Structure-activity studies of rapamycin analogs: evidence that the C-7 methoxy group is part of the effector domain and positioned at the FKBP12-FRAP interface
Open Access
- 31 July 1995
- journal article
- Published by Elsevier in Chemistry & Biology
- Vol. 2 (7) , 471-481
- https://doi.org/10.1016/1074-5521(95)90264-3
Abstract
No abstract availableKeywords
This publication has 19 references indexed in Scilit:
- Manipulation of the Rapamycin Effector Domain. Selective Nucleophilic Substitution of the C7 Methoxy GroupThe Journal of Organic Chemistry, 1994
- A Putative Sirolimus (Rapamycin) Effector ProteinBiochemical and Biophysical Research Communications, 1994
- A mammalian protein targeted by G1-arresting rapamycin–receptor complexNature, 1994
- Rapamycin: A novel immunosuppressive macrolideMedicinal Research Reviews, 1994
- Target of rapamycin in yeast, TOR2, is an essential phosphatidylinositol kinase homolog required for G1 progressionCell, 1993
- Atomic Structures of the Human Immunophilin FKBP-12 Complexes with FK506 and RapamycinJournal of Molecular Biology, 1993
- Inhibition of T cell signaling by immunophilin-ligand complexes correlates with loss of calcineurin phosphatase activityBiochemistry, 1992
- Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexesCell, 1991
- Chemistry and Biology of the Immunophilins and Their Immunosuppressive LigandsScience, 1991
- CHAIN — A crystallographic modeling programJournal of Molecular Graphics, 1988