GroEL Protein

Known as: GroEL Stress Protein 
A chaperonin 60 heat-shock protein isolated from bacteria.
National Institutes of Health

Topic mentions per year

Topic mentions per year

1988-2016
02419882016

Papers overview

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2006
2006
Electron cryomicroscopy reveals an unprecedented conformation of the single-ring mutant of GroEL (SR398) bound to GroES in the… (More)
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2004
2004
The expression of mouse CYP27B1 in Escherichia coli has been dramatically enhanced by coexpression of GroEL/ES. To reveal the… (More)
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2003
2003
Nucleotide regulates the affinity of the bacterial chaperonin GroEL for protein substrates. GroEL binds protein substrates with… (More)
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2003
2003
GroEL assists protein folding by preventing the interaction of partially folded molecules with other non-native proteins. It… (More)
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2000
2000
Luteoviruses avoid degradation in the hemolymph of their aphid vector by interacting with a GroEL homolog from the aphid's… (More)
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Highly Cited
1999
Highly Cited
1999
Evidence for the involvement of a Bemisia tabaci GroEL homologue in the transmission of tomato yellow leaf curl geminivirus… (More)
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1998
1998
Fragments encompassing the apical domain of GroEL, called minichaperones, facilitate the refolding of several proteins in vitro… (More)
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1998
1998
The ATPase cycle of GroE chaperonins has been examined by transient kinetics to dissect partial reactions in complexes where… (More)
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1997
1997
GroE, the chaperonin system of Escherichia coli, prevents the aggregation of partially folded or misfolded proteins by complexing… (More)
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1988
1988
It has been suggested that newly synthesized proteins are maintained in their unfolded state by cellular ATP-driven factors which… (More)
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