The DOI matches its Crossref record; 8 of the 8 references it cites were found in a registry or an index.
Cyclophilin 40 facilitates HSP90‐mediated RISC assembly in plants
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Citations
Cites
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
Roe, S. M., Prodromou, C., O'Brien, R., Ladbury, J. E., Piper, P. W., & Pearl, L. H. (1999) · Journal of Medicinal Chemistry · doi:10.1021/jm980403y · Cited by 1,004
A 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
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 · cited 1×
“For example, FKBP52 potentiates glucocorticoid signalling by increasing hormone-binding affinity, while FKBP51 anta-gonizes the FKBP52 function (Riggs et al , 2003).”
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
Barent, R. L., Nair, S. C., Carr, D. C., Ruan, Y., Rimerman, R. A., Fulton, J., Zhang, Y., & Smith, D. F. (1998) · Molecular Endocrinology · doi:10.1210/mend.12.3.0075 · Cited by 190 · cited 1×
“Because TPR cochaperones compete for binding to the EEVD motif of HSP90 (Barent et al , 1998; Carrello et al , 1999), the population of AGO1–HSP90–cochaperone complexes should exist in a dynamic mixture reflecting the relative abundance and affinity of each TPR cochaperone for AGO1–HSP90.”
Galigniana, M. D., Erlejman, A. G., Monte, M., Gomez-Sanchez, C., & Piwien-Pilipuk, G. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.01190-09 · Cited by 152
Cited by
Biogenesis, Turnover, and Mode of Action of Plant MicroRNAs
Rogers, K., & Chen, X. (2013) · The Plant Cell · doi:10.1105/tpc.113.113159 · Cited by 935
The Functions of MicroRNAs: mRNA Decay and Translational Repression
Iwakawa, H.-O., & Tomari, Y. (2015) · Trends in Cell Biology · doi:10.1016/j.tcb.2015.07.011 · Cited by 732
RNAi in Plants: An Argonaute-Centered View
Fang, X., & Qi, Y. (2016) · The Plant Cell · doi:10.1105/tpc.15.00920 · Cited by 357
Jackson, S. E. (2012) · Topics in Current Chemistry · doi:10.1007/128_2012_356 · Cited by 338
RISC assembly: Coordination between small RNAs and Argonaute proteins
Kobayashi, H., & Tomari, Y. (2016) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2015.08.007 · Cited by 307
Metadata
- Authors
- Iki, T., Yoshikawa, M., Meshi, T., & Ishikawa, M.
- Venue
- The EMBO Journal
- Published
- 2011-11-01
- Volume
- 31
- Issue
- 2
- Pages
- 267-278
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- OpenAlex
- W1952594807
- Cited by
- 162
- References
- 8
- FWCI
- 15.26
- Type
- journal article
- Language
- en
- Open access
- bronze
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- CoChat. (2026). Citation check: Cyclophilin 40 facilitates HSP90‐mediated RISC assembly in plants. https://app.cochat.ai/papers/10.1038/emboj.2011.395
- The paper
- Iki, T., Yoshikawa, M., Meshi, T., & Ishikawa, M. (2012). Cyclophilin 40 facilitates HSP90‐mediated RISC assembly in plants. The EMBO Journal. https://doi.org/10.1038/emboj.2011.395
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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.
