The DOI matches its Crossref record; 55 of the 56 references it cites were found in a registry or an index.
Chemistry and Biology of the Immunophilins and Their Immunosuppressive Ligands
Abstract
Cyclosporin A, FK506, and rapamycin are inhibitors of specific signal transduction pathways that lead to T lymphocyte activation. These immunosuppressive agents bind with high affinity to cytoplasmic receptors termed immunophilins (immunosuppressant binding proteins). Studies in this area have focused on the structural basis for the molecular recognition of immunosuppressants by immunophilins and the biological consequences of their interactions. Defining the biological roles of this emerging family of receptors and their ligands may illuminate the process of protein trafficking in cells and the mechanisms of signal transmission through the cytoplasm.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“The natural product rapamycin binds to FKBP12, leading to the recruitment of mTORC1, resulting in partial inhibition of mTORC1 7.”
From Manumycin polyketides act as molecular glues between UBR7 and P53 (2020) · cites this paper as [7]
Citations
Cites
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
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
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 1,396
Self-citationOates, J. A., Wood, A. J. J., & Kahan, B. D. (1989) · New England Journal of Medicine · doi:10.1056/nejm198912213212507 · Cited by 1,351
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 1,075
Contingent Genetic Regulatory Events in T Lymphocyte Activation
Crabtree, G. R. (1989) · Science · doi:10.1126/science.2783497 · Cited by 1,071
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
Siekierka, J. J., Hung, S. H. Y., Poe, M., Lin, C. S., & SIGAL, N. H. (1989) · Nature · doi:10.1038/341755a0 · Cited by 1,016
Identification of a Putative Regulator of Early T Cell Activation Genes
Shaw, J., Utz, P. J., Durand, D. B., Toole, J. J., Emmel, E. A., & Crabtree, G. R. (1988) · Science · doi:10.1126/science.3260404 · Cited by 946
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
Research works printed but not linked: 2
- Bierer, B. E., Proceedings of the National Academy of Sciences of the United States of America 87: 9231 (1990).
- Matila P. S. EMBO Journal in press.
Cited by
Sorted by citations
Items 901–1,000 of 1,002
Hayman, G. T., & Miernyk, J. A. (1994) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/0167-4781(94)90083-3 · Cited by 20
Quinkert, G., Bang, H., & Reichert, D. (1996) · Helvetica Chimica Acta · doi:10.1002/hlca.19960790504 · Cited by 22
Rapamycin inhibits IL-1-mediated interferon-gamma production in the YAC-1 T cell lymphoma
Altmeyer, A., & Dumont, F. J. (1993) · Cytokine · doi:10.1016/1043-4666(93)90052-7 · Cited by 20
Bundick, R. V., Craggs, R. I., & Holness, E. (1995) · Clinical & Experimental Immunology · doi:10.1111/j.1365-2249.1995.tb05574.x · Cited by 20
Tüter, G., Serdar, M. A., Yalım, M., Gurhan, İ. D., & Baloş, K. (2002) · Journal of Periodontology · doi:10.1902/jop.2002.73.11.1273 · Cited by 20
Mikami, K., & Yoshida, A. (1994) · Tetrahedron Letters · doi:10.1016/0040-4039(94)80120-7 · Cited by 20
Immunopharmacologic Therapy in Renal Transplantation
SHOKER, A. S. (1996) · Pharmacotherapy The Journal of Human Pharmacology and Drug Therapy · doi:10.1002/j.1875-9114.1996.tb03638.x · Cited by 20
Copeland, R. A. (2013) · doi:10.1002/9781118540398.ch6 · Cited by 20
Rapamycin synthetic studies. 1. Construction of the C(27)-C(42) subunit
Smith, A. B., Condon, S. M., McCauley, J. A., Leahy, J. W., Leazer, J. L., & Maleczka, R. E. (1994) · Tetrahedron Letters · doi:10.1016/s0040-4039(00)73279-5 · Cited by 20
Presenilin, γ-Secretase, and the Search for Pathogenic Triggers of Alzheimer’s Disease
Wolfe, M. S. (2025) · Biochemistry · doi:10.1021/acs.biochem.4c00830 · Cited by 21
Gobeil, S., Bobay, B. G., Juvvadi, P. R., Cole, D. C., Heitman, J., Steinbach, W. J., Venters, R. A., & Spicer, L. D. (2021) · mBio · doi:10.1128/mbio.03000-21 · Cited by 18
Synthesis and immunosuppressive activity of new cyclolinopeptide A analogs modified with β‐prolines
Katarzyńska, J., Mazur, A., Bilska, M., Adamek, E., Zimecki, M., Jankowski, S., & Zabrocki, J. (2008) · Journal of Peptide Science · doi:10.1002/psc.1069 · Cited by 20
Analysis of rapamycin induced autophagy in Dictyostelium discoideum.
Swer, P. B., Lohia, R., & Saran, S. (2014) · PubMed · Cited by 19
Xing, H., Yang, X., Liu, T., Lin, J., Chen, X., & Gong, Y. (2012) · Leukemia Research · doi:10.1016/j.leukres.2011.12.018 · Cited by 19
Niehl, A., Zhang, Z. J., Kuiper, M. T. R., Peck, S. C., & Heinlein, M. (2013) · Journal of Proteome Research · doi:10.1021/pr3010698 · Cited by 19
Towards New Therapies for Parkinson's Disease
Finkelstein, D. I. (2011) · InTech eBooks · doi:10.5772/954 · Cited by 19
A concise synthesis of AG5473/5507 utilizing N-acyliminium ion chemistry
Guo, C., Reich, S., Showalter, R., Villafranca, E., & Dong, L. (2000) · Tetrahedron Letters · doi:10.1016/s0040-4039(00)00846-7 · Cited by 19
Analogs of cyclosporin A modified at the D-Ala8 position.
Patchett, A. A., Taub, D., Hensens, O. D., Goegelman, R. T., Yang, L., Dumont, F. J., Peterson, L., & SIGAL, N. H. (1992) · The Journal of Antibiotics · doi:10.7164/antibiotics.45.94 · Cited by 19
Göthel, S. F., Schmid, R., Wipat, A., Carter, N. M., Emmerson, P. T., Harwood, C. R., & Marahiel, M. A. (1997) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1997.00059.x · Cited by 19
Garrity, G. M., Heimbuch, B. K., Motamedi, H., & Shafiee, A. R. (1993) · Journal of Industrial Microbiology & Biotechnology · doi:10.1007/bf01570127 · Cited by 19
Structure−Activity Studies of Ground- and Transition-State Analogue Inhibitors of Cyclophilin
Wang, H. C., Kim, K., Bakhtiar, R., & Germanas, J. P. (2001) · Journal of Medicinal Chemistry · doi:10.1021/jm010009r · Cited by 19
ENHANCING THE EFFECT OF SECRETED CYCLOPHILIN B ON IMMUNOSUPPRESSIVE ACTIVITY OF CYCLOSPORINE1
Denys, A., Allain, F., Masy, E., Dessaint, J., & Spik, G. ̈. (1998) · Transplantation · doi:10.1097/00007890-199804270-00012 · Cited by 19
Nørregaard‐Madsen, M., Myglnd, B., Pedersen, R., Valentin‐Hansen, P., & Søgaard‐Andersen, L. (1994) · Molecular Microbiology · doi:10.1111/j.1365-2958.1994.tb01333.x · Cited by 19
Kaymaz, M., Emmez, H., Bukan, N. C., Dursun, A., Kurt, G., Paşaoğlu, H., & Paşaoğlu, A. (2004) · Spinal Cord · doi:10.1038/sj.sc.3101621 · Cited by 19
Yellow Lupine Cyclophilin Transcripts Are Highly Accumulated in the Nodule Meristem Zone
Nuc, K., Nuc, P., & Słomski, R. (2001) · Molecular Plant-Microbe Interactions · doi:10.1094/mpmi.2001.14.12.1384 · Cited by 19
HEPATOTROPHIC PROPERTIES IN DOGS OF HUMAN FKBP, THE BINDING PROTEIN FOR FK506 AND RAPAMYCIN
&NA; (1991) · Transplantation · doi:10.1097/00007890-199110000-00038 · Cited by 19
Konno, S.-I., Adachi, M., Asano, K., Gonogami, Y., Ikeda, K., Okamoto, K.-I., & Takahashi, T. (1994) · European Journal of Pharmacology · doi:10.1016/0014-2999(94)90151-1 · Cited by 19
Feigel, M., & Straßner, T. (1993) · Journal of Molecular Structure THEOCHEM · doi:10.1016/0166-1280(93)87112-q · Cited by 19
Improved therapies for Parkinson's disease: life beyond dopamine D2D3 receptors agonists
Williams, M. J., Wright, S., & Lloyd, G. K. (1997) · Trends in Pharmacological Sciences · doi:10.1016/s0165-6147(97)90650-7 · Cited by 19
Distribution characteristics of immunosuppressants FK506 and cyclosporin A in the blood compartment
Takada, K., Katayama, N., Kiriyama, A., & Usuda, H. (1993) · Biopharmaceutics & Drug Disposition · doi:10.1002/bdd.2510140803 · Cited by 19
Metal-dependent nucleotide binding to the Escherichia coli rotamase SlyD
Mitterauer, T., Nanoff, C., Ahorn, H., Freissmuth, M., & HOHENEGGER, M. (1999) · Biochemical Journal · doi:10.1042/0264-6021:3420033 · Cited by 19
Immunopharmacology of new xenobiotic immunosuppressive molecules.
Morris, R. E. (1992) · PubMed · Cited by 19
Kallen, J., Mikol, V., Quesniaux, V. F. J., Walkinshaw, M. D., Schneider-Scherzer, E., Schörgendorfer, K., Weber, G., & Fliri, H. G. (1997) · Biotechnology · doi:10.1002/9783527620890.ch12 · Cited by 19
Sin, N., & Kallmerten, J. L. (1993) · Tetrahedron Letters · doi:10.1016/0040-4039(93)89003-9 · Cited by 19
STAT3–CyPA signaling pathway in endothelial cell apoptosis
Xie, Y., Li, X., & Ge, J. (2019) · Cellular Signalling · doi:10.1016/j.cellsig.2019.109413 · Cited by 18
FKBP52 in Neuronal Signaling and Neurodegenerative Diseases: A Microtubule Story
Chambraud, B., Byrne, C., Méduri, G., Baulieu, E. E., & Giustiniani, J. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23031738 · Cited by 18
Introducing Immunophilins. From Organ Transplantation to Plant Biology
Romano, P. G. N., He, Z., & Luan, S. (2004) · PLANT PHYSIOLOGY · doi:10.1104/pp.103.900108 · Cited by 18
Clardy, J. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.5.1826 · Cited by 18
Choi, C., Li, J.-H., Vaal, M. J., Thomas, C., Limburg, D. C., Wu, Y., Chen, Y., Soni, R., Scott, C., Ross, D. T., et al. (2002) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/s0960-894x(02)00147-6 · Cited by 18
Osada, H. (2000) · Springer eBooks · doi:10.1007/978-4-431-65927-3_1 · Cited by 18
An exceptionally mild and efficient route to dehydroalanine peptides
Ranganathan, D., Shah, K., & Vaish, N. K. (1992) · Journal of the Chemical Society Chemical Communications · doi:10.1039/c39920001145 · Cited by 18
Zeng, L., Zhou, Z. G., Xu, J., Zhao, W., Wang, W., Huang, Y., Cheng, C., Xu, M., Xie, Y., & Mao, Y. (2001) · Cytogenetic and Genome Research · doi:10.1159/000057015 · Cited by 18
Squadrito, F., Altavilla, D., Squadrito, G., Ferlito, M., Campo, G. M., Arlotta, M., Grimaldi, S., Quartarone, C., Saitta, A., & Caputi, A. P. (1999) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0702528 · Cited by 18
Synthesis of secorapamycin esters and amides
Skotnicki, J. S., Kearney, R. M., & Smith, A. L. (1994) · Tetrahedron Letters · doi:10.1016/s0040-4039(00)76509-9 · Cited by 18
Activation-induced apoptosis in Jurkat cells through a myc-independent mechanism
Ruiz-Ruiz, M. D. C., Oliver, F. J., Izquierdo, M., & López‐Rivas, A. (1995) · Molecular Immunology · doi:10.1016/0161-5890(95)00059-n · Cited by 18
The panorama of cyclosporin research
Balakrishnan, K., & Pandey, A. (1996) · Journal of Basic Microbiology · doi:10.1002/jobm.3620360212 · Cited by 18
In Vitro Property and Mode of Action.
Fujine, K., Abe, F., SEKI, N., Ueda, H., Hino, M., & Fujii, T. (2003) · The Journal of Antibiotics · doi:10.7164/antibiotics.56.62 · Cited by 18
Friedman, J. S., Weissman, I. L., Friedman, J. S., & Alpert, S. (1994) · PubMed Central · Cited by 18
Carreau, A., Gueugnon, J., Bénavidès, J., & Vigé, X. (1997) · Neuropharmacology · doi:10.1016/s0028-3908(97)00160-3 · Cited by 18
Stereoselective Synthesis of the C1-C7 Segment of (+)-Discodermolide
Miyazawa, M., Oonuma, S., Maruyama, K., & Miyashita, M. (1997) · Chemistry Letters · doi:10.1246/cl.1997.1191 · Cited by 18
Modulation of Nuclear Protein Import
Fujihara, S. M., & Nadler, S. G. (1998) · Biochemical Pharmacology · doi:10.1016/s0006-2952(98)00049-5 · Cited by 18
The “three body solution”: Structural insights into molecular glues
Tomlinson, A. C. A., Knox, J. E., Brunsveld, L., Ottmann, C., & Yano, J. K. (2025) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2025.103007 · Cited by 20
Ferreira, P. A., & Orry, A. J. W. (2012) · Journal of Neurogenetics · doi:10.3109/01677063.2011.647143 · Cited by 17
Risseeuw, M., Clercq, D. J. H. D., Lievens, S., Hillaert, U., Sinnaeve, D., den Broeck, F. V., Martins, J. C., Tavernier, J. H., & Calenbergh, S. V. (2013) · ChemMedChem · doi:10.1002/cmdc.201200493 · Cited by 17
Cyclophilin B facilitates the replication of Orf virus
Zhao, K., Li, J., He, W., Song, D., XiMu, Z., Zhang, D., Zhou, Y., & Gao, F. (2017) · Virology Journal · doi:10.1186/s12985-017-0781-x · Cited by 17
Wu, X., di Vignano, A. T., Zhou, Q., Dziunycz, P., Bai, F., Mi, J., Qin, J., Zu, T., & Hofbauer, G. F. L. (2018) · PLoS Genetics · doi:10.1371/journal.pgen.1007366 · Cited by 17
Zaragoza‐Ojeda, M., Apatiga‐Vega, E., & Arenas‐Huertero, F. (2021) · Oncology Letters · doi:10.3892/ol.2021.12721 · Cited by 17
Computational Insight into Small Molecule Inhibition of Cyclophilins
Sambasivarao, S. V., & Acevedo, O. (2010) · Journal of Chemical Information and Modeling · doi:10.1021/ci1004114 · Cited by 17
Cusack, R. M., Grøndahl, L., Fairlie, D. P., Hanson, G. R., & Gahan, L. R. (2003) · Journal of Inorganic Biochemistry · doi:10.1016/s0162-0134(03)00288-5 · Cited by 17
Solid-Phase synthesis of FKBP12 inhibitors: N-Sulfonyl and N-Carbamoylprolyl/pipecolyl amides
Wei, L., Wu, Y., Wilkinson, D. E., Chen, Y., Soni, R., Scott, C., Ross, D. T., Guo, H., Howorth, P., Valentine, H., et al. (2002) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/s0960-894x(02)00146-4 · Cited by 17
Mechanism of action of cyclosporin in rheumatoid arthritis
Bentin, J. (1995) · Clinical Rheumatology · doi:10.1007/bf02215854 · Cited by 17
Prolactin Receptor Signal Transduction
Clevenger, C. V., Rycyzyn, M. A., Syed, F., & Kline, J. B. (2001) · Endocrine updates · doi:10.1007/978-1-4615-1683-5_18 · Cited by 17
[15] Regulation of gene expression with synthetic dimerizers
Pollock, R. M., & Rivera, V. M. (1999) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(99)06017-6 · Cited by 17
Alemán, C., & Casanovas, J. (2004) · Journal of Molecular Structure THEOCHEM · doi:10.1016/j.theochem.2003.12.039 · Cited by 17
Suzuki, K., & Takahashi, K. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.2737 · Cited by 17
Frassanito, M. A., Dammacco, R., Fusaro, T., Cusmai, A., Guerriero, S., & Sborgia, C. (2003) · Clinical & Experimental Immunology · doi:10.1046/j.1365-2249.2003.02214.x · Cited by 17
Tacrolimus in Kidney Transplantation
Kliem, V., & Brunkhorst, R. R. (1998) · The Nephron journals/Nephron journals · doi:10.1159/000044985 · Cited by 17
Lin, T. A., & Lawrence, J. C. (1997) · Diabetologia · doi:10.1007/s001250051391 · Cited by 17
Immunosuppressant therapy averts rejection of allogeneic FKBP1A-disrupted CAR-T cells
Maldini, C. R., Messana, A., Bendet, P. B., Camblin, A. J., Musenge, F. M., White, M. L., Rocha, J. J., Coholan, L. J., Karaca, C., Li, F., et al. (2024) · Molecular Therapy · doi:10.1016/j.ymthe.2024.06.022 · Cited by 18
The Formal Total Synthesis of FR252921 – An Immunosuppressant
Yadav, J. S., & Sengupta, S. (2012) · European Journal of Organic Chemistry · doi:10.1002/ejoc.201201097 · Cited by 16
Hinds, T. D., John, K., McBeth, L., Trabbic, C. J., & Sánchez, E. R. (2016) · PPAR Research · doi:10.1155/2016/6218637 · Cited by 16
Peptide Conformation: Stability and Dynamics
Marshall, G. R., Beusen, D. D., & Nikiforovich, G. V. (1995) · Elsevier eBooks · doi:10.1016/b978-012310920-0/50006-1 · Cited by 16
Demetriou, C., Chanudet, E., GOSgene, Joseph, A. P., Topf, M., Thomas, A. C., Bitner-Glindzicz, M. A. K., Regan, L., Stanier, P., & Moore, G. E. (2019) · Human Molecular Genetics · doi:10.1093/hmg/ddz203 · Cited by 15
Erben, E., Daum, S., & Téllez-Iñón, M. T. (2007) · Molecular and Biochemical Parasitology · doi:10.1016/j.molbiopara.2007.03.004 · Cited by 16
Marine invertebrates cross phyla comparisons reveal highly conserved immune machinery
Oren, M., Paz, G., Douek, J., Rosner, A., Amar, K.-O., & Rinkevich, B. (2012) · Immunobiology · doi:10.1016/j.imbio.2012.06.004 · Cited by 16
Cymbimicin A and B, Two Novel Cyclophilin-binding Structures Isolated from Actinomycetes.
FEHR, T., Quesniaux, V. F. J., Sanglier, J., Oberer, L., Gschwind, L., Ponelle, M., SCHILLING, W., Wehrli, S., Enz, A., Zenke, G., et al. (1997) · The Journal of Antibiotics · doi:10.7164/antibiotics.50.893 · Cited by 16
Beneficial effects of FK506 for experimental temporal lobe epilepsy
Nishimura, T., Imai, H., Minabe, Y., Sawa, A., & Kato, N. (2006) · Neuroscience Research · doi:10.1016/j.neures.2006.08.006 · Cited by 16
Omay, S. B., Nakai, K., Kuno, T., Shiku, H., & Nishikawa, M. (1996) · Blood · doi:10.1182/blood.v87.7.2947.bloodjournal8772947 · Cited by 16
Cancer Cell‐Based Genomic and Small Molecule Screens
Caldwell, J. S. (2006) · Advances in cancer research · doi:10.1016/s0065-230x(06)96006-0 · Cited by 16
Stereochemical Course of the Oxidation of l -Pipecolic Acid by the Flavoenzyme l -Pipecolate Oxidase
Zabriskie, T. M., Kelly, W. L., & Liang, X. (1997) · Journal of the American Chemical Society · doi:10.1021/ja970825h · Cited by 16
Use of immunosuppressive agents in ocular diseases
Mochizuki, M., & de Smet, M. D. (1994) · Progress in Retinal and Eye Research · doi:10.1016/1350-9462(94)90020-5 · Cited by 16
Kok, R. G., Christoffels, V. M., Vosman, B., & Hellingwerf, K. J. (1994) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/0167-4781(94)90218-6 · Cited by 16
Albers, M. W., Brown, E. J., Tanaka, A., Williams, R. T., Hall, F. L., & Schreiber, S. L. (1993) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1993.tb17142.x · Cited by 16
Self-citationTepper, M. A. (1993) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1993.tb17147.x · Cited by 16
Trivedi, D. K., Ansari, M. W., Dutta, T., Singh, P., & Tuteja, N. K. (2013) · BMC Research Notes · doi:10.1186/1756-0500-6-555 · Cited by 15
Overcoming resistance to rapalogs in gliomas by combinatory therapies
Grzmil, M., & Hemmings, B. A. (2013) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2013.01.041 · Cited by 15
Park, H., Lee, S. Y., You, Y., Yoon, D. S., Kim, B., Ahn, J. C., & Cho, H. S. (2013) · International Journal of Molecular Sciences · doi:10.3390/ijms14035899 · Cited by 15
Okada, K., Arai, S., Nakase, H., Kohno, H., Nakamura, F., Takeda, M., Toda, Y., Itoh, H., Adachi, S., & Ikemoto, M. (2014) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2014.11.099 · Cited by 15
Jin, L., Wang, D., Gooden, D. M., Ball, C. H., & Fitzgerald, M. C. (2016) · Analytical Chemistry · doi:10.1021/acs.analchem.6b02658 · Cited by 15
Cho, K., Orry, A. J. W., Park, S. E., & Ferreira, P. A. (2015) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.5b00134 · Cited by 15
Mouzaki, Α., Dai, Y., Weil, R., & Rungger, D. (1992) · Cytokine · doi:10.1016/1043-4666(92)90050-2 · Cited by 15
Molecular mode of action of cyclosporin and FK506in human thymocytes
Reem, G. H. (1992) · Journal of Autoimmunity · doi:10.1016/0896-8411(92)90030-t · Cited by 15
Sekiya, M., Ueda, K., Fujita, T., Kitayama, M., Kikuchi, H., Oshima, Y., & Kurata, S. (2006) · Life Sciences · doi:10.1016/j.lfs.2006.08.026 · Cited by 15
Mammalian FKBP-25 and Its Associated Proteins
Leclercq, M., Vinci, F., & Gałat, A. (2000) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.2000.1883 · Cited by 15
Kanoh, N., Honda, K., Simizu, S., Muroi, M., & Osada, H. (2005) · Angewandte Chemie · doi:10.1002/ange.200462370 · Cited by 15
Localization of cyclophilin A and cyclophilin C mRNA in murine kidney using RT-PCR
Otsuka, M., Terada, Y., Yang, T., Nonoguchi, H., Tomita, K., & Marumo, F. (1994) · Kidney International · doi:10.1038/ki.1994.175 · Cited by 15
Cloning, characterization and functional expression of a cyclophilin of Entamoeba histolytica☆
Ostoa‐Saloma, P., Carrero, J. C., Petrossian, P., Hérion, P., Landa, A., & Laclette, J. P. (2000) · Molecular and Biochemical Parasitology · doi:10.1016/s0166-6851(00)00190-0 · Cited by 15
Covalent binding of cyclosporine inhibits irreversibly T-lymphocyte activation
Ryffel, B., Woerly, G., Quesniaux, V. F. J., Husi, H., & Foxwell, B. M. J. (1992) · Biochemical Pharmacology · doi:10.1016/0006-2952(92)90598-d · Cited by 15
Ryffel, B., Willcocks, J. L., Brooks, N., & Woerly, G. (1995) · Immunopharmacology · doi:10.1016/0162-3109(95)00023-m · Cited by 15
Hendrickson, B. A., Zhang, W., Craig, R. J., Yong-Jiu, J., Bierer, B. E., Burakoff, S. J., & DiLella, A. G. (1993) · Gene · doi:10.1016/0378-1119(93)90106-d · Cited by 15
Metadata
- Authors
- Schreiber, S. L.
- Affiliations
- Harvard University (US)
- Corresponding author
- Schreiber, Stuart L.
- ORCID
- Schreiber, Stuart L.
- Venue
- Science
- Published
- 1991-01-18
- Volume
- 251
- Issue
- 4991
- Pages
- 283-287
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2024842574
- Cited by
- 1,494
- References
- 56
- Citations by year
- 2026: 7 · 2025: 21 · 2024: 13 · 2023: 18 · 2022: 17 · 2021: 21 · 2020: 13 · 2019: 15 · 2018: 12 · 2017: 19 · 2016: 23 · 2015: 27 · 2014: 28 · 2013: 34 · 2012: 23
- FWCI
- 15.51
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of General Medical Sciences (GM38627)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Signaling Pathways in Disease
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › S100 Proteins and Annexins
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Interaction Studies and Fluorescence Analysis
- Keywords
- immunophilins, cyclosporine, FK506, rapamycin, T cell activation, signal transduction inhibition, protein trafficking, molecular recognition, protein-ligand binding
- MeSH terms
- Amino Acid Isomerases, Animals, Anti-Bacterial Agents, Carrier Proteins, Cyclosporins, Humans, Immunosuppressive Agents, Isomerases, Ligands, Lymphocyte Activation, Polyenes, Receptors, Immunologic, T-Lymphocytes, Tacrolimus, Peptidylprolyl Isomerase, Sirolimus, Tacrolimus Binding Proteins
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review