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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

Related topics

Related topics

15 relations

Narrower (5)

Hsp16.3 protein, Mycobacterium tuberculosisPSMG2 protein, humanSymL protein, BacteriaTpCCTeta protein, Tetrahymena pyriformis
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In BloodMolecular ChaperonesProcess of secretionagonists
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Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
Highly Cited
2012
Highly Cited
2012
ATP-Triggered Conformational Changes Delineate Substrate-Binding and -Folding Mechanics of the GroEL Chaperonin
The chaperonin GroEL assists the folding of nascent or stress-denatured polypeptides by actions of binding and encapsulation. ATP… Expand
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Review
2009
Review
2009
Production of recombinant proteins by microbes and higher organisms.
Large proteins are usually expressed in a eukaryotic system while smaller ones are expressed in prokaryotic systems. For proteins… Expand
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Highly Cited
2007
Highly Cited
2007
A genome-wide association study of global gene expression
We have created a global map of the effects of polymorphism on gene expression in 400 children from families recruited through a… Expand
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Highly Cited
2003
Highly Cited
2003
Chaperonins govern growth of Escherichia coli at low temperatures
Sabine Louët responds: In researching the news story, I had several interviews with Huub Schellekens, who explained to me the key… Expand
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Review
2002
Review
2002
Molecular chaperones in the cytosol: from nascent chain to folded protein.
Efficient folding of many newly synthesized proteins depends on assistance from molecular chaperones, which serve to prevent… Expand
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Review
1995
Review
1995
Genetics, physiology, and evolutionary relationships of the genus Buchnera: intracellular symbionts of aphids.
Evolutionary studies suggest that 200-250 million years ago an aphid ancestor was infected with a free-living eubacterium. The… Expand
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Highly Cited
1991
Highly Cited
1991
Folding of influenza hemagglutinin in the endoplasmic reticulum
The folding of influenza hemagglutinin (HA0) in the ER was analyzed in tissue culture cells by following the formation of… Expand
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Highly Cited
1991
Highly Cited
1991
Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate
Folding of two monomeric enzymes mediated by groE has been reconstituted in vitro. The groEL protein stabilizes the polypeptides… Expand
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Highly Cited
1990
Highly Cited
1990
Requirement for hsp70 in the mitochondrial matrix for translocation and folding of precursor proteins
By analysis of a temperature-sensitive yeast mutant, a heat-shock protein in the matrix of mitochondria, mitochondrial hsp70… Expand
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Highly Cited
1988
Highly Cited
1988
Homologous plant and bacterial proteins chaperone oligomeric protein assembly
An abundant chloroplast protein is implicated in the assembly of the oligomeric enzyme ribulose bisphosphate carboxylase… Expand
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