Cotranslational sorting and processing of newly synthesized proteins in eukaryotes
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- Extent
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Online-Ressource
- Language
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Englisch
- Bibliographic citation
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In: Trends in Biochemical Sciences. Elsevier. 2024, 49(2), pp. 105-118. ISSN 0968-0004. eISSN 1362-4326. Available under: doi: 10.1016/j.tibs.2023.10.003
- Event
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Veröffentlichung
- (where)
-
Konstanz
- (who)
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KOPS Universität Konstanz
- (when)
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2024
- Creator
- URN
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urn:nbn:de:bsz:352-2-pwyyt7eou9zb7
- Rights
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Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
14.08.2025, 10:56 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
- Gamerdinger, Martin
- Deuerling, Elke
- KOPS Universität Konstanz
Time of origin
- 2024
Other Objects (12)
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Trigger factor and DnaK cooperate in folding of newly synthesized proteins
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Getting newly synthesized proteins into shape
Trigger factor and DnaK cooperate in folding of newly synthesized proteins
Trigger factor flexibility
Molecular guardians for newborn proteins : ribosome-associated chaperones and their role in protein folding
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The amino-terminal 118 amino acids of Escherichia coli trigger factor constitute a domain that is necessary and sufficient for binding to ribosomes
Chaperone-assisted folding of newly synthesized proteins in the cytosol
Trigger factor and DnaK cooperate in folding of newly synthesized proteins
Identifizierung und Analyse des ftsH-Gens, einem neuen allgemeinen Stressgen von Bacillus subtilis
Getting newly synthesized proteins into shape
Trigger factor and DnaK cooperate in folding of newly synthesized proteins
Trigger factor flexibility
Molecular guardians for newborn proteins : ribosome-associated chaperones and their role in protein folding
Fluorosomen werfen Licht auf Ribosomenproduktion
Ribosome-associated chaperones as key players in proteostasis
Macrolides : the plug is out
Mechanisms of protein folding : molecular chaperones and their application in biotechnology
The amino-terminal 118 amino acids of Escherichia coli trigger factor constitute a domain that is necessary and sufficient for binding to ribosomes
Chaperone-assisted folding of newly synthesized proteins in the cytosol
Trigger factor and DnaK cooperate in folding of newly synthesized proteins
Identifizierung und Analyse des ftsH-Gens, einem neuen allgemeinen Stressgen von Bacillus subtilis
Getting newly synthesized proteins into shape
Trigger factor and DnaK cooperate in folding of newly synthesized proteins
Trigger factor flexibility
Molecular guardians for newborn proteins : ribosome-associated chaperones and their role in protein folding
Fluorosomen werfen Licht auf Ribosomenproduktion
Ribosome-associated chaperones as key players in proteostasis
Macrolides : the plug is out
Mechanisms of protein folding : molecular chaperones and their application in biotechnology