The DOI matches its Crossref record; 214 of the 217 references it cites were found in a registry or an index.
The Hsp90 chaperone machinery: Conformational dynamics and regulation by co-chaperones
Open accessAbstract
Hsp90 is a dimeric molecular chaperone required for the activation and stabilization of numerous client proteins many of which are involved in essential cellular processes like signal transduction pathways. This activation process is regulated by ATP-induced large conformational changes, co-chaperones and posttranslational modifications. For some co-chaperones, a detailed picture on their structures and functions exists, for others their contributions to the Hsp90 system is still unclear. Recent progress on the conformational dynamics of Hsp90 and how co-chaperones affect the Hsp90 chaperone cycle significantly increased our understanding of the gearings of this complex molecular machinery. This article is part of a Special Issue entitled: Heat Shock Protein 90 (Hsp90).
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In the citing paper
“Hsp90 has weak intrinsic ATPase activity that is modulated by interactions with client proteins and co-chaperones.”
From Fungal Hsp90: a biological transistor that tunes cellular outputs to thermal inputs (2012) · cites this paper as [23]
In the citing paper
“The flexible Hsp90 dimer undergoes major conformational shifts during a dynamic chaperone cycle that is driven by ATP hydrolysis17,23-26 (Figure 1).”
From Fungal Hsp90: a biological transistor that tunes cellular outputs to thermal inputs (2012) · cites this paper as [23]
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Cites
Global analysis of protein expression in yeast
Ghaemmaghami, S., Huh, W.-K., Bower, K., Howson, R. W., Belle, A., Dephoure, N., O'Shea, E. K., & Weissman, J. S. (2003) · Nature · doi:10.1038/nature02046 · Cited by 3,750
Hsp90 as a capacitor for morphological evolution
Rutherford, S. L., & Lindquist, S. (1998) · Nature · doi:10.1038/24550 · Cited by 2,270
The Heat Shock Response: Life on the Verge of Death
Richter, K., Haslbeck, M., & Büchner, J. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.10.006 · Cited by 2,025
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
Targeting the dynamic HSP90 complex in cancer
Trepel, J. B., Mollapour, M., Giaccone, G., & Neckers, L. (2010) · Nature reviews. Cancer · doi:10.1038/nrc2887 · Cited by 1,523
Pratt, W. B., & Toft, D. O. (2003) · Experimental Biology and Medicine · doi:10.1177/153537020322800201 · Cited by 1,497
Hsp90 as a capacitor of phenotypic variation
Queitsch, C., Sangster, T. A., & Lindquist, S. (2002) · Nature · doi:10.1038/nature749 · Cited by 1,372
Zou, J., Guo, Y., Guettouche, T., Smith, D. F., & Voellmy, R. W. (1998) · Cell · doi:10.1016/s0092-8674(00)81588-3 · Cited by 1,232
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
Flagged first, then by citations
3 of the 217 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Molecular Chaperone Functions in Protein Folding and Proteostasis
Kim, Y., Hipp, M. S., Bracher, A., Hayer-Hartl, M. K., & Hartl, F. U. (2013) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060208-092442 · Cited by 1,545
In vivo aspects of protein folding and quality control
Balchin, D., Hayer-Hartl, M. K., & Hartl, F. U. (2016) · Science · doi:10.1126/science.aac4354 · Cited by 1,477
“p23 acts toward the end of the cycle, and facilitates client maturation by stabilizing the closed state of the Hsp90 N domains and inhibiting ATP hydrolysis (107).”
BackgroundChaperone machines for protein folding, unfolding and disaggregation
Saibil, H. R. (2013) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3658 · Cited by 1,211
Lu, H., Zhou, Q., He, J., Jiang, Z., Peng, C., Tong, R., & Shi, J. (2020) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-00315-3 · Cited by 891
“which regulate the cancer cell’s growth and apoptosis signaling pathways.(105,106) Hsp90 stabilizes the conformation of the client proteins mentioned above and prevents them from ubiquitination-mediated degradation, thereby stabilizes them to stay in the active form and promotes the tumor growth and metastasis (Fig.”
BackgroundThe heat‐shock protein/chaperone network and multiple stress resistance
Jacob, P., Hirt, H., & Bendahmane, A. (2016) · Plant Biotechnology Journal · doi:10.1111/pbi.12659 · Cited by 776
“Plant Biotechnology Journal published by Society for Experimental Biology and The Association of Applied Biologists and John Wiley & Sons Ltd., 15, 405–414 immunity, as HSP70 and HSP90 often cooperate in large multichaperone complexes (Li et al., 2012).”
Background
Metadata
- Authors
- Li, J., Soroka, J., & Buchner, J.
- Affiliations
- Technical University of Munich (DE)
- Center for Integrated Protein Science Munich (DE)
- Venue
- Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
- Publisher
- Elsevier BV
- Published
- 2012-03
- Volume
- 1823
- Issue
- 3
- Pages
- 624-635
- ISSN
- 0167-4889 (ISSN-L)
- OpenAlex
- W2093169681
- Cited by
- 498
- References
- 217
- Citations by year
- 2026: 7 · 2025: 18 · 2024: 15 · 2023: 23 · 2022: 31 · 2021: 39 · 2020: 45 · 2019: 44 · 2018: 54 · 2017: 39 · 2016: 51 · 2015: 35 · 2014: 45 · 2013: 33 · 2012: 15
- FWCI
- 2.76
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Biochimica et Biophysica Acta (BBA) - Molecular Cell Research (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Keywords
- HSP90, molecular chaperones, co-chaperones, conformational dynamics, ATP-induced conformational change, chaperone cycle, post-translational modification, signal transduction
- MeSH terms
- Adenosine Triphosphate, Animals, Binding Sites, Humans, Models, Molecular, Protein Binding, Protein Conformation, Molecular Chaperones, HSP90 Heat-Shock Proteins
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