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Cited by 497

The DOI matches its Crossref record; 59 of the 59 references it cites were found in a registry or an index.

Aggrephagy: Selective Disposal of Protein Aggregates by Macroautophagy

Open access
Lamark, Trond, Johansen, Terje·2012·International Journal of Cell Biology

Abstract

Protein aggregation is a continuous process in our cells. Some proteins aggregate in a regulated manner required for different vital functional processes in the cells whereas other protein aggregates result from misfolding caused by various stressors. The decision to form an aggregate is largely made by chaperones and chaperone-assisted proteins. Proteins that are damaged beyond repair are degraded either by the proteasome or by the lysosome via autophagy. The aggregates can be degraded by the proteasome and by chaperone-mediated autophagy only after dissolution into soluble single peptide species. Hence, protein aggregates as such are degraded by macroautophagy. The selective degradation of protein aggregates by macroautophagy is called aggrephagy. Here we review the processes of aggregate formation, recognition, transport, and sequestration into autophagosomes by autophagy receptors and the role of aggrephagy in different protein aggregation diseases.

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Metadata

Authors
Lamark, T., & Johansen, T.
Venue
International Journal of Cell Biology
Published
2012
Volume
2012
Pages
1-21
ISSN
  • 1687-8876 (ISSN-L)
  • 1687-8884
OpenAlex
W1990619980
Cited by
497
References
59
FWCI
24.77
Type
journal article
Language
en
Open access
gold

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CoChat. (2026). Citation check: Aggrephagy: Selective Disposal of Protein Aggregates by Macroautophagy. https://app.cochat.ai/papers/10.1155/2012/736905
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Lamark, T., & Johansen, T. (2012). Aggrephagy: Selective Disposal of Protein Aggregates by Macroautophagy. International Journal of Cell Biology. https://doi.org/10.1155/2012/736905

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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.