Vulnerability of newly synthesized proteins to proteostasis stress
نویسندگان
چکیده
منابع مشابه
Vulnerability of newly synthesized proteins to proteostasis stress.
The capacity of the cell to produce, fold and degrade proteins relies on components of the proteostasis network. Multiple types of insults can impose a burden on this network, causing protein misfolding. Using thermal stress, a classic example of acute proteostatic stress, we demonstrate that ∼5-10% of the soluble cytosolic and nuclear proteome in human HEK293 cells is vulnerable to misfolding ...
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Universitä t Freiburg with the analysis of folding of specific endogenous proteins in mutant strains, these studies have led to signifi-Hermann Herder Str. 7 D-79104 Freiburg cant advances in our understanding of protein folding in the complex cellular milieu. Germany Nascent chains emerging at the peptide exit tunnel of Madison, Wisconsin 53706 the ribosome are awaited by a welcoming committee...
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The way in which a newly synthesized polypeptide chain folds into its unique three-dimensional structure remains one of the fundamental questions in molecular biology. Protein folding in the cell is a problematic process and, in many cases, requires the assistance of a network of molecular chaperones to support productive protein foldingin vivo. During protein biosynthesis, ribosome-associated ...
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ژورنال
عنوان ژورنال: Journal of Cell Science
سال: 2016
ISSN: 1477-9137,0021-9533
DOI: 10.1242/jcs.176479