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Institut für Medizinische Mikrobiologie und Hygiene Elfriede-Aulhorn-Str. 6 72076 Tübingen Germany
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Institut für Medizinische Mikrobiologie und Hygiene Universitätsklinikum Tübingen Elfriede-Aulhorn-Str. 6 72076 Tübingen Germany
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Interfakultäres Institut für Mikrobiologie und Infektionsmedizin Tübingen (IMIT) Institut für Medizinische Mikrobiologie und Hygiene Universität Tübingen Tübingen Germany
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University of Tübingen, Interfaculty Institute of Microbiology and Infection Medicine (IMIT), Section of Cellular and Molecular Microbiology, Elfriede-Aulhorn-Str. 6, 72076 Tübingen, Germany
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xref:PubMed:17026754
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pathogen
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pathogen:bacterium
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Stress-Responsive Periplasmic Chaperones in Bacteria.
Not available
S-EPMC8144458
|
biostudies-literature
Cite
Mechanism of ATPase-mediated Cu+ export and delivery to periplasmic chaperones: the interaction of Escherichia coli CopA and CusF.
Not available
S-EPMC4110264
|
biostudies-literature
Cite
An Unprecedented Tolerance to Deletion of the Periplasmic Chaperones SurA, Skp, and DegP in the Nosocomial Pathogen Acinetobacter baumannii.
Not available
S-EPMC9578438
|
biostudies-literature
Cite
Effects of Periplasmic Chaperones and Membrane Thickness on BamA-Catalyzed Outer-Membrane Protein Folding.
Not available
S-EPMC5692476
|
biostudies-literature
Cite
Role of periplasmic chaperones and BamA (YaeT/Omp85) in folding and secretion of intimin from enteropathogenic Escherichia coli strains.
Not available
S-EPMC2725589
|
biostudies-literature
Cite
Dissecting the effects of periplasmic chaperones on the in vitro folding of the outer membrane protein PagP.
Not available
S-EPMC3906610
|
biostudies-literature
Cite
PpiD is a player in the network of periplasmic chaperones in Escherichia coli.
Not available
S-EPMC2956729
|
biostudies-literature
Cite
Roles of periplasmic chaperone proteins in the biogenesis of serine protease autotransporters of Enterobacteriaceae.
Not available
S-EPMC2795308
|
biostudies-literature
Cite
From Chaperones to the Membrane with a BAM!
Not available
S-EPMC5420074
|
biostudies-literature
Cite
Chaperones Skp and SurA dynamically expand unfolded OmpX and synergistically disassemble oligomeric aggregates.
Not available
S-EPMC8892499
|
biostudies-literature
Cite
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