- Location
-
Deutsche Nationalbibliothek Frankfurt am Main
- Extent
-
Online-Ressource
- Language
-
Deutsch
- Bibliographic citation
-
In: Journal of Biological Chemistry ; 283 (2008), 7. - S. 4124-4132. - ISSN 0021-9258. - eISSN 1083-351X
- Classification
-
Biowissenschaften, Biologie
- Event
-
Veröffentlichung
- (where)
-
Konstanz
- (who)
-
Bibliothek der Universität Konstanz
- (when)
-
2009
- Creator
- URN
-
urn:nbn:de:bsz:352-opus-76393
- Rights
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
14.08.2025, 10:45 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
- Rutkowska, Anna
- Mayer, Matthias P.
- Hoffmann, Anja
- Merz, Frieder
- Zachmann-Brand, Beate
- Berger-Schaffitzel, Christiane Helene
- Ban, Nenad
- Deuerling, Elke
- Bukau, Bernd
- Bibliothek der Universität Konstanz
Time of origin
- 2009
Other Objects (12)
Identifizierung und Analyse des ftsH-Gens, einem neuen allgemeinen Stressgen von Bacillus subtilis
Trigger factor flexibility
The amino-terminal 118 amino acids of Escherichia coli trigger factor constitute a domain that is necessary and sufficient for binding to ribosomes
Trigger factor and DnaK cooperate in folding of newly synthesized proteins
A cradle for new proteins : trigger factor at the ribosome
Fluorosomen werfen Licht auf Ribosomenproduktion
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
Functional dissection of trigger factor and DnaK : interactions with nascent polypeptides and thermally denatured proteins
Identifizierung und Analyse des ftsH-Gens, einem neuen allgemeinen Stressgen von Bacillus subtilis
Trigger factor flexibility
The amino-terminal 118 amino acids of Escherichia coli trigger factor constitute a domain that is necessary and sufficient for binding to ribosomes
Trigger factor and DnaK cooperate in folding of newly synthesized proteins
A cradle for new proteins : trigger factor at the ribosome
Fluorosomen werfen Licht auf Ribosomenproduktion
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
Functional dissection of trigger factor and DnaK : interactions with nascent polypeptides and thermally denatured proteins
Identifizierung und Analyse des ftsH-Gens, einem neuen allgemeinen Stressgen von Bacillus subtilis
Trigger factor flexibility
The amino-terminal 118 amino acids of Escherichia coli trigger factor constitute a domain that is necessary and sufficient for binding to ribosomes
Trigger factor and DnaK cooperate in folding of newly synthesized proteins
A cradle for new proteins : trigger factor at the ribosome
Fluorosomen werfen Licht auf Ribosomenproduktion
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