Molecular mechanism of the Escherichia coli AhpC in the function of a chaperone under heat-shock conditions
- Location
-
Deutsche Nationalbibliothek Frankfurt am Main
- ISSN
-
2045-2322
- Extent
-
Online-Ressource
- Language
-
Englisch
- Notes
-
online resource.
- Bibliographic citation
-
Molecular mechanism of the Escherichia coli AhpC in the function of a chaperone under heat-shock conditions ; volume:8 ; number:1 ; day:20 ; month:9 ; year:2018 ; pages:1-10 ; date:12.2018
Scientific reports ; 8, Heft 1 (20.9.2018), 1-10, 12.2018
- Classification
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Biowissenschaften, Biologie
- Creator
-
Kamariah, Neelagandan
- Contributor
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Eisenhaber, Birgit
Eisenhaber, Frank
Grüber, Gerhard
SpringerLink (Online service)
- DOI
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10.1038/s41598-018-32527-7
- URN
-
urn:nbn:de:101:1-2018103003084513118160
- Rights
-
Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
- 14.08.2025, 11:00 AM CEST
Data provider
This object is provided by:
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Kamariah, Neelagandan
- Eisenhaber, Birgit
- Eisenhaber, Frank
- Grüber, Gerhard
- SpringerLink (Online service)
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AHP based evaluation of AHP software
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The C-terminal domain of Escherichia coli trigger factor represents the central module of its chaperone activity
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Conformational dynamics of the Hsp70 chaperone
Mechanism of the molecular chaperone Hsp90
Characterization of the Molecular Chaperone Get3
Distribution of chaperone-usher fimbriae and curli fimbriae among uropathogenic Escherichia coli
Chaperone mechanism of the small heat shock protein Hsp26
Intracellular chaperone network in Escherichia coli and population heterogeneity of chaperone expression
Investigation of the chaperone function of the small heat shock protein — AgsA
Co-chaperone interactions in the Hsp90 chaperone cycle
AHP based evaluation of AHP software
Data processing for the AHP/ANP
The C-terminal domain of Escherichia coli trigger factor represents the central module of its chaperone activity
Pilicides inhibit the FGL chaperone/usher assisted biogenesis of the Dr fimbrial polyadhesin from uropathogenic Escherichia coli
Conformational dynamics of the Hsp70 chaperone
Mechanism of the molecular chaperone Hsp90
Characterization of the Molecular Chaperone Get3
Distribution of chaperone-usher fimbriae and curli fimbriae among uropathogenic Escherichia coli
Chaperone mechanism of the small heat shock protein Hsp26
Intracellular chaperone network in Escherichia coli and population heterogeneity of chaperone expression
Investigation of the chaperone function of the small heat shock protein — AgsA
Co-chaperone interactions in the Hsp90 chaperone cycle
AHP based evaluation of AHP software
Data processing for the AHP/ANP
The C-terminal domain of Escherichia coli trigger factor represents the central module of its chaperone activity
Pilicides inhibit the FGL chaperone/usher assisted biogenesis of the Dr fimbrial polyadhesin from uropathogenic Escherichia coli
Conformational dynamics of the Hsp70 chaperone
Mechanism of the molecular chaperone Hsp90
Characterization of the Molecular Chaperone Get3