Hochschulschrift
Substrate recognition and processing by the AAA+ chaperone ClpB
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- Dimensions
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30 cm
- Extent
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70, [127] S.
- Language
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Englisch
- Notes
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Ill., graph. Darst.
Enth. außerdem 10 Sonderabdr. aus verschiedenen Zeitschr.
Heidelberg, Univ., Diss., 2004
- Classification
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Biowissenschaften, Biologie
- Keyword
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Escherichia coli
Polypeptidketten bindende Proteine
- Creator
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Schlieker, Christian
- Table of contents
- Rights
-
Bei diesem Objekt liegt nur das Inhaltsverzeichnis digital vor. Der Zugriff darauf ist unbeschränkt möglich.
- Last update
-
11.06.2025, 2:23 PM 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.
Object type
- Hochschulschrift
Associated
- Schlieker, Christian
Other Objects (12)
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Role of the MecA adaptor protein in regulation of the AAA+ chaperone ClpC of Bacillus subtilis
Role of the MecA adaptor protein in regulation of the AAA+ chaperone ClpC of Bacillus subtilis
Mass spectrometric analysis of chaperone-substrate interactions
Regulation of the AAA+ protein ClpC by adaptor proteins
The HSP100 protein ClpA : significance of the N-terminal domain in substrate recognition and binding and characterization of the novel substrate RepE
Characterization of different Hsp90-client and chaperone-substrate interactions
Studies on homotypic and heterotypic communications in chaperone protein ClpB from T. thermophilus
Allosteric regulation of the motor subunits of the AAA+ disaggregation machine ClpB
Untersuchungen zur Struktur und Substratspezifität des AAA+-Chaperons ClpB in Escherichia coli
Multistep mechanism of substrate binding determines chaperone activity of Hsp70
Activation mechanism of the AAA+ chaperone ClpB, Hsp104
Evolution der Substraterkennungsdomänen von AAA-Proteinen : = Evolution of substrate recognition domains of the AAA proteins
Role of the MecA adaptor protein in regulation of the AAA+ chaperone ClpC of Bacillus subtilis
Role of the MecA adaptor protein in regulation of the AAA+ chaperone ClpC of Bacillus subtilis
Mass spectrometric analysis of chaperone-substrate interactions
Regulation of the AAA+ protein ClpC by adaptor proteins
The HSP100 protein ClpA : significance of the N-terminal domain in substrate recognition and binding and characterization of the novel substrate RepE
Characterization of different Hsp90-client and chaperone-substrate interactions
Studies on homotypic and heterotypic communications in chaperone protein ClpB from T. thermophilus
Allosteric regulation of the motor subunits of the AAA+ disaggregation machine ClpB
Untersuchungen zur Struktur und Substratspezifität des AAA+-Chaperons ClpB in Escherichia coli
Multistep mechanism of substrate binding determines chaperone activity of Hsp70
Activation mechanism of the AAA+ chaperone ClpB, Hsp104
Evolution der Substraterkennungsdomänen von AAA-Proteinen : = Evolution of substrate recognition domains of the AAA proteins
Role of the MecA adaptor protein in regulation of the AAA+ chaperone ClpC of Bacillus subtilis
Role of the MecA adaptor protein in regulation of the AAA+ chaperone ClpC of Bacillus subtilis
Mass spectrometric analysis of chaperone-substrate interactions
Regulation of the AAA+ protein ClpC by adaptor proteins
The HSP100 protein ClpA : significance of the N-terminal domain in substrate recognition and binding and characterization of the novel substrate RepE
Characterization of different Hsp90-client and chaperone-substrate interactions
Studies on homotypic and heterotypic communications in chaperone protein ClpB from T. thermophilus
Allosteric regulation of the motor subunits of the AAA+ disaggregation machine ClpB
Untersuchungen zur Struktur und Substratspezifität des AAA+-Chaperons ClpB in Escherichia coli