Hsp70-hsp90 chaperone networking in protein-misfolding disease

C Prodromou, X Aran-Guiu, J Oberoi, L Perna… - The Networking of …, 2022 - Springer
Molecular chaperones and their associated co-chaperones are essential in health and
disease as they are key facilitators of protein-folding, quality control and function. In …

Fluc‐EGFP reporter mice reveal differential alterations of neuronal proteostasis in aging and disease

S Blumenstock, EK Schulz‐Trieglaff, K Voelkl… - The EMBO …, 2021 - embopress.org
The cellular protein quality control machinery is important for preventing protein misfolding
and aggregation. Declining protein homeostasis (proteostasis) is believed to play a crucial …

[HTML][HTML] The insoluble protein deposit (IPOD) in yeast

S Rothe, A Prakash, J Tyedmers - Frontiers in molecular neuroscience, 2018 - frontiersin.org
The appearance of protein aggregates is a hallmark of several pathologies including many
neurodegenerative diseases. Mounting evidence suggests that the accumulation of …

[HTML][HTML] Trehalose reverses cell malfunction in fibroblasts from normal and Huntington's disease patients caused by proteosome inhibition

MA Fernandez-Estevez, MJ Casarejos… - PloS one, 2014 - journals.plos.org
Huntington's disease (HD) is a neurodegenerative disorder characterized by progressive
motor, cognitive and psychiatric deficits, associated with predominant loss of striatal neurons …

[HTML][HTML] Sequestrase chaperones protect against oxidative stress-induced protein aggregation and [PSI+] prion formation

Z Carter, D Creamer, A Kouvidi, CM Grant - Plos Genetics, 2024 - journals.plos.org
Misfolded proteins are usually refolded to their functional conformations or degraded by
quality control mechanisms. When misfolded proteins evade quality control, they can be …

Targeting Hsp70 facilitated protein quality control for treatment of polyglutamine diseases

AK Davis, WB Pratt, AP Lieberman, Y Osawa - Cellular and Molecular Life …, 2020 - Springer
The polyglutamine (polyQ) diseases are a group of nine fatal, adult-onset
neurodegenerative disorders characterized by the misfolding and aggregation of mutant …

[HTML][HTML] The Cdc48 complex alleviates the cytotoxicity of misfolded proteins by regulating ubiquitin homeostasis

R Higgins, MH Kabbaj, D Sherwin, LA Howell… - Cell reports, 2020 - cell.com
The accumulation of misfolded proteins is associated with multiple neurodegenerative
disorders, but it remains poorly defined how this accumulation causes cytotoxicity. Here, we …

[HTML][HTML] Regulation of SETD2 stability is important for the fidelity of H3K36me3 deposition

S Bhattacharya, JL Workman - Epigenetics & Chromatin, 2020 - Springer
Abstract Background The histone H3K36me3 mark regulates transcription elongation, pre-
mRNA splicing, DNA methylation, and DNA damage repair. However, knowledge of the …

[HTML][HTML] Dynamic recruitment of active proteasomes into polyglutamine initiated inclusion bodies

S Schipper-Krom, K Juenemann, AH Jansen… - FEBS letters, 2014 - Elsevier
Neurodegenerative disorders such as Huntington's disease are hallmarked by neuronal
intracellular inclusion body formation. Whether proteasomes are irreversibly recruited into …

[HTML][HTML] Characterization of protein complexes of the endoplasmic reticulum-associated degradation E3 ubiquitin ligase Hrd1

J Hwang, CP Walczak, TA Shaler, JA Olzmann… - Journal of Biological …, 2017 - ASBMB
Hrd1 is the core structural component of a large endoplasmic reticulum membrane-
embedded protein complex that coordinates the destruction of folding-defective proteins in …