Cotranslational sorting and processing of newly synthesized proteins in eukaryotes
- Standort
-
Deutsche Nationalbibliothek Frankfurt am Main
- Umfang
-
Online-Ressource
- Sprache
-
Englisch
- Erschienen in
-
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
- Ereignis
-
Veröffentlichung
- (wo)
-
Konstanz
- (wer)
-
KOPS Universität Konstanz
- (wann)
-
2024
- Urheber
- URN
-
urn:nbn:de:bsz:352-2-pwyyt7eou9zb7
- Rechteinformation
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Letzte Aktualisierung
-
14.08.2025, 10:56 MESZ
Datenpartner
Dieses Objekt wird bereitgestellt von:
Deutsche Nationalbibliothek. Bei Fragen zum Objekt wenden Sie sich bitte an den Datenpartner.
Deutsche Nationalbibliothek. Bei Fragen zum Objekt wenden Sie sich bitte an den Datenpartner.
Beteiligte
- Gamerdinger, Martin
- Deuerling, Elke
- KOPS Universität Konstanz
Entstanden
- 2024
Ähnliche Objekte (12)
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
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
The ftsH gene of Bacillus subtilis is transiently induced after osmotic and temperature upshift
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
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
The ftsH gene of Bacillus subtilis is transiently induced after osmotic and temperature upshift
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
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
The ftsH gene of Bacillus subtilis is transiently induced after osmotic and temperature upshift