Branches on the α-C atom of cyclosporin A residue 3 result in direct calcineurin inhibition and rapid cyclophilin 18 binding

ChemBioChem

Volumn 5, Issue 7, 2004, Pages 1006-1009

  Zhang, Yixin ^a   Raumgrass, Ria ^a,b   Schutkowski, Mike ^a,c   Fischer, Gunter ^a  

^a Max Planck Research Unit   (Germany)

^b DEUTSCHES RHEUMA FORSCHUNGSZENTRUM   (Germany)

^c Jerini AG   (Germany)

Author keywords

Calcineurin; Cyclosporins; Inhibitors; Kinetics; Phosphatase

Indexed keywords

CALCINEURIN INHIBITOR; CYCLOPHILIN; CYCLOSPORIN A;

ARTICLE; BINDING AFFINITY; CRYSTAL STRUCTURE; DRUG EFFECT; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; IMMUNOSUPPRESSIVE TREATMENT; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FUNCTION;

CALCINEURIN; CYCLOPHILINS; CYCLOSPORINE; HUMANS; MODELS, MOLECULAR; PROTEIN BINDING;

EID: 4544238963     PISSN: 14394227     EISSN: None     Source Type: Journal    
DOI: 10.1002/cbic.200400020     Document Type: Article

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