Chaperonin 10

Known as: Heat Shock Protein 10, Heat Shock Proteins 10, Heat-Shock Protein 10 
A group I chaperonin protein that forms a lid-like structure which encloses the non-polar cavity of the chaperonin complex. The protein was… (More)
National Institutes of Health

Topic mentions per year

Topic mentions per year

1990-2018
0519902018

Papers overview

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2006
2006
Mcm10 is a conserved eukaryotic DNA replication factor that is required for S phase progression. Recently, Mcm10 has been shown… (More)
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2006
2006
BACKGROUND Chaperonin 10 (heat shock protein 10, XToll) has anti-inflammatory properties related to the inhibition of Toll-like… (More)
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2005
2005
Heat shock protein 10 (Hsp10) and heat shock protein 60 (Hsp60) were originally described as essential mitochondrial proteins… (More)
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Highly Cited
2004
Highly Cited
2004
It is recognized that monoamine reuptake inhibitors (MARIs) exert beneficial effects in the treatment of major depression and… (More)
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2003
2003
Type I chaperonins are fundamental protein folding machineries that function in eubacteria, mitochondria and chloroplasts… (More)
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2000
2000
Calcium regulates diverse cellular activities in plants through the action of calmodulin (CaM). By using (35)S-labeled CaM to… (More)
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1994
1994
Early-pregnancy factor (EPF), first discovered in the early stages of gestation, is associated with and necessary for cell… (More)
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1992
1992
Chaperonins are thought to participate in the process of protein folding in bacteria and in eukaryotic mitochondria and… (More)
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1991
1991
In vitro refolding of the monomeric mitochondrial enzyme, rhodanese (thiosulfate sulfurtransferase; EC 2.8.1.1) is facilitated by… (More)
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Highly Cited
1990
Highly Cited
1990
Both the chaperonin- and MgATP-dependent reconstitution of unfolded ribulosebisphosphate carboxylase (Rubisco) and the uncoupled… (More)
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