The DOI matches its Crossref record; 11 of the 11 references it cites were found in a registry or an index.
Broad action of Hsp90 as a host chaperone required for viral replication
Open accessAbstract
Viruses are intracellular pathogens responsible for a vast number of human diseases. Due to their small genome size, viruses rely primarily on the biosynthetic apparatus of the host for their replication. Recent work has shown that the molecular chaperone Hsp90 is nearly universally required for viral protein homeostasis. As observed for many endogenous cellular proteins, numerous different viral proteins have been shown to require Hsp90 for their folding, assembly, and maturation. Importantly, the unique characteristics of viral replication cause viruses to be hypersensitive to Hsp90 inhibition, thus providing a novel therapeutic avenue for the development of broad-spectrum antiviral drugs. The major developments in this emerging field are hereby discussed.
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Cites
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HSP90 at the hub of protein homeostasis: emerging mechanistic insights
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Diverse Cellular Functions of the Hsp90 Molecular Chaperone Uncovered Using Systems Approaches
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Self-citationDisassembly of Transcriptional Regulatory Complexes by Molecular Chaperones
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Modulation of p53, ErbB1, ErbB2, and Raf-1 Expression in Lung Cancer Cells by Depsipeptide FR901228
Yu, X. (2002) · CancerSpectrum Knowledge Environment · doi:10.1093/jnci/94.7.504 · Cited by 360
Conformational dynamics of the molecular chaperone Hsp90
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Akt and CHIP coregulate tau degradation through coordinated interactions
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Cited by
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 Family: Structure, Regulation, Function, and Implications in Health and Disease
Hoter, A., El-Sabban, M. E., & Naim, H. Y. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19092560 · Cited by 693
Jackson, S. E. (2012) · Topics in Current Chemistry · doi:10.1007/128_2012_356 · Cited by 338
Wyler, E., Mösbauer, K., Franke, V., Diag, A., Gottula, L. T., Arsiè, R., Klironomos, F., Koppstein, D., Hönzke, K., Ayoub, S., et al. (2021) · iScience · doi:10.1016/j.isci.2021.102151 · Cited by 316
The Plasticity of the Hsp90 Co-chaperone System
Sahasrabudhe, P., Rohrberg, J., Biebl, M. M., Rutz, D. A., & Buchner, J. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.08.004 · Cited by 136
Metadata
- Authors
- Geller, R., Taguwa, S., & Frydman, J.
- Venue
- Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
- Publisher
- Elsevier BV
- Published
- 2012-03
- Volume
- 1823
- Issue
- 3
- Pages
- 698-706
- ISSN
- 0167-4889 (ISSN-L)
- OpenAlex
- W1989600727
- Cited by
- 224
- References
- 11
- FWCI
- 2.70
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Geller, R., Taguwa, S., & Frydman, J. (2012). Broad action of Hsp90 as a host chaperone required for viral replication. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. https://doi.org/10.1016/j.bbamcr.2011.11.007
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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.
