The DOI matches its Crossref record; 20 of the 20 references it cites were found in a registry or an index.
Molecular chaperones, essential partners of steroid hormone receptors for activity and mobility
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Citations
Cites
High-Quality Binary Protein Interaction Map of the Yeast Interactome Network
Yu, H., Braun, P., Yıldırım, M. A., Lemmens, I., Venkatesan, K., Sahalie, J., Hirozane-Kishikawa, T., Gebreab, F., Li, N., Simonis, N., et al. (2008) · Science · doi:10.1126/science.1158684 · Cited by 1,392
Structure of TPR Domain–Peptide Complexes
Scheufler, C., Brinker, A., Bourenkov, G., Pegoraro, S., Moroder, L., Bartunik, H., Hartl, F. U., & Moarefi, I. (2000) · Cell · doi:10.1016/s0092-8674(00)80830-2 · Cited by 1,188
The glucocorticoid receptor: rapid exchange with regulatory sites in living cells
McNally, J. G., Müller, W. G., Walker, D., Wolford, R., & Hager, G. L. (2000) · Science · doi:10.1126/science.287.5456.1262 · Cited by 802 · cited 3×
“Fluorescence recovery after photobleaching (FRAP) studies have shown that several nuclear proteins including SHRs are highly mobile [83,84].”
BackgroundA New First Step in Activation of Steroid Receptors
Davies, T. H., Ning, Y.-M., & Sánchez, E. R. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.c100531200 · Cited by 427
Disassembly of Transcriptional Regulatory Complexes by Molecular Chaperones
Freeman, B. C., & Yamamoto, K. R. (2002) · Science · doi:10.1126/science.1073051 · Cited by 400
Ultradian hormone stimulation induces glucocorticoid receptor-mediated pulses of gene transcription
Stavreva, D. A., Wiench, M., John, S., Conway-Campbell, B. L., McKenna, M. A., Pooley, J. R., Johnson, T. A., Voss, T. C., Lightman, S. L., & Hager, G. L. (2009) · Nature Cell Biology · doi:10.1038/ncb1922 · Cited by 375 · cited 1×
“In a very recent paper, Hager and colleagues [96] demonstrated that the pulsatile release of glucocorticoids is accompanied by a pulsed expression of GR-regulated genes.”
BackgroundThe 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 · cited 1×
“receptor function [39] are Hsp90-dependent.”
Self-citationCochaperone immunophilin FKBP52 is critical to uterine receptivity for embryo implantation
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. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0505775102 · Cited by 232
Vicent, G. P., Ballaré, C., Nacht, A. S., Clausell, J., Subtil-Rodríguez, A., Quiles, I., Jordan, A., & Beato, M. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.10.011 · Cited by 223
Physiological role for the cochaperone FKBP52 in androgen receptor signaling
Cheung-Flynn, J., Prapapanich, V., Cox, M. B., Riggs, D. L., Suarez-Quian, C., & Smith, D. F. (2005) · Molecular Endocrinology · doi:10.1210/me.2005-0071 · Cited by 212
Cited by
Yang (2021) · doi:10.1038/s41598-020-79139-8 · Cited by 5,035
Molecular mechanism of estrogen–estrogen receptor signaling
Yaşar, P., Ayaz, G., User, S. D., Güpür, G., & Muyan, M. (2017) · Reproductive Medicine and Biology · doi:10.1002/rmb2.12006 · Cited by 482
Signaling by Nuclear Receptors
Sever, R., & Glass, C. K. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a016709 · Cited by 374
Hsp90-Tau complex reveals molecular basis for specificity in chaperone action
Karagöz, G. E., Duarte, A. M. S., Akoury, E., Ippel, H., Biernat, J., Morán Luengo, T., Radli, M., Didenko, T., Nordhues, B. A., Veprintsev, D. B., et al. (2014) · Cell · doi:10.1016/j.cell.2014.01.037 · Cited by 318
“Hsp90 interacts with a specific, but structurally diverse, subset of client Cell 156, 963–974, February 27, 2014 ª2014 Elsevier Inc. 963 proteins including kinases and steroid receptors (Echeverria and Picard, 2010; Jakob et al., 1995; Pearl and Prodromou, 2006; Street et al., 2011).”
BackgroundInfluentialStructural mechanism of ergosterol regulation by fungal sterol transcription factor Upc2
Yang, H., Tong, J., Lee, C. W., Ha, S., Eom, S. H., & Im, Y. J. (2015) · Nature Communications · doi:10.1038/ncomms7129 · Cited by 223
Metadata
- Authors
- Echeverria, P. C., & Picard, D.
- Venue
- Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
- Publisher
- Elsevier BV
- Published
- 2010-06
- Volume
- 1803
- Issue
- 6
- Pages
- 641-649
- ISSN
- 0167-4889 (ISSN-L)
- OpenAlex
- W2157261840
- Cited by
- 227
- References
- 20
- FWCI
- 3.48
- Type
- journal article
- Language
- en
- Open access
- bronze
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- CoChat. (2026). Citation check: Molecular chaperones, essential partners of steroid hormone receptors for activity and mobility. https://app.cochat.ai/papers/10.1016/j.bbamcr.2009.11.012
- The paper
- Echeverria, P. C., & Picard, D. (2010). Molecular chaperones, essential partners of steroid hormone receptors for activity and mobility. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. https://doi.org/10.1016/j.bbamcr.2009.11.012
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.