pH Titration of the histidine residues of cyclophilin and FK506 binding protein in the absence and presence of immunosuppressant ligands
- 1 November 1994
- journal article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
- Vol. 1209 (1) , 24-32
- https://doi.org/10.1016/0167-4838(94)90132-5
Abstract
No abstract availableKeywords
This publication has 48 references indexed in Scilit:
- The mechanism of action of cyclosporin A and FK506Published by Elsevier ,2003
- Inhibition of T cell signaling by immunophilin-ligand complexes correlates with loss of calcineurin phosphatase activityBiochemistry, 1992
- The X‐ray structure of a tetrapeptide bound to the active site of human cyclophilin AFEBS Letters, 1992
- Structure of human cyclophilin and its binding site for cyclosporin A determined by X-ray crystallography and NMR spectroscopyNature, 1991
- Mechanistic studies of peptidyl prolyl cis-trans isomerase: evidence for catalysis by distortionBiochemistry, 1990
- A receptor for the immuno-suppressant FK506 is a cis–trans peptidyl-prolyl isomeraseNature, 1989
- A cytosolic binding protein for the immunosuppressant FK506 has peptidyl-prolyl isomerase activity but is distinct from cyclophilinNature, 1989
- Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteinsNature, 1989
- Peptidyl-prolyl cis-trans isomerase is the cyclosporin A-binding protein cyclophilinNature, 1989
- Cyclophilin: A Specific Cytosolic Binding Protein for Cyclosporin AScience, 1984