FAQ

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

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Related topics

13 relations
In BloodMolecular ChaperonesProcess of secretionadministration & dosage
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Related mentions per year

Related mentions per year

1936-2018
19401960198020002020
chaperonin
physiological aspects
agonists
chemical synthesis
Molecular Chaperones
standards characteristics

Papers overview

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Highly Cited
2005
Highly Cited
2005
Proteome-wide Analysis of Chaperonin-Dependent Protein Folding in Escherichia coli
The E. coli chaperonin GroEL and its cofactor GroES promote protein folding by sequestering nonnative polypeptides in a cage-like… (More)
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Highly Cited
2004
Highly Cited
2004
cpnDB: a chaperonin sequence database.
Type I chaperonins are molecular chaperones present in virtually all bacteria, some archaea and the plastids and mitochondria of… (More)
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Highly Cited
2002
Highly Cited
2002
A mitochondrial specific stress response in mammalian cells.
Cells respond to a wide variety of stresses through the transcriptional activation of genes that harbour stress elements within… (More)
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Highly Cited
2001
Highly Cited
2001
Dual Function of Protein Confinement in Chaperonin-Assisted Protein Folding
The GroEL/GroES chaperonin system mediates the folding of a range of newly synthesized polypeptides in the bacterial cytosol… (More)
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Highly Cited
1999
Highly Cited
1999
Identification of in vivo substrates of the chaperonin GroEL.
The chaperonin GroEL has an essential role in mediating protein folding in the cytosol of Escherichia coli. Here we show that… (More)
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Highly Cited
1998
Highly Cited
1998
Prefoldin, a Chaperone that Delivers Unfolded Proteins to Cytosolic Chaperonin
We describe the discovery of a heterohexameric chaperone protein, prefoldin, based on its ability to capture unfolded actin… (More)
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Highly Cited
1997
Highly Cited
1997
The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex.
Chaperonins assist protein folding with the consumption of ATP. They exist as multi-subunit protein assemblies comprising rings… (More)
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Highly Cited
1994
Highly Cited
1994
Residues in chaperonin GroEL required for polypeptide binding and release.
Chaperonins are ring-shaped protein complexes that are essential in the cell, mediating ATP-dependent polypeptide folding in a… (More)
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Highly Cited
1994
Highly Cited
1994
The crystal structure of the bacterial chaperonin GroEL at 2.8 A.
The crystal structure of Escherichia coli GroEL shows a porous cylinder of 14 subunits made of two nearly 7-fold rotationally… (More)
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Highly Cited
1989
Highly Cited
1989
Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfoleded state depends on two chaperonin proteins and Mg-ATP.
In vitro reconstitution of active ribulose bisphosphate carboxylase (Rubisco) from unfolded polypeptides is facilitated by the… (More)
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