Protein degradation and protection against misfolded or damaged proteins

By A. Goldberg. Nature, 2003

2,148 citations recorded by the source corpus.

Subfields: Cell Biology, Epidemiology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/c92c223df1bea64364570428562e13b1a5eb6567

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Citations in the corpus

Protein degradation by the ubiquitin-proteasome pathway in normal and disease states. (2006, background): “peptide bonds are cleaved by the hydroxyl group on a critical threonine residue (45).”
The Concept of Synthetic Lethality in the Context of Anticancer Therapy (2005, background): “The accumulation of mutated and/or misfolded proteins might also alter the requirement of a cell for proteasomal functio”
Autophagy, amyloidogenesis and Alzheimer disease (2007, background): “Complementing the proteasome’s role in the turnover of short-lived nuclear and cytosolic proteins (Goldberg, 2003), autophagy is most important for degrading long-lived proteins and is solely responsible for turnover of organelles and protein complexes that are too big to pass through the…”
Missense meanderings in sequence space: a biophysical view of protein evolution (2005, background): “However, misfolded or abnormal proteins are also selectively targeted for degradatio”
Ubiquitination and selective autophagy (2012, background): “, oxidative stress, heat shock).(10) Misfolded proteins severely impair cellular physiology, as exposed hydrophobic”
Impairment of starvation-induced and constitutive autophagy in Atg7-deficient mice (2005, background): “It plays crucial roles in selective degradation of not only short-lived regulatory proteins but also abnormal proteins that should be eliminated from the cells (Goldberg, 2003).”
Constitutive expression of a stress-inducible heat shock protein gene, hsp70, in phylogenetically distant Antarctic fish (2005, neutral): “More specifically, the unique thermal history of these fish allows us to investigate the relationship between extreme cold temperatures and the expression of genes pivotal to maintaining protein homeostasis through protein triaging—genes such as those encoding for molecular chaperones, ubiquitin, an”
Homeostatic levels of p62 control cytoplasmic inclusion body formation in autophagy-deficient mice. (2007, background): “p62 Handles Formation of Cytoplasmic Inclusions While there is ample evidence that dysfunction of the ubiquitin-proteasome system leads to the formation of ubiquitin-positive inclusions, which are the pathological hallmark of various neurodegenerative diseases (Goldberg, 2003), suppression of autoph”
Divorcing ARF and p53: an unsettled case (2006, background): “Therefore, the ARF protein assumes a stable structure when bound to NPM, whereas unbound mutant forms remain unstructured and, like many misfolded protein”