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GroEL Protein

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

Papers overview

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Highly Cited
2013
Highly Cited
2013
What are the molecular properties of proteins that fall on the radar of protein quality control (PQC)? Here we mutate the E. coli… Expand
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Highly Cited
2006
Highly Cited
2006
Misfolding and aggregation of protein molecules are major threats to all living organisms. Therefore, cells have evolved quality… Expand
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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… Expand
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2003
2003
Nucleotide regulates the affinity of the bacterial chaperonin GroEL for protein substrates. GroEL binds protein substrates with… Expand
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Review
2001
Review
2001
Publisher Summary Chaperonins are large, double-ring complexes that assist the folding to native form of a wide variety of… Expand
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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… Expand
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Highly Cited
1997
Highly Cited
1997
Chaperonins assist protein folding with the consumption of ATP. They exist as multi-subunit protein assemblies comprising rings… Expand
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Highly Cited
1996
Highly Cited
1996
Recent studies of GroE-mediated protein folding indicate that substrate proteins are productively released from a cis ternary… Expand
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Highly Cited
1988
Highly Cited
1988
Monoclonal hybridoma antibodies directed against a 65-kilodalton (kDa) mycobacterial protein could detect similarly sized… Expand
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Highly Cited
1988
Highly Cited
1988
It has been suggested that newly synthesized proteins are maintained in their unfolded state by cellular ATP-driven factors which… Expand
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