NMR relaxation unravels interdomain crosstalk of the two domain prolyl isomerase and chaperone SlyD
- 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: Biochimica et Biophysica Acta : Proteins and Proteomics ; 1814 (2011), 7. - S. 873-881. - ISSN 1570-9639. - eISSN 1878-1454
- Event
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Veröffentlichung
- (where)
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Konstanz
- (who)
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KOPS Universität Konstanz
- (when)
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2011
- Creator
- URN
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urn:nbn:de:bsz:352-2-nel2g86sr65t3
- Rights
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Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
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14.08.2025, 11:03 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
- Kovermann, Michael
- Zierold, Robert
- Haupt, Caroline
- Löw, Christian
- Balbach, Jochen
- KOPS Universität Konstanz
Time of origin
- 2011
Other Objects (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
Studien zu der thaumarchaealen Prolyl-Isomerase NmPin aus Nitrosopumilus maritimus
Synthese von Inhibitoren der humanen Peptidyl-Prolyl-cis-trans-Isomerase Pin1
Cellular localization and function of peptidyl-prolyl cis-trans isomerase hPar14
Prolyl isomerase Pin1: a promoter of cancer and a target for therapy
Molecular function of the prolyl cis/trans isomerase and metallochaperone SlyD
Prolyl‐isomerase Pin1 controls normal and cancer stem cells of the breast
Cellular localization and function of peptidyl-prolyl cis-trans isomerase hPar14
Prolyl‐isomerase Pin1 controls normal and cancer stem cells of the breast
Synthese neuer heterocyclischer Ketone als Inhibitoren der Peptidyl-Prolyl-cis/trans-Isomerase
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
Studien zu der thaumarchaealen Prolyl-Isomerase NmPin aus Nitrosopumilus maritimus
Synthese von Inhibitoren der humanen Peptidyl-Prolyl-cis-trans-Isomerase Pin1
Cellular localization and function of peptidyl-prolyl cis-trans isomerase hPar14
Prolyl isomerase Pin1: a promoter of cancer and a target for therapy
Molecular function of the prolyl cis/trans isomerase and metallochaperone SlyD
Prolyl‐isomerase Pin1 controls normal and cancer stem cells of the breast
Cellular localization and function of peptidyl-prolyl cis-trans isomerase hPar14
Prolyl‐isomerase Pin1 controls normal and cancer stem cells of the breast
Synthese neuer heterocyclischer Ketone als Inhibitoren der Peptidyl-Prolyl-cis/trans-Isomerase
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
Studien zu der thaumarchaealen Prolyl-Isomerase NmPin aus Nitrosopumilus maritimus
Synthese von Inhibitoren der humanen Peptidyl-Prolyl-cis-trans-Isomerase Pin1
Cellular localization and function of peptidyl-prolyl cis-trans isomerase hPar14
Prolyl isomerase Pin1: a promoter of cancer and a target for therapy
Molecular function of the prolyl cis/trans isomerase and metallochaperone SlyD
Prolyl‐isomerase Pin1 controls normal and cancer stem cells of the breast
Cellular localization and function of peptidyl-prolyl cis-trans isomerase hPar14
Prolyl‐isomerase Pin1 controls normal and cancer stem cells of the breast