Small heat shock proteins, ClpB and the DnaK system form a functional triade in reversing protein aggregation
- Location
-
Deutsche Nationalbibliothek Frankfurt am Main
- Extent
-
Online-Ressource
- Language
-
Englisch
- Bibliographic citation
-
In: Molecular Microbiology ; 50 (2003), 2. - S. 585-595. - eISSN 1365-2958
- Classification
-
Biowissenschaften, Biologie
- Event
-
Veröffentlichung
- (where)
-
Konstanz
- (who)
-
Bibliothek der Universität Konstanz
- (when)
-
2007
- Creator
- URN
-
urn:nbn:de:bsz:352-opus-37190
- Rights
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
14.08.2025, 10:52 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
- Mogk, Axel
- Deuerling, Elke
- Vorderwülbecke, Sonja
- Vierling, Elizabeth
- Bukau, Bernd
- Bibliothek der Universität Konstanz
Time of origin
- 2007
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Ca2+-mediated [Ca-mediated] reconstitution of maltose transport and osmoregulation of maltose gene expression in Escherichia coli
Embedding misfolded protein sequestration in protein quality control networks
ClpS is an essential component of the N-end rule pathway in Escherichia coli
Chaperone-assisted folding of newly synthesized proteins in the cytosol
L23 protein functions as a chaperone docking site on the ribosome
Trigger factor and DnaK cooperate in folding of newly synthesized proteins
Impact of translation speed on co-translational protein folding and ribosome associated factor recruitment
Protecting protein homeostasis in neurodegenerative disease models by modulating the HSP70/co-chaperone network
Trigger factor in complex with the ribosome forms a molecular cradle for nascent proteins
Analysis of the role of N-terminal acetylation of newly synthesized proteins in Saccharomyces cerevisiae
Recognition and Targeting of Prion Aggregates to the Insoluble Protein Deposit (IPOD) in Saccharomyces cerevisiae
Profiling interactions of proximal nascent chains reveals a general co-translational mechanism of protein complex assembly
Ca2+-mediated [Ca-mediated] reconstitution of maltose transport and osmoregulation of maltose gene expression in Escherichia coli
Embedding misfolded protein sequestration in protein quality control networks
ClpS is an essential component of the N-end rule pathway in Escherichia coli
Chaperone-assisted folding of newly synthesized proteins in the cytosol
L23 protein functions as a chaperone docking site on the ribosome
Trigger factor and DnaK cooperate in folding of newly synthesized proteins
Impact of translation speed on co-translational protein folding and ribosome associated factor recruitment
Protecting protein homeostasis in neurodegenerative disease models by modulating the HSP70/co-chaperone network
Trigger factor in complex with the ribosome forms a molecular cradle for nascent proteins
Analysis of the role of N-terminal acetylation of newly synthesized proteins in Saccharomyces cerevisiae
Recognition and Targeting of Prion Aggregates to the Insoluble Protein Deposit (IPOD) in Saccharomyces cerevisiae
Profiling interactions of proximal nascent chains reveals a general co-translational mechanism of protein complex assembly
Ca2+-mediated [Ca-mediated] reconstitution of maltose transport and osmoregulation of maltose gene expression in Escherichia coli
Embedding misfolded protein sequestration in protein quality control networks
ClpS is an essential component of the N-end rule pathway in Escherichia coli
Chaperone-assisted folding of newly synthesized proteins in the cytosol
L23 protein functions as a chaperone docking site on the ribosome
Trigger factor and DnaK cooperate in folding of newly synthesized proteins
Impact of translation speed on co-translational protein folding and ribosome associated factor recruitment
Protecting protein homeostasis in neurodegenerative disease models by modulating the HSP70/co-chaperone network
Trigger factor in complex with the ribosome forms a molecular cradle for nascent proteins
Analysis of the role of N-terminal acetylation of newly synthesized proteins in Saccharomyces cerevisiae
Recognition and Targeting of Prion Aggregates to the Insoluble Protein Deposit (IPOD) in Saccharomyces cerevisiae