The DOI matches its Crossref record; 49 of the 50 references it cites were found in a registry or an index.
Structure and in vivo function of Hsp90
Open accessAbstract
Until recently, Hsp90 was one of the least well understood of the molecular chaperones, but considerable progress is now being made in unravelling its biochemistry. Hsp90 has now been shown to possess an inherent ATPase that is essential for the activation of authentic 'client' proteins in vivo and in vitro. The molecular detail of Hsp90's interactions with co-chaperones is also becoming clearer and the identification of key roles in assembling regulatory and signalling pathways has made it a target for anticancer drug development. Despite this, a clear understanding of how Hsp90 contributes to the folding and/or activation of its client proteins remains some way off.
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In the citing paper
“Briefly, the Hsp90 protein has three domains and operates as a dimer24-26 (Figure 1).”
From Fungal Hsp90: a biological transistor that tunes cellular outputs to thermal inputs (2012) · cites this paper as [24]
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 [24]
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 [24]
Citations
Cites
Hsp90 as a capacitor for morphological evolution
Rutherford, S. L., & Lindquist, S. (1998) · Nature · doi:10.1038/24550 · Cited by 2,270
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
Stebbins, C. E., Russo, A. A., Schneider, C. B., Rosen, N. X., Hartl, F. U., & Pavletich, N. P. (1997) · Cell · doi:10.1016/s0092-8674(00)80203-2 · Cited by 1,370
Prodromou, C., Roe, S. M., O’Brien, R., Ladbury, J. E., Piper, P. W., & Pearl, L. H. (1997) · Cell · doi:10.1016/s0092-8674(00)80314-1 · Cited by 1,258
Self-citationZou, 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
Dynamic activation of endothelial nitric oxide synthase by Hsp90
García‐Cardeña, G., Fan, R., Shah, V. H., Sorrentino, R., Cirino, G., Papapetropoulos, A., & Sessa, W. C. (1998) · Nature · doi:10.1038/33934 · Cited by 1,029
Roe, S. M., Prodromou, C., O'Brien, R., Ladbury, J. E., Piper, P. W., & Pearl, L. H. (1999) · Journal of Medicinal Chemistry · doi:10.1021/jm980403y · Cited by 1,004
Self-citationDas, A. K., Cohen, P. T. W., & Barford, D. (1998) · The EMBO Journal · doi:10.1093/emboj/17.5.1192 · Cited by 832
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
Self-citationStructure, function and evolution of DnaJ: conservation and adaptation of chaperone function
Cheetham, M. E., & Caplan, A. J. (1998) · Cell Stress and Chaperones · doi:10.1379/1466-1268(1998)003 · Cited by 604
Research works printed but not linked: 1
- Schulte, 1998, Antibiotic radicicol binds to the N-terminal domain of Hsp90 and shares important biologic activities with geldanamycin, Cell Stress Chaperones, 3, 100, 10.1379/1466-1268(1998)003<0100:ARBTTN>2.3.CO;2 · DOI
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Pratt, W. B., & Toft, D. O. (2003) · Experimental Biology and Medicine · doi:10.1177/153537020322800201 · Cited by 1,497
Folding of Newly Translated Proteins In Vivo: The Role of Molecular Chaperones
Frydman, J. (2001) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.70.1.603 · Cited by 1,184
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
Intestinal epithelial cells secrete exosome–like vesicles
van Niel, G., Raposo, G., Candalh, C., Boussac, M., Hershberg, R. M., Cerf–Bensussan, N., & Heyman, M. (2001) · Gastroenterology · doi:10.1053/gast.2001.26263 · Cited by 698
Metadata
- Authors
- Pearl, L. H., & Prodromou, C.
- Affiliations
- Institute of Cancer Research (GB)
- Corresponding author
- Pearl, Laurence H
- Venue
- Current Opinion in Structural Biology
- Publisher
- Elsevier BV
- Published
- 2000-02
- Volume
- 10
- Issue
- 1
- Pages
- 46-51
- ISSN
- 0959-440X (ISSN-L)
- OpenAlex
- W2046329541
- Cited by
- 317
- References
- 50
- Citations by year
- 2026: 2 · 2025: 3 · 2024: 3 · 2023: 3 · 2022: 7 · 2021: 8 · 2020: 9 · 2019: 14 · 2018: 7 · 2017: 11 · 2016: 13 · 2015: 13 · 2014: 8 · 2013: 12 · 2012: 19
- FWCI
- 2.02
- Type
- journal article
- Language
- en
- Open access
- green
- figshare.com
- Licence
- Locations
- Current Opinion in Structural Biology (publishedVersion)
- PubMed (publishedVersion)
- Figshare (submittedVersion, cc-by)
- Funders
- Wellcome Trust
- Preeclampsia Research Laboratories
- 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, ATPase activity, co-chaperones, protein folding, signaling pathways, anticancer drug targets
- MeSH terms
- Adenosine Triphosphate, Allosteric Regulation, Animals, Bacterial Proteins, Humans, Models, Biological, Models, Molecular, Protein Binding, Quinones, Structure-Activity Relationship, Signal Transduction, Benzoquinones, Rifabutin, HSP90 Heat-Shock Proteins, Macromolecular Substances, Lactams, Macrocyclic
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