Chemistry and Biology of the Immunophilins and Their Immunosuppressive Ligands

Cyclophilin: A Specific Cytosolic Binding Protein for Cyclosporin A

Handschumacher, R. E., Harding, M. W., Rice, J. S., Drugge, R. J., & Speicher, D. W. (1984) · Science · doi:10.1126/science.6238408 · Cited by 1,675 · see citing works

Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins

Fischer, G., Wittmann‐Liebold, B., Lang, K., Kiefhaber, T., & Schmid, F. X. (1989) · Nature · doi:10.1038/337476a0 · Cited by 1,408 · see citing works

A receptor for the immuno-suppressant FK506 is a cis–trans peptidyl-prolyl isomerase

Harding, M. W., Gałat, A., Uehling, D., & Schreiber, S. L. (1989) · Nature · doi:10.1038/341758a0 · Cited by 1,400 · see citing works

Cyclosporine

Oates, J. A., Wood, A. J. J., & Kahan, B. D. (1989) · New England Journal of Medicine · doi:10.1056/nejm198912213212507 · Cited by 1,351 · see citing works

Peptidyl-prolyl cis-trans isomerase is the cyclosporin A-binding protein cyclophilin

Takahashi, N., Hayano, T., & Suzuki, M. (1989) · Nature · doi:10.1038/337473a0 · Cited by 1,088 · see citing works

Contingent Genetic Regulatory Events in T Lymphocyte Activation

Crabtree, G. R. (1989) · Science · doi:10.1126/science.2783497 · Cited by 1,071 · see citing works

FK 506 FOR LIVER, KIDNEY, AND PANCREAS TRANSPLANTATION

Starzl, T., Fung, J. J., Venkataraman, R., Todo, S., Demetris, A. J., & Jain, A. (1989) · The Lancet · doi:10.1016/s0140-6736(89)91014-3 · Cited by 1,036 · see citing works

A cytosolic binding protein for the immunosuppressant FK506 has peptidyl-prolyl isomerase activity but is distinct from cyclophilin

Siekierka, J. J., Hung, S. H. Y., Poe, M., Lin, C. S., & SIGAL, N. H. (1989) · Nature · doi:10.1038/341755a0 · Cited by 1,007 · see citing works

Identification of a Putative Regulator of Early T Cell Activation Genes

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Polypeptide chain binding proteins: Catalysts of protein folding and related processes in cells

Rothman, J. E. (1989) · Cell · doi:10.1016/0092-8674(89)90005-6 · Cited by 887 · see citing works

Two distinct signal transmission pathways in T lymphocytes are inhibited by complexes formed between an immunophilin and either FK506 or rapamycin.

Bierer, B. E., Mattila, P. S., Standaert, R. F., Herzenberg, L. A., Burakoff, S. J., Crabtree, G. R., & Schreiber, S. L. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.23.9231 · Cited by 695 · see citing works

Cyclosporin A Specifically Inhibits Function of Nuclear Proteins Involved in T Cell Activation

Emmel, E. A., Verweij, C. L., Durand, D. B., Higgins, K. M., Lacy, E., & Crabtree, G. R. (1989) · Science · doi:10.1126/science.2595372 · Cited by 664 · see citing works

The immunosuppressant FK506 selectively inhibits expression of early T cell activation genes.

Tocci, M. J., Matkovich, D. A., Collier, K., Kwok, P., Dumont, F. J., Lin, S., DeGudicibus, S. J., Siekierka, J. J., Chin, J., & Hutchinson, N. I. (1989) · The Journal of Immunology · doi:10.4049/jimmunol.143.2.718 · Cited by 661 · see citing works

Distinct mechanisms of suppression of murine T cell activation by the related macrolides FK-506 and rapamycin.

Dumont, F. J., Staruch, M. J., Koprak, S., Melino, M. R., & SIGAL, N. H. (1990) · The Journal of Immunology · doi:10.4049/jimmunol.144.1.251 · Cited by 602 · see citing works

Activators and targets

Ptashne, M., & Gann, A. A. F. (1990) · Nature · doi:10.1038/346329a0 · Cited by 455 · see citing works

Discodermolide: a new bioactive polyhydroxylated lactone from the marine sponge Discodermia dissoluta

Gunasekera, S. P., Gunasekera, M., Longley, R. E., & Schulte, G. K. (1990) · The Journal of Organic Chemistry · doi:10.1021/jo00303a029 · Cited by 377 · see citing works

The immunosuppressive macrolides FK-506 and rapamycin act as reciprocal antagonists in murine T cells.

Dumont, F. J., Melino, M. R., Staruch, M. J., Koprak, S., Fischer, P. A., & SIGAL, N. H. (1990) · The Journal of Immunology · doi:10.4049/jimmunol.144.4.1418 · Cited by 355 · see citing works

Probing Immunosuppressant Action with a Nonnatural Immunophilin Ligand

Bierer, B. E., Somers, P. K., Wandless, T. J., Burakoff, S. J., & Schreiber, S. L. (1990) · Science · doi:10.1126/science.1700475 · Cited by 351 · see citing works

South Africa

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Molecular cloning and overexpression of the human FK506-binding protein FKBP

Standaert, R. F., Gałat, A., Verdine, G. L., & Schreiber, S. L. (1990) · Nature · doi:10.1038/346671a0 · Cited by 312 · see citing works

Substrate specificities of the peptidyl prolyl cis-trans isomerase activities of cyclophilin and FK-506 binding protein: evidence for the existence of a family of distinct enzymes

Harrison, R. K., & Stein, R. L. (1990) · Biochemistry · doi:10.1021/bi00468a001 · Cited by 301 · see citing works

Liver Transplantation

Starzl, T. E., Demetris, A. J., & Thiel, D. H. V. (1989) · New England Journal of Medicine · doi:10.1056/nejm198910193211606 · Cited by 292 · see citing works

The ninaA gene required for visual transduction in Drosophila encodes a homologue of cyclosporin A-binding protein

Shieh, B., Stamnes, M. A., Seavello, S., Harris, G. L., & Zuker, C. S. (1989) · Nature · doi:10.1038/338067a0 · Cited by 278 · see citing works

Total synthesis of FK506 and an FKBP probe reagent, [C(8),C(9)-13C2]-FK506

Nakatsuka, M., Ragan, J. A., Sammakia, T., Smith, D. B., Uehling, D., & Schreiber, S. L. (1990) · Journal of the American Chemical Society · doi:10.1021/ja00170a024 · Cited by 257 · see citing works

Cloning, expression, and purification of human cyclophilin in Escherichia coli and assessment of the catalytic role of cysteines by site-directed mutagenesis.

Liu, J., Albers, M. W., Chen, C., Schreiber, S. L., & Walsh, C. T. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.6.2304 · Cited by 246 · see citing works

Peptidyl-prolyl cis-trans-isomerase from Escherichia coli: a periplasmic homolog of cyclophilin that is not inhibited by cyclosporin A.

Liu, J., & Walsh, C. T. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.11.4028 · Cited by 235 · see citing works

Kidney Transplantation Under FK 506

Starzl, T. E. (1990) · JAMA · doi:10.1001/jama.1990.03450010067032 · Cited by 234 · see citing works

Sensitivity to cyclosporin A is mediated by cyclophilin in Neurospora crassa and Saccharomyces cerevisiae

Tropschug, M., Bartheimess, I. B., & Neupert, W. (1989) · Nature · doi:10.1038/342953a0 · Cited by 216 · see citing works

Inhibition of FKBP Rotamase Activity by Immunosuppressant FK506: Twisted Amide Surrogate

Rosen, M. K., Standaert, R. F., Gałat, A., Nakatsuka, M., & Schreiber, S. L. (1990) · Science · doi:10.1126/science.1693013 · Cited by 201 · see citing works

Drosophila ninaA gene encodes an eye-specific cyclophilin (cyclosporine A binding protein).

Schneuwly, S., Shortridge, R. D., Larrivee, D. C., Ono, T., Ozaki, M., & Pak, W. L. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.14.5390 · Cited by 195 · see citing works

Towards a better definition of human leucocyte surface molecules

Knapp, W., RIEBER, P., Dörken, B., Schmidt, R. E., Stein, H., & Borne, A. E. G. K. V. D. (1989) · Immunology Today · doi:10.1016/0167-5699(89)90135-7 · Cited by 194 · see citing works

FK-506 — How much potential?

Thomson, A. W. (1989) · Immunology Today · doi:10.1016/0167-5699(89)90057-1 · Cited by 181 · see citing works

Mechanistic studies of peptidyl prolyl cis-trans isomerase: evidence for catalysis by distortion

Harrison, R. K., & Stein, R. L. (1990) · Biochemistry · doi:10.1021/bi00459a003 · Cited by 166 · see citing works

Isolation and sequence of an FK506-binding protein from N. crassa which catalyses protein folding

Tropschug, M., Wächter, E., Mayer, S., Schönbrunner, E. R., & Schmid, F. X. (1990) · Nature · doi:10.1038/346674a0 · Cited by 153 · see citing works

Cyclophilin binds to the region of cyclosporine involved in its immunosuppressive activity

Quesniaux, V. F. J., Schreier, M., Wenger, R. M., HIESTAND, P. C., Harding, M. W., & Regenmortel, M. H. V. V. (1987) · European Journal of Immunology · doi:10.1002/eji.1830170921 · Cited by 147 · see citing works

FK-506, a potent novel immunosuppressive agent, binds to a cytosolic protein which is distinct from the cyclosporin A-binding protein, cyclophilin.

Siekierka, J. J., Staruch, M. J., Hung, S. H. Y., & SIGAL, N. H. (1989) · The Journal of Immunology · doi:10.4049/jimmunol.143.5.1580 · Cited by 140 · see citing works

Rapamycin and FK506 binding proteins (immunophilins)

Fretz, H., Albers, M. W., Gałat, A., Standaert, R. F., Lane, W. S., Burakoff, S. J., Bierer, B. E., & Schreiber, S. L. (1991) · Journal of the American Chemical Society · doi:10.1021/ja00004a051 · Cited by 134 · see citing works

Substrate specificity for the human rotamase FKBP: a view of FK506 and rapamycin as leucine-(twisted amide)-proline mimics

Albers, M. W., Walsh, C. T., & Schreiber, S. L. (1990) · The Journal of Organic Chemistry · doi:10.1021/jo00304a003 · Cited by 122 · see citing works

Complementary DNA encoding the human T-cell FK506-binding protein, a peptidylprolyl cis-trans isomerase distinct from cyclophilin.

Maki, N., Sekiguchi, F., Nishimaki, J., Miwa, K., Hayano, T., Takahashi, N., & Suzuki, M. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.14.5440 · Cited by 119 · see citing works

Cytoplasmic anchoring proteins and the control of nuclear localization

Hunt, T. (1989) · Cell · doi:10.1016/0092-8674(89)90747-2 · Cited by 106 · see citing works

The affairs of daughterless and the promiscuity of developmental regulators

Cline, T. W. (1989) · Cell · doi:10.1016/0092-8674(89)90280-8 · Cited by 97 · see citing works

CYCLOSPORINE, FK506, AND RAPAMYCIN

Metcalfe, S. M., & Richards, F. M. (1990) · Transplantation · doi:10.1097/00007890-199004000-00028 · Cited by 96 · see citing works

CYCLOPHILIN, A PRIMARY MOLECULAR TARGET FOR CYCLOSPORINE

Harding, M. W., & Handschumacher, R. E. (1988) · Transplantation · doi:10.1097/00007890-198808001-00006 · Cited by 95 · see citing works

HEPATOTROPHIC EFFECTS OF FK506 IN DOGS

Starzl, T. E., Porter, K. A., Mazzaferro, V., Todo, S., Fung, J. J., & Francavilla, A. (1991) · Transplantation · doi:10.1097/00007890-199101000-00010 · Cited by 75 · see citing works

A second cyclophilin-related gene inSaccharomyces cerevisiae

Koser, P. L., Sylvester, D., Livi, G. P., & Bergsma, D. J. (1990) · Nucleic Acids Research · doi:10.1093/nar/18.6.1643 · Cited by 64 · see citing works

Cyclosporin A inhibits degranulation of rat basophilic leukemia cells and human basophils. Inhibition of mediator release without affecting PI hydrolysis or Ca2+ fluxes.

Hultsch, T., Rodriguez, J. L., Kaliner, M., & Hohman, R. J. (1990) · The Journal of Immunology · doi:10.4049/jimmunol.144.7.2659 · Cited by 62 · see citing works

The design and synthesis of immune regulatory agents: Targets and approaches

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The Effect of Cyclosporine on the Use of Hospital Resources for Kidney Transplantation

Showstack, J. A., Katz, P., AMEND, W. J. C., Bernstein, L., Lipton, H., O'Leary, M., Bindman, A. B., & Salvatierra, O. (1989) · New England Journal of Medicine · doi:10.1056/nejm198910193211605 · Cited by 56 · see citing works

Nuclear factors interacting with the mitogen-responsive regulatory region of the interleukin-2 gene.

Brunvand, M. W., Schmidt, A., & Siebenlist, U. K. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)37368-x · Cited by 52 · see citing works

Kinetic β‐deuterium isotope effects suggest a covalent mechanism for the protein folding enzyme peptidylprolyl cis/trans‐isomerase

Fischer, G. S., Berger, E., & Bang, H. (1989) · FEBS Letters · doi:10.1016/0014-5793(89)80735-5 · Cited by 48 · see citing works

s‐Cisand s‐transisomerism in acylproline analogs

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A study of the correlation between cyclophilin binding and in vitro immunosuppressive activity of cyclosporine A and analogues.

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A COMPARISON OF CYCLOSPORINE BINDING BY CYCLOPHILIN AND CALMODULIN AND THE IDENTIFICATION OF A NOVEL 45 KD CYCLOSPORINE-BINDING PHOSPHOPROTEIN IN JURKAT CELLS

Foxwell, B. M. J., HIESTAND, P. C., Wenger, R. M., & Ryffel, B. (1988) · Transplantation · doi:10.1097/00007890-198808001-00007 · Cited by 22 · see citing works

Effects of spergualin and 15-deoxyspergualin on the development of graft-versus-host disease in mice.

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Is there a scaffolding domain within the structure of the immunosuppressive agent cyclosporin a (CsA)? Studies of the cyclophilin binding domain of CsA

Schreiber, S. L., Anthony, N. J., Dorsey, B. D., & Hawley, R. C. (1988) · Tetrahedron Letters · doi:10.1016/s0040-4039(00)82401-6 · Cited by 6 · see citing works

TGF-β SIGNAL TRANSDUCTION

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Protein folding in the cell

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Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexes

Liu, J., Farmer, J. D., Lane, W. S., Friedman, J., Weissman, I., & Schreiber, S. L. (1991) · Cell · doi:10.1016/0092-8674(91)90124-h · Cited by 4,116 · see citing works

The mechanism of action of cyclosporin A and FK506

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A mammalian protein targeted by G1-arresting rapamycin–receptor complex

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Targets for Cell Cycle Arrest by the Immunosuppressant Rapamycin in Yeast

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Two TOR Complexes, Only One of which Is Rapamycin Sensitive, Have Distinct Roles in Cell Growth Control

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Identification of calcineurin as a key signalling enzyme in T-lymphocyte activation

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RAFT1: A mammalian protein that binds to FKBP12 in a rapamycin-dependent fashion and is homologous to yeast TORs

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The tor pathway: a target for cancer therapy

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Target of rapamycin (TOR): an integrator of nutrient and growth factor signals and coordinator of cell growth and cell cycle progression

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Molten Globule and Protein Folding

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Rapamycin-FKBP specifically blocks growth-dependent activation of and signaling by the 70 kd S6 protein kinases

Chung, J., Kuo, C. J., Crabtree, G. R., & Blenis, J. (1992) · Cell · doi:10.1016/0092-8674(92)90643-q · Cited by 1,151 · see citing works

mTOR as a central hub of nutrient signalling and cell growth

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Nuclear association of a T-cell transcription factor blocked by FK-506 and cyclosporin A

Flanagan, W. M., Corthésy, B., Bram, R. J., & Crabtree, G. R. (1991) · Nature · doi:10.1038/352803a0 · Cited by 1,057 · see citing works

Targeted protein degradation: mechanisms, strategies and application

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Enhanced sensitivity of PTEN-deficient tumors to inhibition of FRAP/mTOR

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Calcium Absorption Across Epithelia

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Structure of the FKBP12-Rapamycin Complex Interacting with Binding Domain of Human FRAP

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Microarrays of cells expressing defined cDNAs

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Target of Rapamycin (TOR) in Nutrient Signaling and Growth Control

Loewith, R., & Hall, M. N. (2011) · Genetics · doi:10.1534/genetics.111.133363 · Cited by 900 · see citing works

A human peptidyl–prolyl isomerase essential for regulation of mitosis

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Molecular Recognition of Protein−Ligand Complexes: Applications to Drug Design

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Controlling Signal Transduction with Synthetic Ligands

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Target of rapamycin in yeast, TOR2, is an essential phosphatidylinositol kinase homolog required for G1 progression

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Stabilization of calcium release channel (ryanodine receptor) function by FK506-binding protein

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Calcineurin phosphatase activity in T lymphocytes is inhibited by FK 506 and cyclosporin A.

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Mechanisms of action of cyclosporine.

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Sequence-Specific and Phosphorylation-Dependent Proline Isomerization: A Potential Mitotic Regulatory Mechanism

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Autophagy in metazoans: cell survival in the land of plenty

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Trichostatin A and trapoxin: Novel chemical probes for the role of histone acetylation in chromatin structure and function

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Rapamycin blocks the phosphorylation of 4E‐BP1 and inhibits cap‐dependent initiation of translation.

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Heat shock proteins: molecular chaperones of protein biogenesis

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Features of Selective Kinase Inhibitors

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Rapamycin-Induced Inhibition of the 70-Kilodalton S6 Protein Kinase

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Atomic Structure of FKBP-FK506, an Immunophilin-Immunosuppressant Complex

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Functional association of cyclophilin A with HIV-1 virions

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Rapamycin selectively represses translation of the "polypyrimidine tract" mRNA family.

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Nutrient sensing and signaling in the yeast Saccharomyces cerevisiae

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The Rise of Molecular Glues

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The CH/π interaction: Significance in molecular recognition

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Molecular chaperones and protein folding in plants

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