Pub. Date : 1993 Jul 5
PMID : 7686148
6 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Calcineurin (CaN), a Ca2+/calmodulin-dependent serine/threonine phosphatase, has been shown to be inhibited by the complex of the immunosuppressant cyclosporin A (CsA) and its receptor, cyclophilin (CyP), but not by either alone. | Cyclosporine | peptidylprolyl isomerase G | Homo sapiens |
| 2 | Calcineurin (CaN), a Ca2+/calmodulin-dependent serine/threonine phosphatase, has been shown to be inhibited by the complex of the immunosuppressant cyclosporin A (CsA) and its receptor, cyclophilin (CyP), but not by either alone. | Cyclosporine | peptidylprolyl isomerase G | Homo sapiens |
| 3 | In the presence of cyclosporin, 125I-CyP, shown to bind to CsA, is extensively cross-linked to the B subunit of CaN but not the catalytic A subunit. | Cyclosporine | peptidylprolyl isomerase G | Homo sapiens |
| 4 | In the presence of cyclosporin, 125I-CyP, shown to bind to CsA, is extensively cross-linked to the B subunit of CaN but not the catalytic A subunit. | Cyclosporine | peptidylprolyl isomerase G | Homo sapiens |
| 5 | However, the A subunit is required for binding of the CyP.CsA complex, since cross-linking to recombinant B subunit alone does not occur. | Cyclosporine | peptidylprolyl isomerase G | Homo sapiens |
| 6 | CyP.CsA cross-linking to CaN is Ca2+/calmodulin-dependent with intact CaN, but Ca2+/calmodulin-independent after digestion to remove the calmodulin binding and autoinhibitory domain. | Cyclosporine | peptidylprolyl isomerase G | Homo sapiens |