Isoform-Specific Inhibition of Cyclophilins-Reference-Cited by-同舟云学术

Isoform-Specific Inhibition of Cyclophilins

Published:2009-06-16 Issue:26 Volume:48 Page:6268-6277
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Daum Sebastian¹,Schumann Michael¹,Mathea Sebastian¹,Aumüller Tobias¹,Balsley Molly A.²,Constant Stephanie L.²,de Lacroix Boris Féaux³,Kruska Fabian³,Braun Manfred³,Schiene-Fischer Cordelia¹

Affiliation:

1. Max Planck Research Unit for Enzymology of Protein Folding, Weinbergweg 22, 06120 Halle/Saale, Germany

2. Department of Microbiology, Immunology and Tropical Medicine, The George Washington University, 2300 I Street NW, Washington, D.C. 20037

3. Department of Chemistry, University of Düsseldorf, Universitätstrasse 1, D-40225 Düsseldorf, Germany

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi9007287

Reference67 articles.

1. Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins

2. Peptidyl-prolyl cis-trans isomerase is the cyclosporin A-binding protein cyclophilin

3. Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexes

4. Regulation of peptide bond cis/trans isomerization by enzyme catalysis and its implication in physiological processes

5. Human and Escherichia coli cyclophilins: sensitivity to inhibition by the immunosuppressant cyclosporin A correlates with a specific tryptophan residue

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