TOR Mutations Confer Rapamycin Resistance by Preventing Interaction with FKBP12-Rapamycin (*)
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[1] R. S. Muir,et al. Targets of immunophilin‐immunosuppressant complexes are distinct highly conserved regions of calcineurin A. , 1995, The EMBO journal.
[2] S. Schreiber,et al. Identification of an 11-kDa FKBP12-rapamycin-binding domain within the 289-kDa FKBP12-rapamycin-associated protein and characterization of a critical serine residue. , 1995, Proceedings of the National Academy of Sciences of the United States of America.
[3] R. Abraham,et al. Isolation of a Protein Target of the FKBP12-Rapamycin Complex in Mammalian Cells (*) , 1995, The Journal of Biological Chemistry.
[4] M. Mclaughlin,et al. Interaction between FKBP12-rapamycin and TOR involves a conserved serine residue. , 1994, The Journal of biological chemistry.
[5] V. Berlin,et al. RAPT1, a mammalian homolog of yeast Tor, interacts with the FKBP12/rapamycin complex. , 1994, Proceedings of the National Academy of Sciences of the United States of America.
[6] James M. Roberts,et al. lnterleukin-2-mediated elimination of the p27Kipl cyclin-dependent kinase inhibitor prevented by rapamycin , 1994, Nature.
[7] R. S. Muir,et al. Immunophilins interact with calcineurin in the absence of exogenous immunosuppressive ligands. , 1994, The EMBO journal.
[8] H. Ogawa,et al. An essential gene, ESR1, is required for mitotic cell growth, DNA repair and meiotic recombination in Saccharomyces cerevisiae. , 1994, Nucleic acids research.
[9] J. Heitman,et al. Yeast as model T cells , 1994 .
[10] Paul Tempst,et al. RAFT1: A mammalian protein that binds to FKBP12 in a rapamycin-dependent fashion and is homologous to yeast TORs , 1994, Cell.
[11] Stuart L. Schreiber,et al. A mammalian protein targeted by G1-arresting rapamycin–receptor complex , 1994, Nature.
[12] M. Mclaughlin,et al. Yeast TOR (DRR) proteins: amino-acid sequence alignment and identification of structural motifs. , 1994, Gene.
[13] W M Barnes,et al. PCR amplification of up to 35-kb DNA with high fidelity and high yield from lambda bacteriophage templates. , 1994, Proceedings of the National Academy of Sciences of the United States of America.
[14] L. Hartwell,et al. Mitotic checkpoint genes in budding yeast and the dependence of mitosis on DNA replication and repair. , 1994, Genes & development.
[15] J. Kunz,et al. TOR1 and TOR2 are structurally and functionally similar but not identical phosphatidylinositol kinase homologues in yeast. , 1994, Molecular biology of the cell.
[16] A. Marks,et al. Rapamycin-FKBP12 blocks proliferation, induces differentiation, and inhibits cdc2 kinase activity in a myogenic cell line. , 1993, The Journal of biological chemistry.
[17] S. Elledge,et al. The p21 Cdk-interacting protein Cip1 is a potent inhibitor of G1 cyclin-dependent kinases , 1993, Cell.
[18] William Arbuthnot Sir Lane,et al. Isolation of the cyclosporin-sensitive T cell transcription factor NFATp. , 1993, Science.
[19] R. Abraham,et al. Rapamycin inhibition of interleukin-2-dependent p33cdk2 and p34cdc2 kinase activation in T lymphocytes. , 1993, The Journal of biological chemistry.
[20] S. Schreiber,et al. FKBP-rapamycin inhibits a cyclin-dependent kinase activity and a cyclin D1-Cdk association in early G1 of an osteosarcoma cell line. , 1993, The Journal of biological chemistry.
[21] M. Mclaughlin,et al. Dominant missense mutations in a novel yeast protein related to mammalian phosphatidylinositol 3-kinase and VPS34 abrogate rapamycin cytotoxicity , 1993, Molecular and cellular biology.
[22] T. Curran,et al. The T-cell transcription factor NFATp is a substrate for calcineurin and interacts with Fos and Jun , 1993, Nature.
[23] J. Heitman,et al. Identification of immunosuppressive drug targets in yeast , 1993 .
[24] S. Fields. The Two-Hybrid System to Detect Protein-Protein Interactions , 1993 .
[25] P. Manivasakam,et al. Introducing DNA into Yeast by Transformation , 1993 .
[26] J. Kunz,et al. Target of rapamycin in yeast, TOR2, is an essential phosphatidylinositol kinase homolog required for G1 progression , 1993, Cell.
[27] J J Burbaum,et al. Improved calcineurin inhibition by yeast FKBP12-drug complexes. Crystallographic and functional analysis. , 1993, The Journal of biological chemistry.
[28] R F Standaert,et al. Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and rapamycin. , 1993, Journal of molecular biology.
[29] S. Schreiber,et al. A composite FKBP12-FK506 surface that contacts calcineurin , 1993 .
[30] S. Schreiber,et al. Activation of an inactive immunophilin by mutagenesis , 1993 .
[31] N. Sigal,et al. Characterization of high molecular weight FK-506 binding activities reveals a novel FK-506-binding protein as well as a protein complex. , 1992, The Journal of biological chemistry.
[32] M. Murcko,et al. Charged surface residues of FKBP12 participate in formation of the FKBP12-FK506-calcineurin complex. , 1992, The Journal of biological chemistry.
[33] J. Avruch,et al. Rapamycin-induced inhibition of the 70-kilodalton S6 protein kinase. , 1992, Science.
[34] G. Crabtree,et al. Rapamycin-FKBP specifically blocks growth-dependent activation of and signaling by the 70 kd S6 protein kinases , 1992, Cell.
[35] S. Schreiber,et al. The mechanism of action of cyclosporin A and FK506. , 1992, Immunology today.
[36] G. Crabtree,et al. Nuclear association of a T-cell transcription factor blocked by FK-506 and cyclosporin A , 1991, Nature.
[37] Stuart L. Schreiber,et al. Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexes , 1991, Cell.
[38] J. Heitman,et al. Targets for cell cycle arrest by the immunosuppressant rapamycin in yeast , 1991, Science.
[39] Ellson Y. Chen,et al. Overview of manual and automated DNA sequencing by the dideoxy chain termination method , 1991 .
[40] R F Standaert,et al. Atomic structure of FKBP-FK506, an immunophilin-immunosuppressant complex , 1991, Science.
[41] J. Heitman,et al. FK 506-binding protein proline rotamase is a target for the immunosuppressive agent FK 506 in Saccharomyces cerevisiae. , 1991, Proceedings of the National Academy of Sciences of the United States of America.
[42] N. Sigal,et al. Is cyclophilin involved in the immunosuppressive and nephrotoxic mechanism of action of cyclosporin A? , 1991, The Journal of experimental medicine.
[43] L A Herzenberg,et al. Two distinct signal transmission pathways in T lymphocytes are inhibited by complexes formed between an immunophilin and either FK506 or rapamycin. , 1990, Proceedings of the National Academy of Sciences of the United States of America.
[44] S. Burakoff,et al. Probing immunosuppressant action with a nonnatural immunophilin ligand , 1990, Science.
[45] N. Sigal,et al. The immunosuppressive macrolides FK-506 and rapamycin act as reciprocal antagonists in murine T cells. , 1990, Journal of immunology.
[46] N. Sigal,et al. Distinct mechanisms of suppression of murine T cell activation by the related macrolides FK-506 and rapamycin. , 1990, Journal of immunology.
[47] S. Schreiber,et al. A receptor for the immuno-suppressant FK506 is a cis–trans peptidyl-prolyl isomerase , 1989, Nature.
[48] Nolan H. Sigal,et al. A cytosolic binding protein for the immunosuppressant FK506 has peptidyl-prolyl isomerase activity but is distinct from cyclophilin , 1989, Nature.
[49] R. Sikorski,et al. A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. , 1989, Genetics.
[50] S. Ho,et al. Site-directed mutagenesis by overlap extension using the polymerase chain reaction. , 1989, Gene.
[51] T. Kiefhaber,et al. Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins , 1989, Nature.
[52] T. Hayano,et al. Peptidyl-prolyl cis-trans isomerase is the cyclosporin A-binding protein cyclophilin , 1989, Nature.
[53] F. Winston,et al. A ten-minute DNA preparation from yeast efficiently releases autonomous plasmids for transformation of Escherichia coli. , 1987, Gene.