The DOI matches its Crossref record; 103 of the 103 references it cites were found in a registry or an index.
The chaperone Hsp90: changing partners for demanding clients
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Citations
Cites
HSP90 at the hub of protein homeostasis: emerging mechanistic insights
Taipale, M., Jarosz, D. F., & Lindquist, S. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2918 · Cited by 1,818
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
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
HDAC6 Regulates Hsp90 Acetylation and Chaperone-Dependent Activation of Glucocorticoid Receptor
Kovacs, J. J., Murphy, P. J. M., Gaillard, S., Zhao, X., Wu, J.-T., Nicchitta, C. V., Yoshida, M., Toft, D. O., Pratt, W. B., & Yao, T.-P. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.04.021 · Cited by 1,153
The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins
Connell, P., Ballinger, C. A., Jiang, J., Wu, Y., Thompson, L. J., Höhfeld, J., & Patterson, C. (2001) · Nature Cell Biology · doi:10.1038/35050618 · Cited by 997
Modulation of Akt kinase activity by binding to Hsp90
Sato, S., Fujita, N., & Tsuruo, T. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.170276797 · Cited by 967
Crystal structure of an Hsp90–nucleotide–p23/Sba1 closed chaperone complex
Ali, M. M. U., Roe, S. M., Vaughan, C. K., Meyer, P., Panaretou, B., Piper, P. W., Prodromou, C., & Pearl, L. H. (2006) · Nature · doi:10.1038/nature04716 · Cited by 962
Ballinger, C. A., Connell, P., Wu, Y., Hu, Z., Thompson, L. J., Yin, L.-Y., & Patterson, C. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.6.4535 · Cited by 943
Quantitative Analysis of Hsp90-Client Interactions Reveals Principles of Substrate Recognition
Taipale, M., Krykbaeva, I., Koeva, M., Kayatekin, C., Westover, K. D., Karras, G. I., & Lindquist, S. (2012) · Cell · doi:10.1016/j.cell.2012.06.047 · Cited by 879
Zhao, R., Davey, M., Hsu, Y.-C., Kaplanek, P., Tong, A., Parsons, A. B., Krogan, N., Cagney, G., Mai, D., Greenblatt, J., et al. (2005) · Cell · doi:10.1016/j.cell.2004.12.024 · Cited by 819
Cited by
Schopf, F. H., Biebl, M. M., & Buchner, J. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.20 · Cited by 1,540
In vivo aspects of protein folding and quality control
Balchin, D., Hayer-Hartl, M., & Hartl, F. U. (2016) · Science · doi:10.1126/science.aac4354 · Cited by 1,439
Hsp90 and Hsp70 chaperones: Collaborators in protein remodeling
Genest, O., Wickner, S., & Doyle, S. M. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.rev118.002806 · Cited by 382
RNAi in Plants: An Argonaute-Centered View
Fang, X., & Qi, Y. (2016) · The Plant Cell · doi:10.1105/tpc.15.00920 · Cited by 357
Modulation of the Hsp90 Chaperone Cycle by a Stringent Client Protein
Lorenz, O. R., Freiburger, L., Rutz, D. A., Krause, M., Zierer, B. K., Alvira, S., Cuéllar, J., Valpuesta, J. M., Madl, T., Sattler, M., et al. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.02.003 · Cited by 151
Metadata
- Authors
- Röhl, A., Rohrberg, J., & Buchner, J.
- Venue
- Trends in Biochemical Sciences
- Publisher
- Elsevier BV
- Published
- 2013-05
- Volume
- 38
- Issue
- 5
- Pages
- 253-262
- ISSN
- 0968-0004 (ISSN-L)
- OpenAlex
- W1999140770
- Cited by
- 269
- References
- 103
- FWCI
- 2.14
- Type
- journal article
- Language
- en
- Open access
- closed
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- The paper
- Röhl, A., Rohrberg, J., & Buchner, J. (2013). The chaperone Hsp90: changing partners for demanding clients. Trends in Biochemical Sciences. https://doi.org/10.1016/j.tibs.2013.02.003
Data sources
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.
