Branches on the α‐C Atom of Cyclosporin A Residue 3 Result in Direct Calcineurin Inhibition and Rapid Cyclophilin 18 Binding | Zendy

Zhang Yixin | Zendy; Raumgrass Ria | Zendy; Schutkowski Mike | Zendy; Fischer Gunter | Zendy

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Branches on the α‐C Atom of Cyclosporin A Residue 3 Result in Direct Calcineurin Inhibition and Rapid Cyclophilin 18 Binding

Author(s) -

Zhang Yixin,

Raumgrass Ria,

Schutkowski Mike,

Fischer Gunter

Publication year - 2004

Publication title -

chembiochem

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.05

H-Index - 126

eISSN - 1439-7633

pISSN - 1439-4227

DOI - 10.1002/cbic.200400020

Subject(s) - cyclophilin , calcineurin , cyclophilin a , chemistry , residue (chemistry) , fkbp , phosphatase , cyclosporins , peptidylprolyl isomerase , biochemistry , plasma protein binding , enzyme , stereochemistry , biology , microbiology and biotechnology , transplantation , isomerase , medicine , gene

It no longer takes two . We report on cyclosporin A (CsA) derivatives that inhibit calcineurin protein phosphatase activity without first forming a binary complex with cyclophilin 18. Furthermore, these derivatives are rapid binding inhibitors for cyclophilin 18, whereas CsA is a slow binding inhibitor.

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