The DOI matches its Crossref record; 11 of the 11 references it cites were found in a registry or an index.
Cooperation of molecular chaperones with the ubiquitin/proteasome system
Open accessAbstract
Molecular chaperones and energy-dependent proteases have long been viewed as opposing forces that control protein biogenesis. Molecular chaperones are specialized in protein folding, whereas energy-dependent proteases such as the proteasome mediate efficient protein degradation. Recent data, however, suggest that molecular chaperones directly cooperate with the ubiquitin/proteasome system during protein quality control in eukaryotic cells. Modulating the intracellular balance of protein folding and protein degradation may open new strategies for the treatment of human diseases that involve chaperone pathways such as cancer and diverse amyloid diseases.
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Cites
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“This effect of the chaperone system was reproduced in yeast and mammalian cells when the polyQ tract was co-expressed with Hsp70 and Hsp40 homologs [76,78].”
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The proteostasis network and its decline in ageing
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Tramutola, A., Di Domenico, F., Barone, E., Arena, A., Giorgi, A., di Francesco, L., Schininà, M. E., Coccia, R., Head, E., Butterfield, D. A., et al. (2017) · Antioxidants & Redox Signaling · doi:10.1089/ars.2016.6686 · Cited by 49
Metadata
- Authors
- Esser, C., Alberti, S., & Höhfeld, J.
- Venue
- Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
- Publisher
- Elsevier BV
- Published
- 2004-11
- Volume
- 1695
- Issue
- 1-3
- Pages
- 171-188
- ISSN
- 0167-4889 (ISSN-L)
- OpenAlex
- W2140586922
- Cited by
- 245
- References
- 11
- FWCI
- 6.12
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Esser, C., Alberti, S., & Höhfeld, J. (2004). Cooperation of molecular chaperones with the ubiquitin/proteasome system. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. https://doi.org/10.1016/j.bbamcr.2004.09.020
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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).
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