Hochschulschrift | Online-Publikation
Role of the MecA adaptor protein in regulation of the AAA+ chaperone ClpC of Bacillus subtilis
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- Extent
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Online-Ressource
- Language
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Englisch
- Notes
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Heidelberg, Univ., Diss., 2004
- Classification
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Biowissenschaften, Biologie
- Keyword
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Heubacillus
Polypeptidketten bindende Proteine
Proteasen ; Polypeptidketten bindende Proteine ; Heubacillus ; Biologischer Abbau ; Oligomerisation
- Creator
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Schlothauer, Tilman
- URN
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urn:nbn:de:bsz:16-opus-47716
- Rights
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Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
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25.03.2025, 1:57 PM CET
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.
Object type
- Hochschulschrift
- Online-Publikation
Associated
- Schlothauer, Tilman
Other Objects (12)
Role of the MecA adaptor protein in regulation of the AAA+ chaperone ClpC of Bacillus subtilis
Regulation of the AAA+ protein ClpC by adaptor proteins
Activation mechanism of the AAA+ chaperone ClpB, Hsp104
Xenogeneic modulation of the ClpCP protease of Bacillus subtilis by a phage-encoded adaptor-like protein
The role of ClpC and its adaptor proteins in protein quality control systems of Bacillus subtilis
Substrate recognition and processing by the AAA+ chaperone ClpB
The disaggregation activity of the ClpB-Hsp104 chaperone is regulated by ist unique M domain
The adaptor protein Sti1/Hop connects the Hsp70 and Hsp90 chaperone cycle
Mec
MEC
MEC
Mec
Role of the MecA adaptor protein in regulation of the AAA+ chaperone ClpC of Bacillus subtilis
Regulation of the AAA+ protein ClpC by adaptor proteins
Activation mechanism of the AAA+ chaperone ClpB, Hsp104
Xenogeneic modulation of the ClpCP protease of Bacillus subtilis by a phage-encoded adaptor-like protein
The role of ClpC and its adaptor proteins in protein quality control systems of Bacillus subtilis
Substrate recognition and processing by the AAA+ chaperone ClpB
The disaggregation activity of the ClpB-Hsp104 chaperone is regulated by ist unique M domain
The adaptor protein Sti1/Hop connects the Hsp70 and Hsp90 chaperone cycle
Mec
MEC
MEC
Mec
Role of the MecA adaptor protein in regulation of the AAA+ chaperone ClpC of Bacillus subtilis
Regulation of the AAA+ protein ClpC by adaptor proteins
Activation mechanism of the AAA+ chaperone ClpB, Hsp104
Xenogeneic modulation of the ClpCP protease of Bacillus subtilis by a phage-encoded adaptor-like protein
The role of ClpC and its adaptor proteins in protein quality control systems of Bacillus subtilis
Substrate recognition and processing by the AAA+ chaperone ClpB
The disaggregation activity of the ClpB-Hsp104 chaperone is regulated by ist unique M domain
The adaptor protein Sti1/Hop connects the Hsp70 and Hsp90 chaperone cycle
Mec
MEC
MEC