Adapting Proteostasis for Disease Intervention

By William E. Balch, Richard I. Morimoto, A. Dillin, J. Kelly. Science, 2008

2,402 citations recorded by the source corpus.

Subfields: Cell Biology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/bfc709e5367fe964cc3618f22763acef4a5fc864

How researchers see this paper

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

In Cell Biology

In Molecular Biology

Citations in the corpus

The CamSol method of rational design of protein mutants with enhanced solubility. (2015, neutral): “living organisms [16–18].”
The amyloid state and its association with protein misfolding diseases (2014, background): “Paired betasheet structure of an Aβ(1-40) amyloid fibril revealed by electron microscopy.”
Direct Observation of the Interconversion of Normal and Toxic Forms of α-Synuclein (2012, background): “These findings highlight the key role that molecular chaperones and the cellular protein degradation machinery must play continually in preventing damage caused by such oligomers and hence the onset of disease (Balch et al., 2008; Morimoto, 2008).”
Amyloid-like aggregates sequester numerous metastable proteins with essential cellular functions. (2011, background): “with Essential Cellular Functions”
Widespread Protein Aggregation as an Inherent Part of Aging in C. elegans (2010, background): “. These age-dependent changes in proteostasis are thought to facilitate the aberrant aggregation of specific proteins in the context of neurodegeneration and amyloidoses”
Understanding the contribution of synonymous mutations to human disease (2011, background): “Misfolding that occurs as a result of a synonymous mutation may have consequences beyond the functionality of the particular protein in which the mutation occurre”
Serine 403 phosphorylation of p62/SQSTM1 regulates selective autophagic clearance of ubiquitinated proteins. (2011, background): “Mutation, aging, and environmental stresses decrease proteasome activity and cause an imbalance of proteostasis, resulting in the production of misfolded proteins and the accumulation of ubiquitinated proteins (Ub proteins) and aggregates (Balch et al., 2008; Morimoto, 2008).”
The cell biology of disease: lysosomal storage disorders: the cellular impact of lysosomal dysfunction. (2012, neutral): “HSp70 (CT) Lysosome + Kirkegaard et al., 2010 Proteostasis regulation therapy (PRT) ER + Balch et al., 2008; Mu et al., 2008 Cholesterol removal using cyclodextrin in NPC1 disease Lysosome + + Davidson et al., 2009; Ward et al., 2010; Aqul et al., 2011 POC, proof of concept.”
Endoplasmic reticulum stress: molecular mechanism and therapeutic targets (2023, background): “INTRODUCTION Proteostasis is fundamental to cell survival, and an imbalance will result in diseases including metabolic, neurodegenerative, oncological, and cardiovascular disorders.(1) The endoplasmic reticulum (ER) functions as a quality-control organelle for the proteins it produces, allowing onl”