Your browser doesn't support javascript.
loading
Fine tuning the inhibition profile of cyclosporine A by derivatization of the MeBmt residue.
Prell, Erik; Kahlert, Viktoria; Rücknagel, Karl Peter; Malesevic, Miroslav; Fischer, Gunter.
Affiliation
  • Prell E; Max Planck Research Unit for Enzymology of Protein Folding, Weinbergweg 22, 06120 Halle/Saale, Germany.
Chembiochem ; 14(1): 63-5, 2013 Jan 02.
Article in En | MEDLINE | ID: mdl-23225707
ABSTRACT
Unique respect The biological properties of four CsA derivatives were fine-tuned by tractable modifications of the MeBmt residue. The new CsA derivatives share strong inhibitory activity toward cyclophilins (Cyps), but each is unique with respect to immunosuppressive action and cellular localization. These CsA analogues can be used to study the physiological roles of extracellular Cyps.
Subject(s)
Fulltext
Add to My VHL
Print
XML
PubMed Links
Search on Google

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Threonine / Drug Design / Cyclosporine / Enzyme Inhibitors Limits: Humans Language: En Journal: Chembiochem Journal subject: BIOQUIMICA Year: 2013 Document type: Article Affiliation country: Germany
Fulltext
Add to My VHL
Print
XML
PubMed Links
Search on Google

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Threonine / Drug Design / Cyclosporine / Enzyme Inhibitors Limits: Humans Language: En Journal: Chembiochem Journal subject: BIOQUIMICA Year: 2013 Document type: Article Affiliation country: Germany