Molecular guardians for newborn proteins : ribosome-associated chaperones and their role in protein folding
- Location
-
Deutsche Nationalbibliothek Frankfurt am Main
- Extent
-
Online-Ressource
- Language
-
Englisch
- Bibliographic citation
-
In: Cellular and Molecular Life Sciences ; 62 (2005), 23. - S. 2727-2738. - ISSN 1420-682X. - eISSN 1420-9071
- Classification
-
Biowissenschaften, Biologie
- Event
-
Veröffentlichung
- (where)
-
Konstanz
- (who)
-
Bibliothek der Universität Konstanz
- (when)
-
2007
- Creator
- URN
-
urn:nbn:de:bsz:352-opus-37005
- Rights
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
25.03.2025, 1:51 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.
Associated
- Wegrzyn, Renee D.
- Deuerling, Elke
- Bibliothek der Universität Konstanz
Time of origin
- 2007
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Trigger factor in complex with the ribosome forms a molecular cradle for nascent proteins
Fluorescence-based monitoring of ribosome assembly landscapes
Dissecting functional similarities of ribosome-associated chaperones from Saccharomyces cerevisiae and Escherichia coli
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Ribosome-associated chaperones as key players in proteostasis
Mechanisms of protein folding : molecular chaperones and their application in biotechnology
Identifizierung und Analyse des ftsH-Gens, einem neuen allgemeinen Stressgen von Bacillus subtilis
A cradle for new proteins : trigger factor at the ribosome
Cotranslational sorting and processing of newly synthesized proteins in eukaryotes
Chaperone-assisted folding of newly synthesized proteins in the cytosol
Trigger factor and DnaK cooperate in folding of newly synthesized proteins
Trigger factor in complex with the ribosome forms a molecular cradle for nascent proteins
Fluorescence-based monitoring of ribosome assembly landscapes
Dissecting functional similarities of ribosome-associated chaperones from Saccharomyces cerevisiae and Escherichia coli
Insights into the Aggregation Mechanism of PolyQ Proteins with Different Glutamine Repeat Lengths
Ribosome Assembly as Antimicrobial Target
Ribosome-associated chaperones as key players in proteostasis
Mechanisms of protein folding : molecular chaperones and their application in biotechnology
Identifizierung und Analyse des ftsH-Gens, einem neuen allgemeinen Stressgen von Bacillus subtilis
A cradle for new proteins : trigger factor at the ribosome
Cotranslational sorting and processing of newly synthesized proteins in eukaryotes
Chaperone-assisted folding of newly synthesized proteins in the cytosol
Trigger factor and DnaK cooperate in folding of newly synthesized proteins
Trigger factor in complex with the ribosome forms a molecular cradle for nascent proteins
Fluorescence-based monitoring of ribosome assembly landscapes
Dissecting functional similarities of ribosome-associated chaperones from Saccharomyces cerevisiae and Escherichia coli
Insights into the Aggregation Mechanism of PolyQ Proteins with Different Glutamine Repeat Lengths