Dynamic control of the prolyl isomerase function of the dual-domain SlyD protein
- Standort
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Deutsche Nationalbibliothek Frankfurt am Main
- Umfang
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Online-Ressource
- Sprache
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Englisch
- Erschienen in
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In: Biophysical Chemistry ; 171 (2013). - S. 16-23. - ISSN 0301-4622. - eISSN 1873-4200
- Ereignis
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Veröffentlichung
- (wo)
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Konstanz
- (wer)
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KOPS Universität Konstanz
- (wann)
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2013
- Urheber
- URN
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urn:nbn:de:bsz:352-2-65gn5jvh7f633
- Rechteinformation
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Letzte Aktualisierung
-
25.03.2025, 13:53 MEZ
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Beteiligte
- Kovermann, Michael
- Balbach, Jochen
- KOPS Universität Konstanz
Entstanden
- 2013
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Role of the peptidyl-prolyl cis-trans isomerase Pin1 in the ubiquitin proteasome system (UPS)
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Mip protein of Legionella pneumophila exhibits peptidyl-prolyl cis-trans-isomerase (PPIase) activity
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NMR relaxation unravels interdomain crosstalk of the two domain prolyl isomerase and chaperone SlyD
Catalysis of protein folding by prolyl isomerase
Molecular function of the prolyl cis/trans isomerase and metallochaperone SlyD
The prolyl isomerase domain of PpiD from Escherichia coli shows a parvulin fold but is devoid of catalytic activity
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