Keyword

GroES

Description: A co-chaperonin protein that binds GroEL and assists the ATP-dependent folding of proteins in bacteria and other organisms.

Primary topic: Heat shock proteins research (68%)

Related topic: Heat shock proteins research (68%)

Wikidata ID: wiki/Q14865007

OpenAlex ID: keywords/groes

The crystal structure of the asymmetric GroEL–GroES–(ADP)7 chaperonin complex

1997 · Zhaohui Xu, Arthur L. Horwich, et al. · Nature · 1,239

A mitochondrial specific stress response in mammalian cells

2002 · Quan Zhao, Jianghui Wang, et al. · The EMBO Journal · 1,026

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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

Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and Mg-ATP

1989 · Pierre Goloubinoff, John T. Christeller, et al. · Nature · 737

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

STRUCTURE AND FUNCTION IN GroEL-MEDIATED PROTEIN FOLDING

1998 · Paul B. Sigler, Zhaohui Xu, et al. · Annual Review of Biochemistry · 572

The heat shock response of Escherichia coli

2000 · Florence Arsène, Toshifumi Tomoyasu, et al. · International Journal of Food Microbiology · 502

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

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

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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Purification and properties of groE, a host protein involved in bacteriophage assembly

1979 · Roger W. Hendrix · Journal of Molecular Biology · 417

Chaperonin‐mediated protein folding: GroES binds to one end of the GroEL cylinder, which accommodates the protein substrate within its central cavity.

1992 · T. Langer, G. Pfeifer, et al. · The EMBO Journal · 414

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Function in protein folding of TRiC, a cytosolic ring complex containing TCP‐1 and structurally related subunits.

1992 · J. Frydman, E. Nimmesgern, et al. · The EMBO Journal · 413

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The GroEL–GroES Chaperonin Machine: A Nano-Cage for Protein Folding

2015 · Manajit Hayer-Hartl, Andreas Bracher, et al. · Trends in Biochemical Sciences · 404

Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL

1997 · Hays S. Rye, Steven G. Burston, et al. · Nature · 404

Characterization of the Active Intermediate of a GroEL–GroES-Mediated Protein Folding Reaction

1996 · Jonathan S Weissman, Hays S Rye, et al. · Cell · 395

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NMR analysis of a 900K GroEL–GroES complex

2002 · Jocelyne Fiaux, Eric B. Bertelsen, et al. · Nature · 386

The Chaperonin ATPase Cycle: Mechanism of Allosteric Switching and Movements of Substrate-Binding Domains in GroEL

1996 · Alan M Roseman, Shaoxia Chen, et al. · Cell · 381

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Chaperonin-facilitated refolding of ribulose bisphosphate carboxylase and ATP hydrolysis by chaperonin 60 (groEL) are potassium dependent

1990 · Paul V. Viitanen, Thomas H. Lubben, et al. · Biochemistry · 380

Protein folding in the central cavity of the GroEL–GroES chaperonin complex

1996 · Mark Mayhew, Ana C. R. da Silva, et al. · Nature · 374

Works count: 1,724

Citation count: 62,510