The DOI matches its Crossref record; 122 of the 122 references it cites were found in a registry or an index.
Hsp90 and Hsp70 chaperones: Collaborators in protein remodeling
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and other bacteria are also discussed. We anticipate that the information gained from exploring the mechanism of the bacterial chaperone system will provide the groundwork for understanding the more complex eukaryotic Hsp90 system and its modulation by Hsp90 co-chaperones.
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Cites
Lindquist, S. (1986) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.55.070186.005443 · Cited by 4,588
The HSP70 chaperone machinery: J proteins as drivers of functional specificity
Kampinga, H. H., & Craig, E. A. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2941 · Cited by 1,755
Molecular Chaperones and Protein Quality Control
Bukau, B., Weissman, J., & Horwich, A. (2006) · Cell · doi:10.1016/j.cell.2006.04.014 · Cited by 1,557
Schopf, F. H., Biebl, M. M., & Buchner, J. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.20 · Cited by 1,540
Structural Analysis of Substrate Binding by the Molecular Chaperone DnaK
Zhu, X., Zhao, X., Burkholder, W. F., Gragerov, A., Ogata, C. M., Gottesman, M. E., & Hendrickson, W. A. (1996) · Science · doi:10.1126/science.272.5268.1606 · Cited by 1,258
Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein
Flaherty, K. M., DeLuca-Flaherty, C., & McKay, D. B. (1990) · Nature · doi:10.1038/346623a0 · Cited by 1,030
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
Quantitative Analysis of Hsp90-Client Interactions Reveals Principles of Substrate Recognition
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Mechanism of regulation of Hsp70 chaperones by DnaJ cochaperones
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Cited by
Structure of Hsp90–Hsp70–Hop–GR reveals the Hsp90 client-loading mechanism
Wang, R. Y.-R., Noddings, C. M., Kirschke, E., Myasnikov, A. G., Johnson, J. L., & Agard, D. A. (2022) · Nature · doi:10.1038/s41586-021-04252-1 · Cited by 220
Intermolecular Interactions between Hsp90 and Hsp70
Doyle, S. M., Hoskins, J. R., Kravats, A. N., Heffner, A. L., Garikapati, S., & Wickner, S. (2019) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.05.026 · Cited by 64
Self-citationJin, W., Brannan, K. W., Kapeli, K., Park, S. S., Tan, H. Q., Gosztyla, M. L., Mujumdar, M., Ahdout, J., Henroid, B., Rothamel, K., et al. (2023) · Molecular Cell · doi:10.1016/j.molcel.2023.06.019 · Cited by 52
Wang, R. Y.-R., Noddings, C. M., Kirschke, E., Myasnikov, A. G., Johnson, J. L., & Agard, D. A. (2020) · doi:10.1101/2020.11.05.370247 · Cited by 10
Kirschke, E., Roe-Zurz, Z., Noddings, C., & Agard, D. (2020) · doi:10.1101/2020.05.03.075523 · Cited by 6
Metadata
- Authors
- Genest, O., Wickner, S., & Doyle, S. M.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2019-02
- Volume
- 294
- Issue
- 6
- Pages
- 2109-2120
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2899701660
- Cited by
- 382
- References
- 122
- FWCI
- 9.65
- Type
- journal article
- Language
- en
- Open access
- hybrid
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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.
