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Keyword

GroEL

Description: GroEL is a bacterial molecular chaperonin that assists protein folding and assembly, and is studied in biochemistry and microbiology.
Wikidata ID: wiki/Q14864994
OpenAlex ID: keywords/groel
The crystal structure of the bacterial chaperonln GroEL at 2.8 Å
1994 · Kerstin Braig, Zbyszek Otwinowski, et al. · Nature · 1,321
Homologous plant and bacterial proteins chaperone oligomeric protein assembly
1988 · Sean M. Hemmingsen, Carol Woolford, et al. · Nature · 1,283
The crystal structure of the asymmetric GroEL–GroES–(ADP)7 chaperonin complex
1997 · Zhaohui Xu, Arthur L. Horwich, et al. · Nature · 1,239
Chaperone-Mediated Protein Folding
1999 · Anthony L. Fink · Physiological Reviews · 1,054
Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding
1992 · Thomas Langer, Chi Lu, et al. · Nature · 953
Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria
1989 · Ming Y. Cheng, F.-Ulrich Hartl, et al. · Nature · 952
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Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate
1991 · Jörg Martin, Thomas Langer, et al. · Nature · 854
GroE heat-shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli
1989 · Pierre Goloubinoff, Anthony A. Gatenby, et al. · Nature · 708
The groES and groEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperatures
1989 · O Fayet, T Ziegelhoffer, et al. · Journal of Bacteriology · 705
Proteome-wide Analysis of Chaperonin-Dependent Protein Folding in Escherichia coli
2005 · Michael J. Kerner, Dean J. Naylor, et al. · Cell · 659
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Residues in chaperonin GroEL required for polypeptide binding and release
1994 · Wayne A. Fenton, Yechezkel Kashi, et al. · Nature · 639
An Enhanced System for Unnatural Amino Acid Mutagenesis in E. coli
2009 · Travis S. Young, Insha Ahmad, et al. · Journal of Molecular Biology · 638
STRUCTURE AND FUNCTION IN GroEL-MEDIATED PROTEIN FOLDING
1998 · Paul B. Sigler, Zhaohui Xu, et al. · Annual Review of Biochemistry · 572
Identification of in vivo substrates of the chaperonin GroEL
1999 · Walid A. Houry, Dmitrij Frishman, et al. · Nature · 504
The heat shock response of Escherichia coli
2000 · Florence Arsène, Toshifumi Tomoyasu, et al. · International Journal of Food Microbiology · 502
Trigger factor and DnaK cooperate in folding of newly synthesized proteins
1999 · Elke Deuerling, Agnes Schulze-Specking, et al. · Nature · 501
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GroE facilitates refolding of citrate synthase by suppressing aggregation
1991 · Johannes Buchner, Marion Schmidt, et al. · Biochemistry · 485
Mechanisms of protein folding
2001 · Viara Grantcharova, Eric J Alm, et al. · Current Opinion in Structural Biology · 474
Chemical Chaperones Regulate Molecular Chaperones in Vitro and in Cells under Combined Salt and Heat Stresses
2001 · Sophia Diamant, Noa Eliahu, et al. · Journal of Biological Chemistry · 461
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Dynamics of the Chaperonin ATPase Cycle: Implications for Facilitated Protein Folding
1994 · Matthew J. Todd, Paul V. Viitanen, et al. · Science · 457
The crystal structure of the GroES co-chaperonin at 2.8 Å resolution
1996 · John F. Hunt, Arthur J. Weaver, et al. · Nature · 435
Induction of Salmonella Stress Proteins Upon Infection of Macrophages
1990 · Nancy A. Buchmeier, Fred Heffron · Science · 428
Two Families of Chaperonin: Physiology and Mechanism
2007 · Arthur L. Horwich, Wayne A. Fenton, et al. · Annual Review of Cell and Developmental Biology · 422
Defining the TRiC/CCT interactome links chaperonin function to stabilization of newly made proteins with complex topologies
2008 · Alice Y Yam, Yu Xia, et al. · Nature Structural & Molecular Biology · 421
Mechanism of GroEL action: Productive release of polypeptide from a sequestered position under groes
1995 · Jonathan S. Weissman, Corinne M. Hohl, et al. · Cell · 420
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Works count: 4,300
Citation count: 139,400
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