The DOI matches its Crossref record; 38 of the 38 references it cites were found in a registry or an index.
Dissection of the ATP-induced conformational cycle of the molecular chaperone Hsp90
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Citations
Cites
Molecular Chaperones in the Cytosol: from Nascent Chain to Folded Protein
Hartl, F. U., & Hayer-Hartl, M. (2002) · Science · doi:10.1126/science.1068408 · Cited by 3,347
HSP90 and the chaperoning of cancer
Whitesell, L., & Lindquist, S. L. (2005) · Nature Reviews Cancer · doi:10.1038/nrc1716 · Cited by 2,502
Hsp90 as a capacitor for morphological evolution
Rutherford, S. L., & Lindquist, S. (1998) · Nature · doi:10.1038/24550 · Cited by 2,270
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
Whitesell, L., Mimnaugh, E. G., De Costa, B., Myers, C. E., & Neckers, L. M. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.18.8324 · Cited by 1,444
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
Heat-shock protein 90, a chaperone for folding and regulation
Picard, D. (2002) · Cellular and Molecular Life Sciences · doi:10.1007/pl00012491 · Cited by 796
GHKL, an emergent ATPase/kinase superfamily
DUTTA, R., & INOUYE, M. (2000) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(99)01503-0 · Cited by 762
ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo
Panaretou, B., Prodromou, C., Roe, S. M., O'Brien, R., Ladbury, J. E., Piper, P. W., & Pearl, L. H. (1998) · The EMBO Journal · doi:10.1093/emboj/17.16.4829 · Cited by 735
In Vivo Function of Hsp90 Is Dependent on ATP Binding and ATP Hydrolysis
Obermann, W. M. J., Sondermann, H., Russo, A. A., Pavletich, N. P., & Hartl, F. U. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.143.4.901 · Cited by 601
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
Verghese, J., Abrams, J., Wang, Y., & Morano, K. A. (2012) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.05018-11 · Cited by 575
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
Protein Quality Control in the Cytosol and the Endoplasmic Reticulum: Brothers in Arms
Buchberger, A., Bukau, B., & Sommer, T. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.10.001 · Cited by 483
Metadata
- Authors
- Hessling, M., Richter, K., & Buchner, J.
- Venue
- Nature Structural & Molecular Biology
- Published
- 2009-02-22
- Volume
- 16
- Issue
- 3
- Pages
- 287-293
- ISSN
- 1545-9985 (ISSN-L)
- 1545-9993
- OpenAlex
- W1974206962
- Cited by
- 349
- References
- 38
- FWCI
- 12.36
- Type
- journal article
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: Dissection of the ATP-induced conformational cycle of the molecular chaperone Hsp90. https://app.cochat.ai/papers/10.1038/nsmb.1565
- The paper
- Hessling, M., Richter, K., & Buchner, J. (2009). Dissection of the ATP-induced conformational cycle of the molecular chaperone Hsp90. Nature Structural & Molecular Biology. https://doi.org/10.1038/nsmb.1565
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.
