Widespread Protein Aggregation as an Inherent Part of Aging in C. elegans

By Della C. David, Noah Ollikainen, J. Trinidad, Michael P. Cary, Alma Burlingame, C. Kenyon. PLoS Biology, 2010

633 citations recorded by the source corpus.

Several hundred proteins become insoluble and aggregation-prone as a consequence of aging in Caenorhabditis elegans. The data indicate that these proteins influence disease-related protein aggregation and toxicity.

Subfields: Aging, Cellular and Molecular Neuroscience, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/64682b5945eb222e4193cad7935c8ebfd1fd8e76

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Aging

1. M. Hayer-Hartl
2. F. Hartl
3. G. Jayaraj
4. A. Bracher
5. C. L. Klaips

In Cellular and Molecular Neuroscience

1. M. Hayer-Hartl
2. F. Hartl

In Molecular Biology

1. F. Hartl
2. M. Hayer-Hartl
3. G. Jayaraj
4. C. L. Klaips
5. A. Bracher
6. Christopher M. Dobson
7. A. Goldberg
8. Richard I. Morimoto

Citations in the corpus

• Pathways of cellular proteostasis in aging and disease (2018, background): “, 2011; Cuervo and Wong, 2014), contributing to the widespread protein aggregation that is observed in postmitotic cells, such as muscle and neurons, and predisposing the latter for certain neurodegenerative diseases (David et al., 2010; Hamer et al., 2010; Walther et al., 2015).”
• Molecular chaperones in protein folding and proteostasis (2011, background): “Proteostasis collapse in ageing and disease The accumulation of misfolded and/or oxidized proteins in cells during ageing is a challenge to the proteostasis system and eventually results in the deposition of aggregates, as shown in model organisms such as Caenorhabditis elegans and Drosophila”