thermostable and promiscuous Precambrian proteinsBacterial secretion chaperones: the mycobacterial type VII case
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Breaking on through to the other side: protein export through the bacterial Sec system.
description
article científic
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article scientifique
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articol științific
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articolo scientifico
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artigo científico
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artigo científico
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artigo científico
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artikel ilmiah
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artikull shkencor
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artículo científico
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name
Breaking on through to the other side: protein export through the bacterial Sec system.
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type
label
Breaking on through to the other side: protein export through the bacterial Sec system.
@en
prefLabel
Breaking on through to the other side: protein export through the bacterial Sec system.
@en
P2860
P50
P356
P1433
P1476
Breaking on through to the other side: protein export through the bacterial Sec system
@en
P2093
Spyridoula Karamanou
P2860
P356
10.1042/BJ20121227
P407
P577
2013-01-01T00:00:00Z