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… (More)
National Institutes of Health

Topic mentions per year

Topic mentions per year

1988-2018
020406019882018

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
Highly Cited
2005
Highly Cited
2005
The E. coli chaperonin GroEL and its cofactor GroES promote protein folding by sequestering nonnative polypeptides in a cage-like… (More)
  • figure 1
  • figure 2
  • figure 3
  • figure 4
  • figure 5
Is this relevant?
Highly Cited
2004
Highly Cited
2004
Type I chaperonins are molecular chaperones present in virtually all bacteria, some archaea and the plastids and mitochondria of… (More)
Is this relevant?
Highly Cited
2002
Highly Cited
2002
Cells respond to a wide variety of stresses through the transcriptional activation of genes that harbour stress elements within… (More)
  • figure 1
  • figure 2
  • figure 3
  • figure 4
  • figure 5
Is this relevant?
Highly Cited
2001
Highly Cited
2001
The GroEL/GroES chaperonin system mediates the folding of a range of newly synthesized polypeptides in the bacterial cytosol… (More)
  • figure 1
  • figure 2
  • figure 3
  • figure 5
  • table 1
Is this relevant?
Highly Cited
1999
Highly Cited
1999
The chaperonin GroEL has an essential role in mediating protein folding in the cytosol of Escherichia coli. Here we show that… (More)
  • figure 1
  • figure 2
  • figure 3
  • figure 4
  • figure 5
Is this relevant?
Highly Cited
1998
Highly Cited
1998
We describe the discovery of a heterohexameric chaperone protein, prefoldin, based on its ability to capture unfolded actin… (More)
  • table 1
  • figure 2
  • figure 3
  • figure 4
  • figure 5
Is this relevant?
Highly Cited
1997
Highly Cited
1997
Chaperonins assist protein folding with the consumption of ATP. They exist as multi-subunit protein assemblies comprising rings… (More)
Is this relevant?
Highly Cited
1994
Highly Cited
1994
Chaperonins are ring-shaped protein complexes that are essential in the cell, mediating ATP-dependent polypeptide folding in a… (More)
Is this relevant?
Highly Cited
1994
Highly Cited
1994
The crystal structure of Escherichia coli GroEL shows a porous cylinder of 14 subunits made of two nearly 7-fold rotationally… (More)
Is this relevant?
Highly Cited
1989
Highly Cited
1989
In vitro reconstitution of active ribulose bisphosphate carboxylase (Rubisco) from unfolded polypeptides is facilitated by the… (More)
Is this relevant?