The DOI matches its Crossref record; 53 of the 53 references it cites were found in a registry or an index.
Polyglutamine aggregates alter protein folding homeostasis in Caenorhabditis elegans
Open accessAbstract
Expansion of polyglutamine repeats in several unrelated proteins causes neurodegenerative diseases with distinct but related pathologies. To provide a model system for investigating common pathogenic features, we have examined the behavior of polyglutamine expansions expressed in Caenorhabditis elegans . The expression of polyglutamine repeats as green fluorescent protein (GFP)-fusion proteins in body wall muscle cells causes discrete cytoplasmic aggregates that appear early in embryogenesis and correlates with a delay in larval to adult development. The heat shock response is activated idiosyncratically in individual cells in a polyglutamine length-dependent fashion. The toxic effect of polyglutamine expression and the formation of aggregates can be reversed by coexpression of the yeast chaperone Hsp104. The altered homeostasis associated with polyglutamine aggregates causes both the sequestration of an otherwise soluble protein with shorter arrays of glutamine repeats and the relocalization of a nuclear glutamine-rich protein. These observations of induced aggregation and relocalization have implications for disorders involving protein aggregation.
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Cites
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Self-citationAggregation of Huntingtin in Neuronal Intranuclear Inclusions and Dystrophic Neurites in Brain
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Cited by
Cellular Defenses against Unfolded Proteins
Sherman, M. Y., & Goldberg, A. L. (2001) · Neuron · doi:10.1016/s0896-6273(01)00177-5 · Cited by 991
Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging
Morimoto, R. I. (2008) · Genes & Development · doi:10.1101/gad.1657108 · Cited by 872
Self-citationA chaperome subnetwork safeguards proteostasis in aging and neurodegenerative disease
Brehme, M., Voisine, C., Rolland, T., Wachi, S., Soper, J. H., Zhu, Y., Orton, K., Villella, A., Garza, D., Vidal, M., et al. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.09.042 · Cited by 584
Self-citationWyttenbach, A. (2002) · Human Molecular Genetics · doi:10.1093/hmg/11.9.1137 · Cited by 494
Snyder, H., Mensah, K., Theisler, C., Lee, J., Matouschek, A., & Wolozin, B. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m208641200 · Cited by 420
Metadata
- Authors
- Satyal, S. H., Schmidt, E., Kitagawa, K., Sondheimer, N., Lindquist, S., Kramer, J. M., & Morimoto, R. I.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2000-05-16
- Volume
- 97
- Issue
- 11
- Pages
- 5750-5755
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2169579807
- Cited by
- 371
- References
- 53
- FWCI
- 8.95
- Type
- journal article
- Language
- en
- Open access
- green
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