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.

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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

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article

Abstract 2808 Hsp70 and Hsp110 Chaperones Influence Human Transthyretin Protein Aggregation

Claire M. Radtke, Anita L. Manogaran
Journal of Biological Chemistry
Endoplasmic Reticulum Stress and Disease
article

Abstract 2808 Hsp70 and Hsp110 Chaperones Influence Human Transthyretin Protein Aggregation

Claire M. Radtke, Anita L. Manogaran
article en

Abstract

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.

Journal of Biological ChemistryVol. 301(5)
Marquette University (US)
U.S. Department of Energy, Office of Science, Basic Energy Sciences
Zero hunger
Openalex Percentile: Top 86%
Endoplasmic Reticulum Stress and Disease
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