Skip to search formSkip to main content
You are currently offline. Some features of the site may not work correctly.

chaperonin

Known as: Chaperonin Family, Chaperonins, Chaperonins [Chemical/Ingredient] 
A family of multisubunit protein complexes that form into large cylindrical structures which bind to and encapsulate non-native proteins. Chaperonins… Expand
National Institutes of Health

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
Highly Cited
2012
Highly Cited
2012
The chaperonin GroEL assists the folding of nascent or stress-denatured polypeptides by actions of binding and encapsulation. ATP… Expand
  • figure 1
  • figure 2
  • figure 3
  • figure 4
  • figure 5
Is this relevant?
Review
2009
Review
2009
Large proteins are usually expressed in a eukaryotic system while smaller ones are expressed in prokaryotic systems. For proteins… Expand
  • table 1
  • table 2
  • table 3
  • table 4
  • table 5
Is this relevant?
Highly Cited
2007
Highly Cited
2007
We have created a global map of the effects of polymorphism on gene expression in 400 children from families recruited through a… Expand
  • table 2
  • figure 2
  • figure 3
  • table 1
  • figure 4
Is this relevant?
Highly Cited
2003
Highly Cited
2003
Sabine Louët responds: In researching the news story, I had several interviews with Huub Schellekens, who explained to me the key… Expand
  • figure 1
Is this relevant?
Review
2002
Review
2002
Efficient folding of many newly synthesized proteins depends on assistance from molecular chaperones, which serve to prevent… Expand
Is this relevant?
Review
1995
Review
1995
Evolutionary studies suggest that 200-250 million years ago an aphid ancestor was infected with a free-living eubacterium. The… Expand
Is this relevant?
Highly Cited
1991
Highly Cited
1991
The folding of influenza hemagglutinin (HA0) in the ER was analyzed in tissue culture cells by following the formation of… Expand
  • figure 1
  • figure 2
  • figure 3
  • figure 4
  • figure 5
Is this relevant?
Highly Cited
1991
Highly Cited
1991
Folding of two monomeric enzymes mediated by groE has been reconstituted in vitro. The groEL protein stabilizes the polypeptides… Expand
Is this relevant?
Highly Cited
1990
Highly Cited
1990
By analysis of a temperature-sensitive yeast mutant, a heat-shock protein in the matrix of mitochondria, mitochondrial hsp70… Expand
  • figure 1
  • figure 2
  • figure 3
  • figure 4
  • figure 5
Is this relevant?
Highly Cited
1988
Highly Cited
1988
An abundant chloroplast protein is implicated in the assembly of the oligomeric enzyme ribulose bisphosphate carboxylase… Expand
Is this relevant?