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Chaperone (protein) - Wikipedia
Some chaperone systems work as foldases: they support the folding of proteins in an ATP-dependent manner (for example, the GroEL / GroES or the DnaK / DnaJ / GrpE system). Although most newly synthesized proteins can fold in absence of chaperones, a minority strictly requires them for the same. See more
In molecular biology, molecular chaperones are proteins that assist the conformational folding or unfolding of large proteins or macromolecular protein complexes. There are a number of classes of molecular … See more
In human cell lines, chaperone proteins were found to compose ~10% of the gross proteome mass, and are ubiquitously and highly expressed … See more
The genes of bacteriophage (phage) T4 that encode proteins with a role in determining phage T4 structure were identified using conditional lethal mutants. Most of these … See more
There are many disorders associated with mutations in genes encoding chaperones (i.e. multisystem proteinopathy) that can affect muscle, bone … See more
Many chaperones are heat shock proteins, that is, proteins expressed in response to elevated temperatures or other cellular stresses. Heat shock … See more
The investigation of chaperones has a long history. The term "molecular chaperone" appeared first in the literature in 1978, and was invented by Ron Laskey to describe the ability … See more
Wikipedia text under CC-BY-SA license Molecular chaperones and protein quality control: an introduction …
The Hsp70 chaperone network | Nature Reviews …
WEBJun 28, 2019 · The Hsp70 chaperones regulate protein metabolism, including folding, unfolding, subcellular localization, …
- Author: Rina Rosenzweig, Nadinath B. Nillegoda, Matthias P. Mayer, Bernd Bukau, Bernd Bukau
- Publish Year: 2019
- Studies of companion vs chaperone proteins
Multiple functionalities of molecular chaperones revealed through ...
Chaperone machines for protein folding, unfolding and …
WEBSep 12, 2013 · Chaperones are heavy-duty molecular machines that assist nascent proteins to reach their native fold but also mediate unfolding and prevent the accumulation of toxic protein aggregates.
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