NMR relaxation unravels interdomain crosstalk of the two domain prolyl isomerase and chaperone SlyD
- Standort
-
Deutsche Nationalbibliothek Frankfurt am Main
- Umfang
-
Online-Ressource
- Sprache
-
Englisch
- Erschienen in
-
In: Biochimica et Biophysica Acta : Proteins and Proteomics ; 1814 (2011), 7. - S. 873-881. - ISSN 1570-9639. - eISSN 1878-1454
- Ereignis
-
Veröffentlichung
- (wo)
-
Konstanz
- (wer)
-
KOPS Universität Konstanz
- (wann)
-
2011
- Urheber
- URN
-
urn:nbn:de:bsz:352-2-nel2g86sr65t3
- Rechteinformation
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Letzte Aktualisierung
-
14.08.2025, 11:03 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
- Kovermann, Michael
- Zierold, Robert
- Haupt, Caroline
- Löw, Christian
- Balbach, Jochen
- KOPS Universität Konstanz
Entstanden
- 2011
Ähnliche Objekte (12)
Catalysis of protein folding by prolyl isomerase
Molecular insights into substrate recognition and catalytic mechanism of the chaperone and FKBP peptidyl-prolyl isomerase SlyD
Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins
Synthese von Inhibitoren der humanen Peptidyl-Prolyl-cis-trans-Isomerase Pin1
Studien zu der thaumarchaealen Prolyl-Isomerase NmPin aus Nitrosopumilus maritimus
Cellular localization and function of peptidyl-prolyl cis-trans isomerase hPar14
Molecular function of the prolyl cis/trans isomerase and metallochaperone SlyD
Prolyl isomerase Pin1: a promoter of cancer and a target for therapy
Cellular localization and function of peptidyl-prolyl cis-trans isomerase hPar14
The Peptidyl-prolyl Isomerase Pin1 in Neuronal Signaling: from Neurodevelopment to Neurodegeneration
Prolyl‐isomerase Pin1 controls normal and cancer stem cells of the breast
Prolyl‐isomerase Pin1 controls normal and cancer stem cells of the breast
Catalysis of protein folding by prolyl isomerase
Molecular insights into substrate recognition and catalytic mechanism of the chaperone and FKBP peptidyl-prolyl isomerase SlyD
Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins
Synthese von Inhibitoren der humanen Peptidyl-Prolyl-cis-trans-Isomerase Pin1
Studien zu der thaumarchaealen Prolyl-Isomerase NmPin aus Nitrosopumilus maritimus
Cellular localization and function of peptidyl-prolyl cis-trans isomerase hPar14
Molecular function of the prolyl cis/trans isomerase and metallochaperone SlyD
Prolyl isomerase Pin1: a promoter of cancer and a target for therapy
Cellular localization and function of peptidyl-prolyl cis-trans isomerase hPar14
The Peptidyl-prolyl Isomerase Pin1 in Neuronal Signaling: from Neurodevelopment to Neurodegeneration
Prolyl‐isomerase Pin1 controls normal and cancer stem cells of the breast
Prolyl‐isomerase Pin1 controls normal and cancer stem cells of the breast
Catalysis of protein folding by prolyl isomerase
Molecular insights into substrate recognition and catalytic mechanism of the chaperone and FKBP peptidyl-prolyl isomerase SlyD
Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins
Synthese von Inhibitoren der humanen Peptidyl-Prolyl-cis-trans-Isomerase Pin1
Studien zu der thaumarchaealen Prolyl-Isomerase NmPin aus Nitrosopumilus maritimus
Cellular localization and function of peptidyl-prolyl cis-trans isomerase hPar14
Molecular function of the prolyl cis/trans isomerase and metallochaperone SlyD
Prolyl isomerase Pin1: a promoter of cancer and a target for therapy
Cellular localization and function of peptidyl-prolyl cis-trans isomerase hPar14
The Peptidyl-prolyl Isomerase Pin1 in Neuronal Signaling: from Neurodevelopment to Neurodegeneration
Prolyl‐isomerase Pin1 controls normal and cancer stem cells of the breast