Biological and chemical approaches to diseases of proteostasis deficiency.

By E. Powers, Richard I. Morimoto, A. Dillin, J. Kelly, William E. Balch. Annual Review of Biochemistry, 2009

1,170 citations recorded by the source corpus.

Subfields: Cell Biology, Epidemiology, Genetics

View Paper: https://www.semanticscholar.org/paper/6060f785e1fabab9cf45c2589bdb5e5f3ead0e33

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Citations in the corpus

Pathways of cellular proteostasis in aging and disease (2018, background): “The PN has previously been proposed to consist of ∼1,000–1,400 components on the basis of our initial understanding of its organization (Balch et al., 2008; Powers et al., 2009; Kim et al., 2013; Hipp et al., 2014).”
Heat shock factors: integrators of cell stress, development and lifespan (2010, background): “HSFs as stress integrators A hallmark of stressed cells and organisms is the increased synthesis of HSPs, which function as molecular chaperones to prevent protein misfolding and aggregation to maintain protein homeostasis, also called proteostasis”
In vivo aspects of protein folding and quality control (2016, background): “Thus, boosting PN capacity may be beneficial in both loss-of-function and gain-of-toxic function diseases of protein misfolding (170).”
Cellular strategies for controlling protein aggregation (2010, background): “A proper balance between these protein quality-control components is required for protein homeostasis, also referred to as proteostasi”
Pathogenic Protein Seeding in Alzheimer’s Disease and Other Neurodegenerative Disorders (2011, background): “Advancing age is the most prevalent risk factor for the accumulation of Ab in the brain,(10,11) possibly because of the decline of cellular protein quality control processes.(12) All firmly established genetic risk factors for AD promote the buildup of Ab, either by increasing its production, promot”
The hallmarks of aging. (2013, background): “Loss of Proteostasis Aging and some aging-related diseases are linked to impaired protein homeostasis or proteostasis (Powers et al., 2009) (Figure 3).”
Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade. (2017, neutral): “3D structure of Alzheimer’s amyloid-β(1-42) fibrils.”
Molecular chaperones in protein folding and proteostasis (2011, background): “Proteostasis is achieved by an integrated network of several hundred protein”