about
SecA, a remarkable nanomachineThe Sec-dependent pathwayMaking a beta-barrel: assembly of outer membrane proteins in Gram-negative bacteria.TP0326, a Treponema pallidum β-barrel assembly machinery A (BamA) orthologue and rare outer membrane proteinThe complete genome sequence of 'Candidatus Liberibacter solanacearum', the bacterium associated with potato zebra chip disease.Th17-stimulating protein vaccines confer protection against Pseudomonas aeruginosa pneumoniaStructural characterization of the complex of SecB and metallothionein-labeled proOmpA by cryo-electron microscopy.Multitasking SecB chaperones in bacteriaAsp2 and Asp3 interact directly with GspB, the export substrate of the Streptococcus gordonii accessory Sec SystemLarge-scale evolutionary analyses on SecB subunits of bacterial sec system.Revisiting the interaction between the chaperone Skp and lipopolysaccharideIn Vitro Interaction of the Housekeeping SecA1 with the Accessory SecA2 Protein of Mycobacterium tuberculosis.Functional implementation of the posttranslational SecB-SecA protein-targeting pathway in Bacillus subtilis.Emerging themes in SecA2-mediated protein export.TAC from Mycobacterium tuberculosis: a paradigm for stress-responsive toxin-antitoxin systems controlled by SecB-like chaperones.Evolutionary evidence on suitability of SecD as a target for development of antibacterial agents against Staphylococcus aureusMosaic origin of the mitochondrial proteome.Coupling between codon usage, translation and protein export in Escherichia coli.Breaking on through to the other side: protein export through the bacterial Sec system.Breaking the bacterial protein targeting and translocation model: oral organisms as a case in point.Yeast Mitochondria as a Model System to Study the Biogenesis of Bacterial β-Barrel Proteins.Promiscuous binding by Hsp70 results in conformational heterogeneity and fuzzy chaperone-substrate ensembles.Structure and conservation of the periplasmic targeting factor Tic22 protein from plants and cyanobacteria.Novel translocation intermediate allows re-evaluation of roles of ATP, proton motive force and SecG at the late stage of preprotein translocation.Signal peptides for recombinant protein secretion in bacterial expression systems.Conformation and dynamics of the periplasmic membrane-protein-chaperone complexes OmpX-Skp and tOmpA-Skp.
P2860
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P2860
description
article científic
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article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on 19 October 2009
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
SecB--a chaperone dedicated to protein translocation.
@en
SecB--a chaperone dedicated to protein translocation.
@nl
type
label
SecB--a chaperone dedicated to protein translocation.
@en
SecB--a chaperone dedicated to protein translocation.
@nl
prefLabel
SecB--a chaperone dedicated to protein translocation.
@en
SecB--a chaperone dedicated to protein translocation.
@nl
P2093
P2860
P356
P1433
P1476
SecB--a chaperone dedicated to protein translocation
@en
P2093
Nico Nouwen
Philipp Bechtluft
Sander J Tans
P2860
P304
P356
10.1039/B915435C
P577
2009-10-19T00:00:00Z