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GroEL Protein
Known as:
GroEL Stress Protein
A chaperonin 60 heat-shock protein isolated from bacteria.
National Institutes of Health
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Related topics
Related topics
2 relations
Broader (2)
Chaperonin 60
Molecular Chaperones
Papers overview
Semantic Scholar uses AI to extract papers important to this topic.
Highly Cited
2013
Highly Cited
2013
Protein quality control acts on folding intermediates to shape the effects of mutations on organismal fitness.
S. Bershtein
,
W. Mu
,
Adrian W. R. Serohijos
,
Jingwen Zhou
,
E. Shakhnovich
Molecules and Cells
2013
Corpus ID: 3681390
Highly Cited
2007
Highly Cited
2007
An essential role for the DnaK molecular chaperone in stabilizing over-expressed substrate proteins of the bacterial twin-arginine translocation pathway.
R. Pérez-Rodríguez
,
Adam C. Fisher
,
+6 authors
M. DeLisa
Journal of Molecular Biology
2007
Corpus ID: 23878295
Highly Cited
2007
Highly Cited
2007
Making a friend from a foe: expressing a GroEL gene from the whitefly Bemisia tabaci in the phloem of tomato plants confers resistance to tomato yellow leaf curl virus
F. Akad
,
A. Eybishtz
,
+4 authors
H. Czosnek
Archives of Virology
2007
Corpus ID: 5798407
SummarySome (perhaps all) plant viruses transmitted in a circulative manner by their insect vectors avoid destruction in the…
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Highly Cited
2006
Highly Cited
2006
GroES/GroEL and DnaK/DnaJ Have Distinct Roles in Stress Responses and during Cell Cycle Progression in Caulobacter crescentus
M. F. Susin
,
R. Baldini
,
Frederico J. Gueiros-Filho
,
S. Gomes
Journal of Bacteriology
2006
Corpus ID: 2669020
ABSTRACT Misfolding and aggregation of protein molecules are major threats to all living organisms. Therefore, cells have evolved…
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Highly Cited
2005
Highly Cited
2005
Coexpression of folding accessory proteins for production of active cyclodextrin glycosyltransferase of Bacillus macerans in recombinant Escherichia coli.
Sung-gun Kim
,
D. Kweon
,
Dae-Hee Lee
,
Yong-Cheol Park
,
Jin-Ho Seo
Protein Expression and Purification
2005
Corpus ID: 21891678
Highly Cited
2004
Highly Cited
2004
Transcriptional analysis of dynamic heat-shock response by the hyperthermophilic bacterium Thermotoga maritima
Marybeth Pysz
,
D. Ward
,
+4 authors
R. Kelly
Extremophiles
2004
Corpus ID: 8538758
AbstractThe thermal stress response of the hyperthermophilic bacterium Thermotoga maritima was characterized using a 407-open…
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2000
2000
Identifying the Determinants in the Equatorial Domain ofBuchnera GroEL Implicated in Binding Potato Leafroll Virus
S. Hogenhout
,
F. van der Wilk
,
M. Verbeek
,
R. Goldbach
,
J. van den Heuvel
Journal of Virology
2000
Corpus ID: 7982146
ABSTRACT Luteoviruses avoid degradation in the hemolymph of their aphid vector by interacting with a GroEL homolog from the aphid…
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1998
1998
Divalent Cations Can Induce the Exposure of GroEL Hydrophobic Surfaces and Strengthen GroEL Hydrophobic Binding Interactions
Bill T. Brazil
,
J. Ybarra
,
P. Horowitz
Journal of Biological Chemistry
1998
Corpus ID: 22486654
Fluorescent and non-fluorescent probes have been used to show that divalent cations (Ca2+, Mg2+, Mn2+, and Zn2+) significantly…
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Highly Cited
1988
Highly Cited
1988
Transient association of newly synthesized unfolded proteins with the heat-shock GroEL protein
E. Bochkareva
,
N. Lissin
,
A. Girshovich
Nature
1988
Corpus ID: 28202603
It has been suggested that newly synthesized proteins are maintained in their unfolded state by cellular ATP-driven factors which…
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Highly Cited
1988
Highly Cited
1988
The Mycobacterium tuberculosis 65-kilodalton antigen is a heat shock protein which corresponds to common antigen and to the Escherichia coli GroEL protein
T. Shinnick
,
Michael H. Vodkin
,
Jim C. Williams
Infection and Immunity
1988
Corpus ID: 13142915
Monoclonal hybridoma antibodies directed against a 65-kilodalton (kDa) mycobacterial protein could detect similarly sized…
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