The DOI matches its Crossref record; 43 of the 43 references it cites were found in a registry or an index.
Glucocorticoid Resistance in the Squirrel Monkey Is Associated with Overexpression of the Immunophilin FKBP511
Abstract
Squirrel monkeys are neotropical primates that have high circulating cortisol to compensate for expression of glucocorticoid receptors (GRs) with reduced affinity. The low binding affinity of squirrel monkey GR does not result from substitutions in the receptor, because squirrel monkey GR expressed in vitro exhibits high affinity. Rather, squirrel monkeys express a soluble factor that, in mixing studies of cytosol from squirrel monkey lymphocytes (SML) and mouse L929 cells, reduced GR binding affinity by 11-fold. In an effort to identify this factor, the cellular levels of components of the GR heterocomplex in SML and human lymphocytes (HL) were compared. The immunophilin FKBP51 was 13-fold higher in SML than in HL cytosol; FKBP52 in SML was 42% of that in HL cytosol. A role for changes in immunophilins, causing glucocorticoid resistance in neotropical primates, is supported by the following: the changes in FKBP51 and FKBP52 were observed in cells from other neotropical primates with glucocorticoid resistance; the elevated level of FKBP51 was reflected in an abundance of FKBP51 in heat shock protein 90 complexes in SML; when cytosols of SML and L929 cells were mixed, the decrease in GR binding was associated with incorporation of FKBP51 into GR heterocomplexes; the effect of SML cytosol on GR binding was reproduced with cytosol from COS cells expressing squirrel monkey FKBP51; and both the effect of SML cytosol on GR binding and the incorporation of FKBP51 into GR heterocomplexes were blocked by FK506. Regulation of GR binding by FKBP51 represents a previously unrecognized mechanism for regulating glucocorticoid sensitivity.
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
“Thus, the relative concentrations of FKBP51 and FKBP52 in the cell dictate the level of GR activity in vivo23,28,55.”
From Cryo-EM reveals how Hsp90 and FKBP immunophilins co-regulate the glucocorticoid receptor (2023) · cites this paper as [55]
Citations
Cites
Bradford, M. M. (1976) · Analytical Biochemistry · doi:10.1016/0003-2697(76)90527-3 · Cited by 255,302
THE ATTRACTIONS OF PROTEINS FOR SMALL MOLECULES AND IONS
Scatchard, G. (1949) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1949.tb27297.x · Cited by 19,724
The Steroid and Thyroid Hormone Receptor Superfamily
Evans, R. M. (1988) · Science · doi:10.1126/science.3283939 · Cited by 7,394
STEROID RECEPTOR REGULATED TRANSCRIPTION OF SPECIFIC GENES AND GENE NETWORKS
Yamamoto, K. R. (1985) · Annual Review of Genetics · doi:10.1146/annurev.ge.19.120185.001233 · Cited by 1,850
Steroid Receptor Interactions with Heat Shock Protein and Immunophilin Chaperones*
Pratt, W. B., & Toft, D. O. (1997) · Endocrine Reviews · doi:10.1210/edrv.18.3.0303 · Cited by 1,791
Molecular Determinants of Glucocorticoid Receptor Function and Tissue Sensitivity to Glucocorticoids
Bamberger, C. M., Schulte, H. M., & Chrousos, G. P. (1996) · Endocrine Reviews · doi:10.1210/edrv-17-3-245 · Cited by 912
Reduced levels of hsp90 compromise steroid receptor action in vivo
Picard, D., Khursheed, B., Garabedian, M. J., Fortin, M. G., Lindquist, S., & Yamamoto, K. R. (1990) · Nature · doi:10.1038/348166a0 · Cited by 787
Glucocorticoid receptor beta, a potential endogenous inhibitor of glucocorticoid action in humans
Bamberger, C. M., Bamberger, A. M., de Castro, M., & Chrousos, G. P. (1995) · Journal of Clinical Investigation · doi:10.1172/jci117943 · Cited by 642
The Human Glucocorticoid Receptor β Isoform
Oakley, R. H., Sar, M., & Cidlowski, J. A. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.16.9550 · Cited by 562
Identification of a 60-Kilodalton Stress-Related Protein, p60, which Interacts with hsp90 and hsp70
Smith, D. F., Sullivan, W. P., Marion, T. N., Zaitsu, K., Madden, B. J., McCormick, D., & Toft, D. O. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.2.869 · Cited by 269
Self-citation
Cited by
Sorted by citations
The Corticosteroid Receptor Hypothesis of Depression
Holsboer, F. (2000) · Neuropsychopharmacology · doi:10.1016/s0893-133x(00)00159-7 · Cited by 2,181
Woodruff, P. G., Boushey, H. A., Dolganov, G. M., Barker, C. S., Yang, Y. H., Donnelly, S., Ellwanger, A., Sidhu, S. S., Dao-Pick, T. P., Pantoja, C., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0707413104 · Cited by 828
Abbott, D. H., Keverne, E. B., Bercovitch, F. B., Shively, C. A., Mendoza, S. P., Wendy Saltzman, A., Snowdon, C. T., Ziegler, T. E., Banjevic, M., Garland, T., et al. (2003) · Hormones and Behavior · doi:10.1016/s0018-506x(02)00037-5 · Cited by 748
Role of glucocorticoid negative feedback in the regulation of HPA axis pulsatility
Gjerstad, J. K., Lightman, S. L., & Spiga, F. (2018) · Stress · doi:10.1080/10253890.2018.1470238 · Cited by 437
The glucocorticoid responses are shaped by molecular chaperones
Grad, I., & Picard, D. (2007) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2007.05.018 · Cited by 423
The Hsp90‐binding peptidylprolyl isomerase FKBP52 potentiates glucocorticoid signaling in vivo
Riggs, D. L., Roberts, P. J., Chirillo, S. C., Cheung‐Flynn, J., Prapapanich, V., Ratajczak, T., Gaber, R., Picard, D., & Smith, D. F. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg108 · Cited by 353
Self-citationAspects of common marmoset basic biology and life history important for biomedical research.
Abbott, D. H., Barnett, D. K., Colman, R. J., Yamamoto, M. E., & SCHULTZ‐DARKEN, N. J. (2003) · PubMed · Cited by 356
Genome-wide Expression Analysis of Mouse Liver Reveals CLOCK-regulated Circadian Output Genes
Oishi, K., Miyazaki, K., Kadota, K., Kikuno, R. F., Nagase, T., Atsumi, G.-I., Ohkura, N., Azama, T., Mesaki, M., Yukimasa, S., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304564200 · Cited by 349
Ising, M., Depping, A., Siebertz, A., Lucae, S., Unschuld, P. G., Kloiber, S. M., Horstmann, S., Uhr, M., Müller‐Myhsok, B., & Holsboer, F. (2008) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2008.06332.x · Cited by 320
Squirrel Monkey Immunophilin FKBP51 Is a Potent Inhibitor of Glucocorticoid Receptor Binding1
Denny, W. B., Valentine, D. L., Reynolds, P. D., Smith, D. F., & Scammell, J. G. (2000) · Endocrinology · doi:10.1210/en.141.11.4107 · Cited by 66
Self-citationVermeer, H., Hendriks-Stegeman, B. I., van der Burg, B., van Buul-Offers, S. C., & Jansen, M. (2003) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2002-020354 · Cited by 285
Role of hsp90 and the hsp90-binding immunophilins in signalling protein movement
Pratt, W. B., Galigniana, M. D., Harrell, J. M., & DeFranco, D. B. (2004) · Cellular Signalling · doi:10.1016/j.cellsig.2004.02.004 · Cited by 285
Touma, C., Gassen, N. C., Herrmann, L., Cheung‐Flynn, J., Büll, D., Ionescu, I. A., Heinzmann, J.-M., Knapman, A., Siebertz, A., Depping, A., et al. (2011) · Biological Psychiatry · doi:10.1016/j.biopsych.2011.07.023 · Cited by 280
Effects of social isolation on glucocorticoid regulation in social mammals
Hawkley, L. C., Cole, S. W., Capitanio, J. P., Norman, G. J., & Cacioppo, J. T. (2012) · Hormones and Behavior · doi:10.1016/j.yhbeh.2012.05.011 · Cited by 262
Glucocorticoid and mineralocorticoid receptor mRNA expression in squirrel monkey brain
Patel, P. D., Lopez, J. F., Lyons, D. M., Burke, S., Wallace, M., & Schatzberg, A. F. (2000) · Journal of Psychiatric Research · doi:10.1016/s0022-3956(00)00035-2 · Cited by 252
Sinars, C. R., Cheung-Flynn, J., Rimerman, R. A., Scammell, J. G., Smith, D. F., & Clardy, J. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0231020100 · Cited by 254
Self-citationVersatile TPR domains accommodate different modes of target protein recognition and function
Allan, R. K., & Ratajczak, T. (2010) · Cell Stress and Chaperones · doi:10.1007/s12192-010-0248-0 · Cited by 245
Scammell, J. G., Denny, W. B., Valentine, D. L., & Smith, D. F. (2001) · General and Comparative Endocrinology · doi:10.1006/gcen.2001.7696 · Cited by 238
Self-citationGlucocorticoid receptor physiology
Heitzer, M. D., Wolf, I. M., Sánchez, E. R., Witchel, S. F., & DeFranco, D. B. (2007) · Reviews in Endocrine and Metabolic Disorders · doi:10.1007/s11154-007-9059-8 · Cited by 235
Molecular chaperone interactions with steroid receptors: an update.
Cheung, J., & Smith, D. F. (2000) · Molecular Endocrinology · doi:10.1210/mend.14.7.0489 · Cited by 198
Self-citationIntronic hormone response elements mediate regulation of FKBP5 by progestins and glucocorticoids
Hubler, T. R., & Scammell, J. G. (2004) · Cell Stress & Chaperones · doi:10.1379/csc-32r.1 · Cited by 201
Self-citationUp-regulation of glucocorticoid-regulated genes in a mouse model of Rett syndrome
Nuber, U. A., Kriaučionis, S., Roloff, T. C., Guy, J., Selfridge, J., Steinhoff, C., Schulz, R., Lipkowitz, B., Ropers, H., Holmes, M. C., et al. (2005) · Human Molecular Genetics · doi:10.1093/hmg/ddi229 · Cited by 190
Schiene-Fischer, C., & Yu, C. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)02326-2 · Cited by 190
Davies, T. H., Ning, Y.-M., & Sánchez, E. R. (2005) · Biochemistry · doi:10.1021/bi048503v · Cited by 180
Molecular mechanisms regulating glucocorticoid sensitivity and resistance
Gross, K. L., Lu, N. Z., & Cidlowski, J. A. (2008) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2008.10.001 · Cited by 180
Pirkl, F., & Buchner, J. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.4595 · Cited by 179
Smith, D. F., & Toft, D. O. (2008) · Molecular Endocrinology · doi:10.1210/me.2008-0089 · Cited by 173
Self-citationSteroid up-regulation of FKBP51 and its role in hormone signaling
Jääskeläinen, T., Makkonen, H., & Palvimo, J. J. (2011) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2011.04.006 · Cited by 167
FKBP Ligands—Where We Are and Where to Go?
Kolos, J. M., Voll, A. M., Bauder, M., & Hausch, F. (2018) · Frontiers in Pharmacology · doi:10.3389/fphar.2018.01425 · Cited by 158
Russell, L. C., Whitt, S. R., Chen, M.-S., & Chinkers, M. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.29.20060 · Cited by 165
Wu, B., Li, P., Liu, Y., Lou, Z., Ding, Y., Shu, C., Ye, S., Bartlam, M., Shen, B., & Rao, Z. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0305969101 · Cited by 165
Family-based association of FKBP5 in bipolar disorder
Willour, V. L., Chen, H., Toolan, J., Belmonte, P. L., Cutler, D. J., Goes, F. S., Zandi, P. P., Lee, R. S., MacKinnon, D. F., Mondimore, F. M., et al. (2008) · Molecular Psychiatry · doi:10.1038/sj.mp.4002141 · Cited by 165
Yong, W., Yang, Z., Periyasamy, S., Chen, H., Yucel, S., Li, W., Lin, L. Y., Wolf, I. M., Cohn, M. J., Baskin, L. S., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m609360200 · Cited by 156
Menke, A., Klengel, T., Rubel, J., Brückl, T., Pfister, H., Lucae, S., Uhr, M., Holsboer, F., & Binder, E. B. (2013) · Genes, Brain and Behavior · doi:10.1111/gbb.12026 · Cited by 151
Riggs, D. L., Cox, M. B., Tardif, H. L., Hessling, M., Buchner, J., & Smith, D. F. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.00985-07 · Cited by 150
Self-citationTetratricopeptide repeat cochaperones in steroid receptor complexes
Smith, D. F. (2004) · Cell stress & chaperones (Print) · doi:10.1379/csc-31.1 · Cited by 156
Self-citationRohleder, N., Wolf, J. M., & Wolf, O. T. (2010) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2009.12.003 · Cited by 150
Hsp90 and FKBP51: complex regulators of psychiatric diseases
Criado‐Marrero, M., Rein, T., Binder, E. B., Porter, J. T., Koren, J., & Blair, L. J. (2017) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2016.0532 · Cited by 152
Hubler, T. R., Denny, W. B., Valentine, D. L., Cheung-Flynn, J., Smith, D. F., & Scammell, J. G. (2003) · Endocrinology · doi:10.1210/en.2003-0092 · Cited by 145
Self-citationChen, H., Hewison, M., Hu, B., & Adams, J. S. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1031395100 · Cited by 136
Functional Specificity of Co-Chaperone Interactions with Hsp90 Client Proteins
Riggs, D., Cox, M., Cheung-Flynn, J., Prapapanich, V., Carrigan, P., & Smith, D. F. (2004) · Critical reviews in biochemistry and molecular biology · doi:10.1080/10409230490892513 · Cited by 141
Self-citationHsp90 regulates tau pathology through co-chaperone complexes in Alzheimer's disease
Salminen, A., Ojala, J. O., Kaarniranta, K., Hiltunen, M., & Soininen, H. S. (2010) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2010.10.006 · Cited by 131
FK506-Binding Proteins and Their Diverse Functions
Tong, M., & Jiang, Y. (2015) · Current Molecular Pharmacology · doi:10.2174/1874467208666150519113541 · Cited by 135
Tatro, E. T., Everall, I. P., Kaul, M., & Achim, C. L. (2009) · Brain Research · doi:10.1016/j.brainres.2009.06.036 · Cited by 125
Glucocorticoid receptor activates poised FKBP51 locus through long-distance interactions
Paakinaho, V., Makkonen, H., Jääskeläinen, T., & Palvimo, J. J. (2010) · Molecular Endocrinology · doi:10.1210/me.2009-0443 · Cited by 122
Yang, Z., Wolf, I. M., Chen, H., Periyasamy, S., Chen, Z., Yong, W., Shi, S., Zhao, W., Xu, J., Srivastava, A., et al. (2006) · Molecular Endocrinology · doi:10.1210/me.2006-0024 · Cited by 119
Zhang, X., Clark, A. F., & Yorio, T. (2008) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.07-1279 · Cited by 116
Periyasamy, S., Hinds, T., Shemshedini, L., Shou, W., & Sanchez, E. R. (2010) · Oncogene · doi:10.1038/onc.2009.458 · Cited by 108
“A number of studies have shown contributions of FKBP52, FKBP51 and Cyp40 to protein folding, ligand binding and nuclear localization of glucocorticoid, estrogen and progesterone receptors (Reynolds et al., 1999; Denny et al., 2000; Cheung-Flynn et al., 2003; Ratajczak et al., 2003; Pratt et al., 2004).”
BackgroundYan, H., Frost, P., Shi, Y., Hoang, B. Q., Sharma, S., Fisher, M., Gera, J., & Lichtenstein, A. K. (2006) · Cancer Research · doi:10.1158/0008-5472.can-05-2447 · Cited by 108
Differential Impact of Tetratricopeptide Repeat Proteins on the Steroid Hormone Receptors
Schülke, J.-P., Wochnik, G. M., Lang‐Rollin, I., Gassen, N. C., Knapp, R., Berning, B., Yassouridis, A., & Rein, T. (2010) · PLoS ONE · doi:10.1371/journal.pone.0011717 · Cited by 109
Hennessy, M. B. (2013) · Applied Animal Behaviour Science · doi:10.1016/j.applanim.2013.09.004 · Cited by 108
Cheung-Flynn, J., Roberts, P. J., Riggs, D. L., & Smith, D. F. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m300955200 · Cited by 96
Self-citationThe prospect of FKBP51 as a drug target
Schmidt, M. V., Paez‐Pereda, M., Holsboer, F., & Hausch, F. (2012) · ChemMedChem · doi:10.1002/cmdc.201200137 · Cited by 99
Annett, S., Moore, G., & Robson, T. (2020) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2020.107623 · Cited by 104
Hinds, T. D., Stechschulte, L. A., Cash, H. A., Whisler, D., Banerjee, A. T., Yong, W., Khuder, S. S., Kaw, M., Shou, W., Najjar, S. M., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.311662 · Cited by 96
Biological Actions of the Hsp90-binding Immunophilins FKBP51 and FKBP52
Zgajnar, N. R., Leo, S. A. D., Lotufo, C. M., Erlejman, A. G., Piwien‐Pilipuk, G., & Galigniana, M. D. (2019) · Biomolecules · doi:10.3390/biom9020052 · Cited by 95
FKBP51 – a selective modulator of glucocorticoid and androgen sensitivity
Stechschulte, L. A., & Sanchez, E. R. (2011) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2011.04.012 · Cited by 92
“Using GR as prototype, the inhibitory effect of FKBP51 occurs by mechanisms that include sequestering of receptor to the cytoplasm, and reduction of hormone-binding affinity [19,22 ,23].”
MethodWestberry, J. M., Sadosky, P. W., Hubler, T. R., Gross, K. L., & Scammell, J. G. (2006) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2006.03.004 · Cited by 91
Self-citationFluorescent Probes to Characterise FK506‐Binding Proteins
Kozany, C., März, A., Kress, C., & Hausch, F. (2009) · ChemBioChem · doi:10.1002/cbic.200800806 · Cited by 91
Daikoku, T., Tranguch, S., Friedman, D., Das, S., Smith, D. F., & Dey, S. (2005) · Molecular Endocrinology · doi:10.1210/me.2004-0332 · Cited by 90
Self-citationProlyl isomerases in gene transcription
Hanes, S. D. (2014) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2014.10.028 · Cited by 87
Environmental Stressors and Epigenetic Control of the Hypothalamic-Pituitary-Adrenal Axis
Lee, R. S., & Sawa, A. (2014) · Neuroendocrinology · doi:10.1159/000369585 · Cited by 84
Ramsey, A. J., Russell, L. C., Whitt, S. R., & Chinkers, M. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m001625200 · Cited by 79
Periyasamy, S., Warrier, M., Tillekeratne, M. P. M., Shou, W., & Sanchez, E. R. (2007) · Endocrinology · doi:10.1210/en.2007-0145 · Cited by 78
Glucocorticoids and immune function
Rook, G. A. W. (1999) · Best Practice & Research Clinical Endocrinology & Metabolism · doi:10.1053/beem.1999.0044 · Cited by 78
Glucocorticoid-regulated genes in eosinophilic esophagitis: A role for FKBP51
Caldwell, J. M., Blanchard, C., Collins, M. H., Putnam, P. E., Kaul, A., Aceves, S. S., Bouska, C. A., & Rothenberg, M. E. (2010) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2010.01.038 · Cited by 76
Ward, B. K., Mark, P., Ingram, D., Minchin, R., & Ratajczak, T. (1999) · Breast Cancer Research and Treatment · doi:10.1023/a:1006390804515 · Cited by 74
Kumar, P., Mark, P., Ward, B. K., Minchin, R., & Ratajczak, T. (2001) · Biochemical and Biophysical Research Communications - BBRC · doi:10.1006/bbrc.2001.4952 · Cited by 66
The Hsp110 and Grp170 stress proteins: newly recognized relatives of the Hsp70s
Easton, D. P., Kaneko, Y., & Subjeck, J. R. (2000) · Cell Stress and Chaperones · doi:10.1379/1466-1268(2000)005 · Cited by 328
Cryo-EM reveals how Hsp90 and FKBP immunophilins co-regulate the glucocorticoid receptor
Noddings, C. M., Johnson, J. L., & Agard, D. A. (2023) · Nature Structural & Molecular Biology · doi:10.1038/s41594-023-01128-y · Cited by 75
Banerjee, A., Periyasamy, S., Wolf, I. M., Hinds, T. D., Yong, W., Shou, W., & Sanchez, E. R. (2008) · Biochemistry · doi:10.1021/bi8011862 · Cited by 73
Salivary cortisol as a marker of acute stress in dogs: a review
Chmelíková, E., Bolechová, P., Chaloupková, H., Svobodová, I., Jovičić, M., & Sedmíková, M. (2019) · Domestic Animal Endocrinology · doi:10.1016/j.domaniend.2019.106428 · Cited by 93
Glucocorticoid therapy and ocular hypertension
Dibas, A., & Yorio, T. (2016) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2016.06.018 · Cited by 75
Zhang, X., Clark, A. F., & Yorio, T. (2005) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.05-0571 · Cited by 72
Are there meaningful biomarkers of treatment response for depression?
Breitenstein, B., Scheuer, S., & Holsboer, F. (2014) · Drug Discovery Today · doi:10.1016/j.drudis.2014.02.002 · Cited by 71
Denny, W. B., Prapapanich, V., Smith, D. F., & Scammell, J. (2005) · Endocrinology · doi:10.1210/en.2005-0027 · Cited by 68
Self-citationMechanisms of brain glucocorticoid resistance in stress-induced psychopathologies
Merkulov, V. M., Merkulova, T. I., & Bondar, N. P. (2017) · Biochemistry (Moscow) · doi:10.1134/s0006297917030142 · Cited by 65
Intracellular Vitamin D Binding Proteins: Novel Facilitators of Vitamin D-Directed Transactivation
Wu, S., Ren, S., Chen, H., Chun, R. F., Gacad, M. A., & Adams, J. S. (2000) · Molecular Endocrinology · doi:10.1210/me.14.9.1387 · Cited by 65
The Vitamin D Response Element-binding Protein
Chen, H., Hu, B., Allegretto, E. A., & Adams, J. S. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m007117200 · Cited by 64
FKBP4 is regulated by HOXA10 during decidualization and in endometriosis
Yang, H., Zhou, Y., Edelshain, B., Schatz, F., Lockwood, C. J., & Taylor, H. S. (2012) · Reproduction · doi:10.1530/rep-11-0438 · Cited by 63
Hereditary 1,25-Dihydroxyvitamin D-Resistant Rickets
Malloy, P. J., & Feldman, D. (2003) · KARGER eBooks · doi:10.1159/000072776 · Cited by 62
Cox, M. B., Riggs, D. L., Hessling, M., Schumacher, F., Buchner, J., & Smith, D. F. (2007) · Molecular Endocrinology · doi:10.1210/me.2006-0547 · Cited by 60
Self-citationWard, B. K., Allan, R. K., Mok, D., Temple, S. E. L., Taylor, P., Dornan, J., Mark, P. J., Shaw, D. J., Kumar, P., Walkinshaw, M. D., et al. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m207097200 · Cited by 61
Malekpour, M., Shekouh, D., Safavinia, M. E., Shiralipour, S., Jalouli, M., Mortezanejad, S., Azarpira, N., & Ebrahimi, N. D. (2023) · Frontiers in Psychiatry · doi:10.3389/fpsyt.2023.1182345 · Cited by 71
Approaches for defining the Hsp90-dependent proteome
Hartson, S. D., & Matts, R. L. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2011.08.013 · Cited by 54
Progesterone receptor requires a co-chaperone for signalling in uterine biology and implantation
Tranguch, S. L., Smith, D. F., & Dey, S. K. (2006) · Reproductive BioMedicine Online · doi:10.1016/s1472-6483(10)60655-4 · Cited by 53
Self-citationHunsberger, J. G., Austin, D. R., Chen, G., & Manji, H. K. (2009) · Brain Research · doi:10.1016/j.brainres.2009.06.103 · Cited by 52
Transcriptional signatures of steroid hormones in the striatal neurons and astrocytes
Piechota, M., Korostyński, M., Gołda, S., Ficek, J., Jantas, D., Ziółkowska, B., & Przewłocki, R. (2017) · BMC Neuroscience · doi:10.1186/s12868-017-0352-5 · Cited by 52
Peptidyl-prolyl isomerases: a full cast of critical actors in cardiovascular diseases
Perrucci, G. L., Gowran, A., Zanobini, M., Capogrossi, M. C., Pompilio, G., & Nigro, P. (2015) · Cardiovascular Research · doi:10.1093/cvr/cvv096 · Cited by 50
Chaperones in progesterone receptor complexes
Smith, D. F. (2000) · Seminars in Cell and Developmental Biology · doi:10.1006/scdb.1999.0350 · Cited by 49
Self-citationDean, M. E., & Johnson, J. L. (2020) · Cell Stress and Chaperones · doi:10.1007/s12192-020-01167-0 · Cited by 48
&cestflwr; The Hsp90 family of proteins in Arabidopsis thaliana
Krishna, P., & Gloor, G. B. (2001) · Cell Stress and Chaperones · doi:10.1379/1466-1268(2001)006 · Cited by 360
Loss of FKBP5 Affects Neuron Synaptic Plasticity: An Electrophysiology Insight
Qiu, B., Xu, Y., Wang, J., Liu, M., Dou, L., Deng, R., Wang, C., Williams, K. E., Stewart, R. B., Xie, Z., et al. (2019) · Neuroscience · doi:10.1016/j.neuroscience.2019.01.021 · Cited by 44
Kumar, R., Moche, M., Winblad, B., & Pavlov, P. F. (2017) · Scientific Reports · doi:10.1038/s41598-017-14731-z · Cited by 40
Rees‐Unwin, K. S., Craven, R. A., Davenport, E. L., Hanrahan, S. J., Totty, N. F., Dring, A. M., Banks, R. E., Morgan, G. J., & Davies, F. E. (2007) · British Journal of Haematology · doi:10.1111/j.1365-2141.2007.06837.x · Cited by 43
Regulation of the Atrial Natriuretic Peptide Receptor by Heat Shock Protein 90 Complexes
Kumar, R., Grammatikakis, N., & Chinkers, M. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010480200 · Cited by 42
Su, S., Blackwelder, A. J., Grossman, G., Minges, J. T., Yuan, L., Young, S. L., & Wilson, E. M. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.372797 · Cited by 40
Calcium‐ and FK506‐independent interaction between the immunophilin FKBP51 and calcineurin*
Li, T., Baksh, S., Cristillo, A. D., & Bierer, B. E. (2002) · Journal of Cellular Biochemistry · doi:10.1002/jcb.10026 · Cited by 40
The Mechanisms Underlying Autonomous Adrenocorticotropic Hormone Secretion in Cushing’s Disease
Fukuoka, H., Shichi, H., Yamamoto, M., & Takahashi, Y. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21239132 · Cited by 40
Wolf, I. M., Periyasamy, S., Hinds, T., Yong, W., Shou, W., & Sanchez, E. R. (2009) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2008.11.006 · Cited by 38
Metadata
- Authors
- Reynolds, P. D., Ruan, Y., Smith, D. F., & Scammell, J. G.
- Affiliations
- University of South Alabama (US)
- University of Nebraska Medical Center (US)
- Corresponding author
- Scammell, J. G.
- Venue
- The Journal of Clinical Endocrinology & Metabolism
- Publisher
- The Endocrine Society
- Published
- 1999-02
- Volume
- 84
- Issue
- 2
- Pages
- 663-669
- ISSN
- 0021-972X (ISSN-L)
- 1945-7197
- OpenAlex
- W1978913374
- Cited by
- 184
- References
- 43
- Citations by year
- 2026: 1 · 2023: 5 · 2022: 2 · 2021: 2 · 2020: 8 · 2019: 5 · 2018: 2 · 2017: 7 · 2016: 7 · 2015: 6 · 2014: 6 · 2013: 7 · 2012: 11
- FWCI
- 4.95
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- The Journal of Clinical Endocrinology & Metabolism (publishedVersion)
- PubMed (publishedVersion)
- Funders
- U.S. Public Health Service (01254, 13200)
- National Institute of Diabetes and Digestive and Kidney Diseases (DK-48218, R01DK048218)
- National Center for Research Resources (P40RR001254, R24RR013200)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Endocrinology › Estrogen and related hormone effects
- Life Sciences › Neuroscience › Behavioral Neuroscience › Stress Responses and Cortisol
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Signaling Pathways in Disease
- Keywords
- glucocorticoid resistance, squirrel monkey, FKBP51, FKBP52, immunophilins, glucocorticoid receptor, receptor binding affinity, HSP90, lymphocytes, Neotropical primates, cortisol, FK506
- MeSH terms
- Animals, Cytosol, Drug Resistance, Glucocorticoids, Humans, Immunosuppressive Agents, Lymphocytes, Receptors, Glucocorticoid, Saimiri, Gene Expression, Tacrolimus, HSP90 Heat-Shock Proteins, Immunophilins, 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