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Small-molecule proteostasis regulators for protein conformational diseases

Calamini, Barbara, Silva, Maria Catarina, Madoux, Franck, Hutt, Darren M, Khanna, Shilpi, Chalfant, Monica A, Saldanha, S Adrian, Hodder, Peter, Tait, Bradley D, Garza, Dan, Balch, William E, Morimoto, Richard I·2012·Nature Chemical Biology
DOI 10.1038/nchembio.763PMC PMC3262058
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Crossref · 10.1038/nchembio.763

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  • Small molecules may be employed as pharmacological chaperones to assure the refolding of damaged proteins and to improve age-related phenotypes in model organisms.

    “Small molecules may be also employed as pharmacological chaperones to assure the refolding of damaged proteins and to improve age-related phenotypes in model organisms (Calamini et al., 2012).”

    From The Hallmarks of Aging (2013) · cites this paper as Calamini et al., 2012

    The Results section, “Suppression of Aggregation and Toxicity in C. elegans” (page unavailable), reports that small-molecule proteostasis regulators reduced age-dependent protein aggregation and restored motility in a disease-model organism. The Abstract and Discussion say the compounds induce cellular chaperone expression and restore protein folding in disease models. They do not establish that the compounds themselves act as pharmacological chaperones directly refolding damaged proteins, or that they improve age-related phenotypes beyond this age-dependent disease model. (LLM, conf=0.87)

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Research works printed but not linked: 43

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Metadata

Authors
Calamini, B., Silva, M. C., Madoux, F., Hutt, D. M., Khanna, S., Chalfant, M. A., Saldanha, S. A., Hodder, P., Tait, B. D., Garza, D., Balch, W. E., & Morimoto, R. I.
Venue
Nature Chemical Biology
Publisher
Springer Science and Business Media LLC
Published
2011-12-25
Volume
8
Issue
2
Pages
185-196
ISSN
  • 1552-4450
  • 1552-4469
DOI
10.1038/nchembio.763
PMC
PMC3262058
Cited by
199
References
7
Language
en
Licence
www.springer.com/tdm (tdm)

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