The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
The large conformational changes of Hsp90 are only weakly coupled to ATP hydrolysis
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Citations
Cites
HSP90 and the chaperoning of cancer
Whitesell, L., & Lindquist, S. L. (2005) · Nature Reviews Cancer · doi:10.1038/nrc1716 · Cited by 2,502
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
The Hsp90 molecular chaperone: an open and shut case for treatment
Pearl, L. H., Prodromou, C., & Workman, P. (2008) · Biochemical Journal · doi:10.1042/bj20071640 · Cited by 447
Co-chaperone regulation of conformational switching in the Hsp90 ATPase cycle
Siligardi, G., Hu, B., Panaretou, B., Piper, P. W., Pearl, L. H., & Prodromou, C. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m410562200 · Cited by 207 · cited 1×
“Even though considerable progress has been made toward understanding the mechanochemical cycle of Hsp90, a clear dynamic picture is still missin”
BackgroundKrukenberg, K. A., Förster, F., Rice, L. M., Sali, A., & Agard, D. A. (2008) · Structure · doi:10.1016/j.str.2008.01.021 · Cited by 160
Cited by
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
Schopf, F. H., Biebl, M. M., & Buchner, J. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.20 · Cited by 1,540
The Hsp90 chaperone machinery: Conformational dynamics and regulation by co-chaperones
Li, J., Soroka, J., & Buchner, J. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2011.09.003 · Cited by 498
Conformational dynamics of the molecular chaperone Hsp90
Krukenberg, K. A., Street, T. O., Lavery, L. A., & Agard, D. A. (2011) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583510000314 · Cited by 308
Post-translational modifications of Hsp90 and their contributions to chaperone regulation
Mollapour, M., & Neckers, L. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2011.07.018 · Cited by 288
Metadata
- Authors
- Mickler, M., Hessling, M., Ratzke, C., Buchner, J., & Hugel, T.
- Venue
- Nature Structural & Molecular Biology
- Published
- 2009-02-22
- Volume
- 16
- Issue
- 3
- Pages
- 281-286
- ISSN
- 1545-9985 (ISSN-L)
- 1545-9993
- OpenAlex
- W2003439582
- Cited by
- 254
- References
- 5
- FWCI
- 9.24
- Type
- journal article
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: The large conformational changes of Hsp90 are only weakly coupled to ATP hydrolysis. https://app.cochat.ai/papers/10.1038/nsmb.1557
- The paper
- Mickler, M., Hessling, M., Ratzke, C., Buchner, J., & Hugel, T. (2009). The large conformational changes of Hsp90 are only weakly coupled to ATP hydrolysis. Nature Structural & Molecular Biology. https://doi.org/10.1038/nsmb.1557
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.
