The DOI matches its Crossref record; 28 of the 28 references it cites were found in a registry or an index.
Cochaperone immunophilin FKBP52 is critical to uterine receptivity for embryo implantation
Open accessAbstract
Embryo implantation in the uterus is a critical step in mammalian reproduction, requiring preparation of the uterus receptive to blastocyst implantation. Uterine receptivity, also known as the window of implantation, lasts for a limited period, and it is during this period blastocysts normally implant. Ovarian steroid hormones estrogen and progesterone (P(4)) are the primary regulators of this process. The immunophilin FKBP52 serves as a cochaperone for steroid hormone nuclear receptors to govern appropriate hormone action in target tissues. Here we show a critical role for FKBP52 in mouse implantation. This immunophilin has unique spatiotemporal expression in the uterus during implantation, and females missing the Fkbp52 gene have complete implantation failure due to lack of attainment of uterine receptivity. The overlapping uterine expression of FKBP52 with nuclear progesterone receptor (PR) in wild-type mice together with reduced P(4) binding to PR, attenuated PR transcriptional activity and down-regulation of several P(4)-regulated genes in uteri of Fkbp52(-/-) mice, establishes this cochaperone as a critical regulator of uterine P(4) function. Interestingly, ovulation, another P(4)-mediated event, remains normal. Collectively, the present investigation provides evidence for an in vivo role for this cochaperone in regulating tissue-specific hormone action and its critical role in uterine receptivity for implantation.
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
“While FKBP52 is known to functionally interact with AR, GR and PR [6–8], β-catenin only interacts strongly with AR, but not GR and PR [20].”
From The FKBP52 Cochaperone Acts in Synergy with β-Catenin to Potentiate Androgen Receptor Signaling (2015) · cites this paper as [8]
In the citing paper
“FKBP52 is a positive regulator of glucocorticoid receptor (GR) [5], progesterone receptor (PR) [6], and androgen receptor (AR) [7], but not estrogen receptor (ER) or mineralocorticoid receptor (MR) [5].”
From FKBP51 and FKBP52 in signaling and disease (2011) · cites this paper as [6]
In the citing paper
“Given the androgen, progesterone and glucocorticoid insensitivity phenotypes observed in the fkbp52-deficient mice [6, 7, 32, 35, 51], FKBP52 is likely to have an important role and to serve as a therapeutic target in a variety of diseases that are dependent on these hormone signaling pathways.”
From FKBP51 and FKBP52 in signaling and disease (2011) · cites this paper as [6]
In the citing paper
“The infertility is the result of embryonic implantation and decidualization failure due to progesterone insensitivity and uterine defects [6, 34, 35].”
From FKBP51 and FKBP52 in signaling and disease (2011) · cites this paper as [6]
In the citing paper
“Recently, Tranguch et al. (29) made mice deficient in FKBP52 and showed that this protein plays an essential role in PR-mediated uterine receptivity to implantation, but they were not able to discriminate between PR-A and PR-B actions.”
From FK506-binding protein 52 is essential to uterine reproductive physiology controlled by the progesterone receptor A isoform (2006) · cites this paper as [29]
In the citing paper
“Recently, Tranguch et al. (29) made mice deficient in FKBP52 and showed that this protein plays an essential role in PR-mediated uterine receptivity to implantation, but they were not able to discriminate between PR-A and PR-B actions.”
From FK506-binding protein 52 is essential to uterine reproductive physiology controlled by the progesterone receptor A isoform (2006) · cites this paper as [29]
Citations
Cites
Todaro, G. J., & Green, H. (1963) · The Journal of Cell Biology · doi:10.1083/jcb.17.2.299 · Cited by 2,747
Mice lacking progesterone receptor exhibit pleiotropic reproductive abnormalities.Preprint
Lydon, J. P., DeMayo, F. J., Funk, C. R., Mani, S. K., Hughes, A. R., Montgomery, C. A., Shyamala, G., Conneely, O. M., & O’Malley, B. W. (1995) · Genes & Development · doi:10.1101/gad.9.18.2266 · Cited by 1,862
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 Cues to Implantation
Dey, S. K., Lim, H. J., Das, S. K., Reese, J., Paria, B. C., Daikoku, T., & Wang, H. (2004) · Endocrine Reviews · doi:10.1210/er.2003-0020 · Cited by 1,120
Self-citationSubgroup of reproductive functions of progesterone mediated by progesterone receptor-B isoform
Mulac-Jericevic, B., Mullinax, R. A., DeMayo, F. J., Lydon, J. P., & Conneely, O. M. (2000) · Science · doi:10.1126/science.289.5485.1751 · Cited by 704
LPA3-mediated lysophosphatidic acid signalling in embryo implantation and spacing
Ye, X., Hama, K., Contos, J. J. A., Anliker, B., Inoue, A., Skinner, M. K., Suzuki, H., Amano, T., Kennedy, G., Arai, H., et al. (2005) · Nature · doi:10.1038/nature03505 · Cited by 567
Das, S., Wang, X., Paria, B. C., Damm, D. L., Abraham, J. A., Klagsbrun, M., Andrews, G. K., & Dey, S. K. (1994) · Development · doi:10.1242/dev.120.5.1071 · Cited by 563
Self-citationDefective mammary gland morphogenesis in mice lacking the progesterone receptor B isoform
Mulac‐Jeričević, B., Lydon, J. P., DeMayo, F. J., & Conneely, O. M. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1732707100 · Cited by 542
Deciphering the Cross-Talk of Implantation: Advances and Challenges
Paria, B. C., Reese, J., Das, S. K., & Dey, S. K. (2002) · Science · doi:10.1126/science.1071601 · Cited by 486
Self-citationLim, H. J., Ma, L., Ma, W., Maas, R. L., & Dey, S. K. (1999) · Molecular Endocrinology · doi:10.1210/mend.13.6.0284 · Cited by 327
Self-citation
Research works printed but not linked: 4
- Song, H., Lim, H., Paria, B. C., Matsumoto, H., Swift, L. L., Morrow, J., Bonventre, J. V. & Dey, S. K. (2002) Development (Cambridge, U.K.) 129, 2879-2889.
- Das, S. K., Wang, X. N., Paria, B. C., Damm, D., Abraham, J. A., Klagsbrun, M., Andrews, G. K. & Dey, S. K. (1994) Development (Cambridge, U.K.) 120, 1071-1083.
- Das, S. K., Chakraborty, I., Paria, B. C., Wang, X. N., Plowman, G. & Dey, S. K. (1995) Mol. Endocrinol. 9, 691-705.8592515
- McMaster, M. T., Teng, C. T., Dey, S. K. & Andrews, G. K. (1992) Mol. Endocrinol. 6, 101-111.1738363
Cited by
Sorted by citations
Mechanisms of implantation: strategies for successful pregnancy
Cha, J., Sun, X., & Dey, S. K. (2012) · Nature Medicine · doi:10.1038/nm.3012 · Cited by 1,391
Self-citationRoadmap to embryo implantation: clues from mouse models
Wang, H., & Dey, S. K. (2006) · Nature Reviews Genetics · doi:10.1038/nrg1808 · Cited by 1,324
Self-citationCyclic Decidualization of the Human Endometrium in Reproductive Health and Failure
Gellersen, B., & Brosens, J. J. (2014) · Endocrine Reviews · doi:10.1210/er.2014-1045 · Cited by 1,176
The Aryl Hydrocarbon Receptor Complex and the Control of Gene Expression
Beischlag, T. V., Morales, J. L., Hollingshead, B. D., & Perdew, G. H. (2008) · Critical Reviews™ in Eukaryotic Gene Expression · doi:10.1615/critreveukargeneexpr.v18.i3.20 · Cited by 727
Physiological and molecular determinants of embryo implantation
Zhang, S., Lin, H., Kong, S., Wang, S., Wang, H., Wang, H., & Armant, D. R. (2013) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2012.12.011 · Cited by 598
Self-citationEndometrial Decidualization: Of Mice and Men
Ramathal, C. Y., Bagchi, I. C., Taylor, R. N., & Bagchi, M. K. (2010) · Seminars in Reproductive Medicine · doi:10.1055/s-0029-1242989 · Cited by 519
Progesterone and Estrogen Signaling in the Endometrium: What Goes Wrong in Endometriosis?
Marquardt, R. M., Kim, T. H., Shin, J., & Jeong, J. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20153822 · Cited by 527
Bmp2 Is Critical for the Murine Uterine Decidual Response
Lee, K. Y., Jeong, J., Wang, J., Ma, L., Martin, J. F., Tsai, S. Y., Lydon, J. P., & DeMayo, F. J. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.00342-07 · Cited by 352
Accelerated neurodegeneration through chaperone-mediated oligomerization of tau
Blair, L. J., Nordhues, B. A., Hill, S. E., Scaglione, K. M., O’Leary, J. C., Fontaine, S. N., Breydo, L., Zhang, B., Li, P., Wang, L., et al. (2013) · Journal of Clinical Investigation · doi:10.1172/jci69003 · Cited by 322
Wetendorf, M., & DeMayo, F. J. (2011) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2011.10.028 · Cited by 284
Franco, H. L., Dai, D., Lee, K. Y., Rubel, C. A., Roop, D. R., Boerboom, D., Jeong, J., Lydon, J. P., Bagchi, I. C., Bagchi, M. K., et al. (2010) · The FASEB Journal · doi:10.1096/fj.10-175349 · Cited by 273
FKBP51 and FKBP52 in signaling and disease
Storer, C. L., Dickey, C. A., Galigniana, M. D., Rein, T., & Cox, M. B. (2011) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2011.08.001 · Cited by 266
“Given the androgen, progesterone and glucocorticoid insensitivity phenotypes observed in fkbp52 -deficient mice [6,7,31,34,50], FKBP52 is likely to have an important role and to serve as a therapeutic target in a variety of diseases that are dependent on these hormone signaling pathways.”
Self-citationSelective inhibitors of the FK506-binding protein 51 by induced fit
Gaali, S., Kirschner, A., Cuboni, S., Hartmann, J., Kozany, C., Balsevich, G., Namendorf, C., Fernandez-Vizarra, P., Sippel, C., Zannas, A. S., et al. (2015) · Nature Chemical Biology · doi:10.1038/nchembio.1699 · Cited by 245
Versatile 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
Genomic and epigenomic mechanisms of glucocorticoids in the brain
Gray, J. D., Kogan, J. F., Marrocco, J., & McEwen, B. S. (2017) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2017.97 · Cited by 242
Molecular chaperones, essential partners of steroid hormone receptors for activity and mobility
Echeverría, P. C., & Picard, D. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2009.11.012 · Cited by 225
Hartmann, J., Wagner, K. V., Liebl, C., Scharf, S. H., Wang, X.-D., Wolf, M., Hausch, F., Rein, T., Schmidt, U., Touma, C., et al. (2012) · Neuropharmacology · doi:10.1016/j.neuropharm.2011.07.041 · Cited by 224
Self-citationImmunophilins: for the love of proteins
Barik, S. (2006) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-006-6215-3 · Cited by 218
Progesterone Actions and Resistance in Gynecological Disorders
MacLean, J. A., & Hayashi, K. (2022) · Cells · doi:10.3390/cells11040647 · Cited by 199
Chaperoning steroid hormone action
Picard, D. (2006) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2006.06.003 · Cited by 190
Young, S. L. (2013) · Reproductive BioMedicine Online · doi:10.1016/j.rbmo.2013.06.010 · Cited by 177
Smith, D. F., & Toft, D. O. (2008) · Molecular Endocrinology · doi:10.1210/me.2008-0089 · Cited by 173
Self-citationSavaris, R. F., Groll, J. M., Young, S. L., DeMayo, F. J., Jeong, J.-W., Hamilton, A. E., Giudice, L. C., & Lessey, B. A. (2011) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2010-2600 · Cited by 162
Large, M. J., & DeMayo, F. J. (2011) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2011.07.027 · Cited by 161
Allan, R. K., Mok, D., Ward, B. K., & Ratajczak, T. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m512406200 · Cited by 160
Stress-induced sex differences: Adaptations mediated by the glucocorticoid receptor
Bourke, C. H., Harrell, C. S., & Neigh, G. N. (2012) · Hormones and Behavior · doi:10.1016/j.yhbeh.2012.02.024 · Cited by 166
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-citationProgesterone Resistance in Endometriosis: Current Evidence and Putative Mechanisms
Zhang, P., & Wang, G. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24086992 · Cited by 138
Stress-responsive FKBP51 regulates AKT2-AS160 signaling and metabolic function
Balsevich, G., Häusl, A. S., Meyer, C. W., Karamihalev, S., Feng, X., Pöhlmann, M. L., Dournes, C., Uribe-Marino, A., Santarelli, S., Labermaier, C., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-01783-y · Cited by 134
De Leon, J. T., Iwai, A., Feau, C., Garcia, Y., Balsiger, H. A., Storer, C. L., Suro, R. M., Garza, K. M., Lee, S., Sang Kim, Y., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1105160108 · Cited by 132
Self-citationFK506-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
Uterine disorders and pregnancy complications: insights from mouse models
Lim, H. J., & Wang, H. (2010) · Journal of Clinical Investigation · doi:10.1172/jci41210 · Cited by 126
Self-citationA New Anti-Depressive Strategy for the Elderly: Ablation of FKBP5/FKBP51
O’Leary, J. C., Dharia, S. P., Blair, L. J., Brady, S., Johnson, A. G., Peters, M. M., Cheung‐Flynn, J., Cox, M. B., de Erausquin, G. A., Weeber, E. J., et al. (2011) · PLoS ONE · doi:10.1371/journal.pone.0024840 · Cited by 128
Self-citationTranguch, S., Wang, H., Daikoku, T., Xie, H., Smith, D. F., & Dey, S. K. (2007) · Journal of Clinical Investigation · doi:10.1172/jci31622 · Cited by 121
Self-citationYang, 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
“These observations are consistent with recent work from Dey’s group (29) describing an independent FKBP52 KO strain.”
Fukui, Y., Hirota, Y., Matsuo, M., Gebril, M., Akaeda, S., Hiraoka, T., & Osuga, Y. (2019) · Reproductive Medicine and Biology · doi:10.1002/rmb2.12280 · Cited by 119
Mukherjee, A., Soyal, S. M., Fernandez‐Valdivia, R., Géhin, M., Chambon, P., DeMayo, F. J., Lydon, J. P., & O’Malley, B. W. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.00654-06 · Cited by 115
In vivo analysis of progesterone receptor action in the uterus during embryo implantation
Franco, H. L., Jeong, J., Tsai, S. Y., Lydon, J. P., & DeMayo, F. J. (2008) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2007.12.001 · Cited by 109
Periyasamy, S., Hinds, T., Shemshedini, L., Shou, W., & Sanchez, E. R. (2010) · Oncogene · doi:10.1038/onc.2009.458 · Cited by 108
“Yet, it is clear that the PPIase domain (rather than catalytic activity) is critical to FKBP52 actions on GR and PR (Riggs et al., 2003; Tranguch et al., 2005; Wochnik et al., 2005).”
Martinez, G. J., Appleton, M., Kipp, Z. A., Loria, A. S., Min, B., & Hinds, T. D. (2023) · Physiological Reviews · doi:10.1152/physrev.00021.2023 · Cited by 115
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
Yoshinaga, K. (2007) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2007.10.006 · Cited by 104
Multidomain Peptidyl Prolyl cis/trans Isomerases
Schiene‐Fischer, C. (2014) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2014.11.012 · Cited by 103
Progesterone receptor signaling in the initiation of pregnancy and preservation of a healthy uterus
Wetendorf, M., & DeMayo, F. J. (2014) · The International Journal of Developmental Biology · doi:10.1387/ijdb.140069mw · Cited by 101
Progesterone Function in Human Endometrium: Clinical Perspectives
Young, S. L., & Lessey, B. A. (2010) · Seminars in Reproductive Medicine · doi:10.1055/s-0029-1242988 · Cited by 105
The 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
NF-κB Transcriptional Activity Is Modulated by FK506-binding Proteins FKBP51 and FKBP52
Erlejman, A. G., Leo, S. A. D., Mazaira, G. I., Molinari, A. M., Camisay, M. F., Fontana, V. A., Cox, M. B., Piwien‐Pilipuk, G., & Galigniana, M. D. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.582882 · Cited by 98
Self-citationDeMayo, F. J., & Lydon, J. P. (2020) · Journal of Molecular Endocrinology · doi:10.1530/jme-19-0212 · Cited by 99
Chaperoning steroidal physiology: Lessons from mouse genetic models of Hsp90 and its cochaperones
Sánchez, E. R. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2011.11.006 · Cited by 98
Unraveling the Dynamics of Estrogen and Progesterone Signaling in the Endometrium: An Overview
Silva, I. D. D., Wuidar, V., Zielonka, M., & Péqueux, C. (2024) · Cells · doi:10.3390/cells13151236 · Cited by 99
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
“Indeed, several investigations using FKBP52-deficient mice have shown that FKBP52 is essential for progesterone receptor action in uterine implantation [29,30], for androgen receptor regulation of penile and prostate gland development”
Fluorescent Probes to Characterise FK506‐Binding Proteins
Kozany, C., März, A., Kress, C., & Hausch, F. (2009) · ChemBioChem · doi:10.1002/cbic.200800806 · Cited by 91
Zhang, S., Kong, S., Wang, B. J., Cheng, X., Chen, Y., Wu, W., Wang, Q., Shi, J., Zhang, Y., Wang, S., et al. (2014) · Cell Research · doi:10.1038/cr.2014.82 · Cited by 91
Self-citationRegional development of uterine decidualization: Molecular signaling by Hoxa‐10
Das, S. (2009) · Molecular Reproduction and Development · doi:10.1002/mrd.21133 · Cited by 91
Self-citationThe Hsp90 Cochaperone p23 Is Essential for Perinatal Survival
Grad, I., McKee, T., Ludwig, S. M., Hoyle, G. W., Ruíz, P., Wurst, W., Floß, T., Miller, C. A., & Picard, D. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.00734-06 · Cited by 93
Joshi, N. R., Miyadahira, E. H., Afshar, Y., Jeong, J.-W., Young, S. L., Lessey, B. A., Serafini, P. C., & Fazleabas, A. T. (2016) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2016-2076 · Cited by 87
FKBP51 Null Mice Are Resistant to Diet-Induced Obesity and the PPARγ Agonist Rosiglitazone
Stechschulte, L. A., Qiu, B., Warrier, M., Hinds, T. D., Zhang, M., Gu, H., Xu, Y., Khuder, S. S., Russo, L., Najjar, S. M., et al. (2016) · Endocrinology · doi:10.1210/en.2015-1996 · Cited by 89
The immunophilin FKBP52 specifically binds to tubulin and prevents microtubule formation
Chambraud, B., Belabes, H., Fontaine‐Lenoir, V., Fellous, A., & Baulieu, E. E. (2007) · The FASEB Journal · doi:10.1096/fj.06-7667com · Cited by 85
The non-human primate model of endometriosis: research and implications for fecundity
Braundmeier, A. G., & Fazleabas, A. T. (2009) · Molecular Human Reproduction · doi:10.1093/molehr/gap057 · Cited by 85
Lee, K. Y., Jeong, J., Tsai, S. Y., Lydon, J. P., & DeMayo, F. J. (2007) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2007.06.002 · Cited by 84
Combinatory approaches prevent preterm birth profoundly exacerbated by gene-environment interactions
Cha, J., Bartos, A., Egashira, M., Haraguchi, H., Saito‐Fujita, T., Leishman, E., Bradshaw, H. B., Dey, S. K., & Hirota, Y. (2013) · Journal of Clinical Investigation · doi:10.1172/jci70098 · Cited by 84
Self-citationRegulation of steroid hormone receptor function by the 52-kDa FK506-binding protein (FKBP52)
Sivils, J. C., Storer, C. L., Galigniana, M. D., & Cox, M. B. (2011) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2011.03.010 · Cited by 81
Self-citationYu, Y., Zhao, Z., Shi, Y., Tian, H., Liu, L., Bian, X., Xu, Y., Zheng, X., Gan, L., Shen, Y., et al. (2016) · Genetics · doi:10.1534/genetics.115.183848 · Cited by 80
Imbalances in the Hsp90 Chaperone Machinery: Implications for Tauopathies
Shelton, L. B., Koren, J., & Blair, L. J. (2017) · Frontiers in Neuroscience · doi:10.3389/fnins.2017.00724 · Cited by 80
Jackson, K. S., Brudney, A., Hastings, J. M., Mavrogianis, P. A., Kim, J. J., & Fazleabas, A. T. (2007) · Reproductive Sciences · doi:10.1177/1933719106298409 · Cited by 77
ARID1A Is Essential for Endometrial Function during Early Pregnancy
Kim, T. H., Yoo, J., Wang, Z., Lydon, J. P., Khatri, S., Hawkins, S. M., Leach, R. E., Fazleabas, A. T., Young, S. L., Lessey, B. A., et al. (2015) · PLoS Genetics · doi:10.1371/journal.pgen.1005537 · Cited by 79
Daikoku, T., Tranguch, S. L., Trofimova, I. N., Dinulescu, D. M., Jacks, T., Nikitin, A. Y., Connolly, D. C., & Dey, S. K. (2006) · Cancer Research · doi:10.1158/0008-5472.can-05-4063 · Cited by 76
Self-citationGaligniana, N. M., Ballmer, L. T., Toneatto, J., Erlejman, A. G., Lagadari, M., & Galigniana, M. D. (2012) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2012.07775.x · Cited by 76
Kruppel-like factor 5 (KLF5) is critical for conferring uterine receptivity to implantation
Sun, X., Zhang, L., Xie, H., Wan, H., Magella, B., Whitsett, J. A., & Dey, S. K. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1118411109 · Cited by 75
Self-citationFKBP51 and the molecular chaperoning of metabolism
Smedlund, K., Sánchez, E. R., & Hinds, T. D. (2021) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2021.08.003 · Cited by 75
Diverse structures, functions and uses of FK506 binding proteins
Bonner, J. M., & Boulianne, G. L. (2017) · Cellular Signalling · doi:10.1016/j.cellsig.2017.06.013 · Cited by 78
GCUNC-45 Is a Novel Regulator for the Progesterone Receptor/hsp90 Chaperoning Pathway
Chadli, A., Graham, J. D., Abel, M. G., Jackson, T. A., Gordon, D. F., Wood, W. M., Felts, S. J., Horwitz, K. B., & Toft, D. O. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.5.1722-1730.2006 · Cited by 68
Progesterone governs endometrial proliferation-differentiation switching and blastocyst implantation
Hirota, Y. (2019) · Endocrine Journal · doi:10.1507/endocrj.ej18-0431 · Cited by 67
FKBP family proteins as promising new biomarkers for cancer
Solassol, J., Mangé, A., & Maudelondé, T. (2011) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2011.03.012 · Cited by 67
Deficiency of Immunophilin FKBP52 Promotes Endometriosis
Hirota, Y., Tranguch, S., Daikoku, T., Hasegawa, A., Osuga, Y., Taketani, Y., & Dey, S. K. (2008) · The American Journal of Pathology · doi:10.2353/ajpath.2008.080527 · Cited by 67
Self-citationUterine receptivity and embryo–uterine interactions in embryo implantation: lessons from mice
Egashira, M., & Hirota, Y. (2013) · Reproductive Medicine and Biology · doi:10.1007/s12522-013-0153-1 · Cited by 66
Haraguchi, H., Saito‐Fujita, T., Hirota, Y., Egashira, M., Matsumoto, L., Matsuo, M., Hiraoka, T., Koga, K., Yamauchi, N., Fukayama, M., et al. (2014) · Molecular Endocrinology · doi:10.1210/me.2014-1097 · Cited by 66
Self-citationFKBP4 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
Wan, S., Sun, Y., Zong, J., Meng, W., Yan, J., Chen, K., Wang, S., Guo, D., Xiao, Z., Zhou, Q., et al. (2023) · Cell Death and Disease · doi:10.1038/s41419-023-05866-1 · Cited by 63
FKBP51 inhibits GSK3β and augments the effects of distinct psychotropic medications
Gassen, N. C., Hartmann, J., Zannas, A. S., Kretzschmar, A., Zschocke, J., Maccarrone, G., Hafner, K., Zellner, A., Kollmannsberger, L. K., Wagner, K. V., et al. (2016) · Molecular Psychiatry · doi:10.1038/mp.2015.38 · Cited by 62
Structural characterization of the PPIase domain of FKBP51, a cochaperone of human Hsp90
Bracher, A., Kozany, C., Thost, A.-K., & Hausch, F. (2011) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444911013862 · Cited by 62
Hirota, Y., Acar, N., Tranguch, S., Burnum, K. E., Xie, H., Kodama, A., Osuga, Y., Ustunel, I., Friedman, D. B., Caprioli, R. M., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1009324107 · Cited by 62
Self-citationMolecular mechanisms involved in progesterone receptor regulation of uterine function
Lee, K., Jeong, J., Tsai, M., Tsai, S. Y., Lydon, J. P., & DeMayo, F. J. (2006) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2006.09.006 · Cited by 61
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-citationStructure, Function, and Evaluation of the Female Reproductive Tract
Lessey, B. A., & Young, S. L. (2019) · Elsevier eBooks · doi:10.1016/b978-0-323-47912-7.00009-3 · Cited by 60
Warrier, M., Hinds, T. D., Ledford, K. J., Cash, H. A., Patel, P. R., Bowman, T. A., Stechschulte, L. A., Yong, W., Shou, W., Najjar, S. M., et al. (2010) · Endocrinology · doi:10.1210/en.2009-1158 · Cited by 57
Xin, Q., Kong, S., Yan, J., Qiu, J., He, B., Zhou, C., Ni, Z., Bao, H., Huang, L., Lu, J., et al. (2017) · Journal of Clinical Investigation · doi:10.1172/jci92862 · Cited by 60
Self-citationDeciphering the molecular basis of uterine receptivity
Zhang, S., Kong, S., Lu, J., Wang, Q., Chen, Y., Wang, W., Wang, B. J., & Wang, H. (2012) · Molecular Reproduction and Development · doi:10.1002/mrd.22118 · Cited by 57
Self-citationSmits, K., Willems, S., Steendam, K. V., Velde, M. V. D., Lange, V. D., Ververs, C., Roels, K., Govaere, J., Nieuwerburgh, F. V., Peelman, L. J., et al. (2018) · Scientific Reports · doi:10.1038/s41598-018-23537-6 · Cited by 58
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-citationNamiki, T., Ito, J., & Kashiwazaki, N. (2018) · Reproductive Medicine and Biology · doi:10.1002/rmb2.12103 · Cited by 52
Aikawa, S., Deng, W., Liang, X., Yuan, J., Bartos, A., Sun, X., & Dey, S. K. (2019) · Cell Death and Differentiation · doi:10.1038/s41418-019-0429-z · Cited by 52
Self-citationHaller, M., Yin, Y., & Ma, L. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1907652116 · Cited by 52
Structure‐based classification of 45 FK506‐binding proteins
Somarelli, J. A., Lee, S. Y., Skolnick, J., & Herrera, R. J. (2008) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.21908 · Cited by 51
Öztürk, S., & Demir, R. (2010) · PubMed · doi:10.14670/hh-25.1215 · Cited by 50
Epigenetic Changes Through DNA Methylation Contribute to Uterine Stromal Cell Decidualization
Gao, F., Ma, X., Rusie, A., Hemingway, J., Ostmann, A. B., Chung, D., & Das, S. (2012) · Endocrinology · doi:10.1210/en.2012-1457 · Cited by 49
Self-citationAlbu, S., Romanowski, C. P. N., Curzi, M. L., Jakubcakova, V., Flachskamm, C., Gassen, N. C., Hartmann, J., Schmidt, M. V., Schmidt, U., Rein, T., et al. (2013) · Journal of Sleep Research · doi:10.1111/jsr.12112 · Cited by 50
Sabbagh, J. J., Cordova, R. A., Zheng, D., Criado-Marrero, M., Lemus, A., Li, P., Baker, J. D., Nordhues, B. A., Darling, A. L., Martinez-Licha, C., et al. (2018) · ACS Chemical Biology · doi:10.1021/acschembio.8b00454 · Cited by 48
Gałat, A. (2012) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-012-1206-z · Cited by 48
Metadata
- Authors
- Tranguch, S., Cheung-Flynn, J., Daikoku, T., Prapapanich, V., Cox, M. B., Xie, H., Wang, H., Das, S. K., Smith, D. F., & Dey, S. K.
- Affiliations
- Mayo Clinic in Arizona (US)
- Departments of Pediatrics, Cell and Developmental Biology, Cancer Biology, and Pharmacology, Vanderbilt University Medical Center, Nashville, TN 37232; and Department of Biochemistry and Molecular Biology, Mayo Clinic, Scottsdale, AZ 85259
- ORCID
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2005-09-21
- Volume
- 102
- Issue
- 40
- Pages
- 14326-14331
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC1242310
- OpenAlex
- W1567400069
- Cited by
- 232
- References
- 28
- Citations by year
- 2026: 6 · 2025: 1 · 2024: 2 · 2023: 9 · 2022: 11 · 2021: 7 · 2020: 10 · 2019: 13 · 2018: 7 · 2017: 12 · 2016: 6 · 2015: 13 · 2014: 23 · 2013: 12 · 2012: 17
- FWCI
- 5.08
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of Diabetes and Digestive and Kidney Diseases (5T32 DK07563, F32DK068983)
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › Reproductive System and Pregnancy
- Health Sciences › Medicine › Reproductive Medicine › Reproductive Biology and Fertility
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Endocrinology › Estrogen and related hormone effects
- Keywords
- FKBP52, immunophilins, endometrial receptivity, embryo implantation, progesterone receptor, progesterone signaling, co-chaperones, implantation failure
- MeSH terms
- Animals, Female, Histological Techniques, Mice, Inbred C57BL, Embryo Implantation, Progesterone, Receptors, Progesterone, Uterus, Blotting, Southern, Blotting, Northern, Down-Regulation, In Situ Hybridization, Mice, Knockout, Molecular Chaperones, Reverse Transcriptase Polymerase Chain Reaction, Tacrolimus Binding Proteins, Mice
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
