The amino-terminal 118 amino acids of Escherichia coli trigger factor constitute a domain that is necessary and sufficient for binding to ribosomes
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- Extent
-
Online-Ressource
- Language
-
Englisch
- Bibliographic citation
-
In: Journal of Biological Chemistry ; 272 (1997), 35. - S. 21865-21871. - ISSN 0021-9258. - eISSN 1083-351X
- Classification
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Biowissenschaften, Biologie
- Event
-
Veröffentlichung
- (where)
-
Konstanz
- (who)
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Bibliothek der Universität Konstanz
- (when)
-
2007
- Creator
- URN
-
urn:nbn:de:bsz:352-opus-37287
- Rights
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
14.08.2025, 10:53 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
- Hesterkamp, Thomas
- Deuerling, Elke
- Bukau, Bernd
- Bibliothek der Universität Konstanz
Time of origin
- 2007
Other Objects (12)
Identifizierung und Analyse des ftsH-Gens, einem neuen allgemeinen Stressgen von Bacillus subtilis
Trigger factor and DnaK cooperate in folding of newly synthesized proteins
Fluorosomen werfen Licht auf Ribosomenproduktion
Trigger factor flexibility
Molecular guardians for newborn proteins : ribosome-associated chaperones and their role in protein folding
Ribosome-associated chaperones as key players in proteostasis
Macrolides : the plug is out
Cotranslational sorting and processing of newly synthesized proteins in eukaryotes
Chaperone-assisted folding of newly synthesized proteins in the cytosol
Dynamics of Trigger Factor Interaction with Translating Ribosomes
A dual function for chaperones SSB–RAC and the NAC nascent polypeptide–associated complex on ribosomes
The ftsH gene of Bacillus subtilis is transiently induced after osmotic and temperature upshift
Identifizierung und Analyse des ftsH-Gens, einem neuen allgemeinen Stressgen von Bacillus subtilis
Trigger factor and DnaK cooperate in folding of newly synthesized proteins
Fluorosomen werfen Licht auf Ribosomenproduktion
Trigger factor flexibility
Molecular guardians for newborn proteins : ribosome-associated chaperones and their role in protein folding
Ribosome-associated chaperones as key players in proteostasis
Macrolides : the plug is out
Cotranslational sorting and processing of newly synthesized proteins in eukaryotes
Chaperone-assisted folding of newly synthesized proteins in the cytosol
Dynamics of Trigger Factor Interaction with Translating Ribosomes
A dual function for chaperones SSB–RAC and the NAC nascent polypeptide–associated complex on ribosomes
The ftsH gene of Bacillus subtilis is transiently induced after osmotic and temperature upshift
Identifizierung und Analyse des ftsH-Gens, einem neuen allgemeinen Stressgen von Bacillus subtilis
Trigger factor and DnaK cooperate in folding of newly synthesized proteins
Fluorosomen werfen Licht auf Ribosomenproduktion
Trigger factor flexibility
Molecular guardians for newborn proteins : ribosome-associated chaperones and their role in protein folding
Ribosome-associated chaperones as key players in proteostasis
Macrolides : the plug is out
Cotranslational sorting and processing of newly synthesized proteins in eukaryotes
Chaperone-assisted folding of newly synthesized proteins in the cytosol
Dynamics of Trigger Factor Interaction with Translating Ribosomes
A dual function for chaperones SSB–RAC and the NAC nascent polypeptide–associated complex on ribosomes