Abstract 2808 Hsp70 and Hsp110 Chaperones Influence Human Transthyretin Protein Aggregation
Molecular chaperones play a crucial role in maintaining proper protein folding and limiting protein aggregation. However, as we age, the decline of the proteostasis network can lead to protein aggregation, which is commonly associated with protein aggregation diseases. Despite significant progress in understanding molecular chaperones, the mechanisms by which chaperones influence intracellular protein aggregation in vivo is not fully clear. This gap in knowledge is particularly evident in diseases like transthyretin amyloidosis (ATTR), which remains significantly understudied.
Authors
- Claire M. Radtke
- Anita L. Manogaran (ORCID: https://orcid.org/0000-0003-0844-1479)
Institutions
- Marquette University (US)
Publication Details
- Journal
- Journal of Biological Chemistry
- Published
- 2025-05-01
- DOI
- https://doi.org/10.1016/j.jbc.2025.110033
- Primary Topic
- Endoplasmic Reticulum Stress and Disease
- Type
- article
- Field-Weighted Citation Impact
- 0.00
Funders
- U.S. Department of Energy
- Office of Science
- Basic Energy Sciences