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Symmetry, Rigidity, and Allosteric Signaling: From Monomeric Proteins to Molecular Machines

Chemical reviews, 2019-06, Vol.119 (12), p.6788-6821

2019

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Substrate protein switches GroE chaperonins from asymmetric to symmetric cycling by catalyzing nucleotide exchange

Proceedings of the National Academy of Sciences - PNAS, 2013-11, Vol.110 (46), p.E4289-E4297

2013

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Formation and structures of GroEL:GroES₂ chaperonin footballs, the protein-folding functional form

Proceedings of the National Academy of Sciences - PNAS, 2014-09, Vol.111 (35), p.12775-12780

2014

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Subunit conformational variation within individual GroEL oligomers resolved by Cryo-EM

Proceedings of the National Academy of Sciences - PNAS, 2017-08, Vol.114 (31), p.8259-8264

2017

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Symmetric GroEL:GroES₂ complexes are the protein-folding functional form of the chaperonin nanomachine

Proceedings of the National Academy of Sciences - PNAS, 2013-11, Vol.110 (46), p.E4298-E4305

2013

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A Helping Hand to Overcome Solubility Challenges in Chemical Protein Synthesis

Journal of the American Chemical Society, 2016-09, Vol.138 (36), p.11775-11782

2016

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Friends in need: How chaperonins recognize and remodel proteins that require folding assistance

Frontiers in molecular biosciences, 2022-11, Vol.9, p.1071168-1071168

2022

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Dynamics of Allosteric Transitions in GroEL

Proceedings of the National Academy of Sciences - PNAS, 2006-12, Vol.103 (50), p.18939-18944

2006

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Serum binding folate receptor autoantibodies lower in autistic boys and positively-correlated with folate

Biomedicine & pharmacotherapy, 2024-03, Vol.172, p.116191-116191, Article 116191

2024

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Measuring how much work the chaperone GroEL can do

Proceedings of the National Academy of Sciences - PNAS, 2013-07, Vol.110 (27), p.E2451-E2459

2013

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HemN2 Regulates the Virulence of Pseudomonas donghuensis HYS through 7-Hydroxytropolone Synthesis and Oxidative Stress

Biology (Basel, Switzerland), 2024-06, Vol.13 (6), p.373

2024

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Commentary: Directions for Optimization of Photosynthetic Carbon Fixation: RuBisCO's Efficiency May Not Be So Constrained After All

Frontiers in plant science, 2018-06, Vol.9 (929), p.929-929

2018

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Rubisco is not really so bad

Plant, cell and environment, 2018-04, Vol.41 (4), p.705-716

2018

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Iterative annealing mechanism explains the functions of the GroEL and RNA chaperones

Protein science, 2020-02, Vol.29 (2), p.360-377

2020

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Molecular chaperones maximize the native state yield on biological times by driving substrates out of equilibrium

Proceedings of the National Academy of Sciences - PNAS, 2017-12, Vol.114 (51), p.E10919-E10927

2017

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Chaperonin Function: Folding by Forced Unfolding

Science (American Association for the Advancement of Science), 1999-04, Vol.284 (5415), p.822-825

1999

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Redox and spectroscopic properties of mammalian nitrite reductase-like hemoproteins

Journal of inorganic biochemistry, 2022-12, Vol.237, p.111982-111982, Article 111982

2022

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Ribulose 1,5-bisphosphate carboxylase/oxygenase activates O₂ by electron transfer

Proceedings of the National Academy of Sciences - PNAS, 2020-09, Vol.117 (39), p.24234-24242

2020

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Setting the Chaperonin Timer: The Effects of K⁺ and Substrate Protein on ATP Hydrolysis

Proceedings of the National Academy of Sciences - PNAS, 2008-11, Vol.105 (45), p.17334-17338

2008

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Allostery and molecular machines

Philosophical transactions of the Royal Society of London. Series B. Biological sciences, 2018-06, Vol.373 (1749)

2018

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Setting the chaperonin timer: A two-stroke, two-speed, protein machine

Proceedings of the National Academy of Sciences - PNAS, 2008-11, Vol.105 (45), p.17339-17344

2008

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Neuropeptides affecting social behavior in mammals: Oxytocin

Peptides (New York, N.Y. : 1980), 2024-07, Vol.177, p.171223, Article 171223

2024

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Mechanism of Rubisco: The Carbamate as General Base

Chemical reviews, 1998-04, Vol.98 (2), p.549-562

1998

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The GroEL chaperonin: a protein machine with pistons driven by ATP binding and hydrolysis

Philosophical transactions of the Royal Society of London. Series B. Biological sciences, 2018-06, Vol.373 (1749)

2018

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Coupling between allosteric transitions in GroEL and assisted folding of a substrate protein

Proceedings of the National Academy of Sciences - PNAS, 2007-05, Vol.104 (21), p.8803-8808

2007

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Symmetry, Rigidity, and Allosteric Signaling: From Monomeric Proteins to Molecular Machines

Substrate protein switches GroE chaperonins from asymmetric to symmetric cycling by catalyzing nucleotide exchange

Formation and structures of GroEL:GroES₂ chaperonin footballs, the protein-folding functional form

Subunit conformational variation within individual GroEL oligomers resolved by Cryo-EM

Symmetric GroEL:GroES₂ complexes are the protein-folding functional form of the chaperonin nanomachine

A Helping Hand to Overcome Solubility Challenges in Chemical Protein Synthesis

Friends in need: How chaperonins recognize and remodel proteins that require folding assistance

Dynamics of Allosteric Transitions in GroEL

Serum binding folate receptor autoantibodies lower in autistic boys and positively-correlated with folate

Measuring how much work the chaperone GroEL can do

HemN2 Regulates the Virulence of Pseudomonas donghuensis HYS through 7-Hydroxytropolone Synthesis and Oxidative Stress

Commentary: Directions for Optimization of Photosynthetic Carbon Fixation: RuBisCO's Efficiency May Not Be So Constrained After All

Rubisco is not really so bad

Iterative annealing mechanism explains the functions of the GroEL and RNA chaperones

Molecular chaperones maximize the native state yield on biological times by driving substrates out of equilibrium

Chaperonin Function: Folding by Forced Unfolding

Redox and spectroscopic properties of mammalian nitrite reductase-like hemoproteins

Ribulose 1,5-bisphosphate carboxylase/oxygenase activates O₂ by electron transfer

Setting the Chaperonin Timer: The Effects of K⁺ and Substrate Protein on ATP Hydrolysis

Allostery and molecular machines

Setting the chaperonin timer: A two-stroke, two-speed, protein machine

Neuropeptides affecting social behavior in mammals: Oxytocin

Mechanism of Rubisco: The Carbamate as General Base

The GroEL chaperonin: a protein machine with pistons driven by ATP binding and hydrolysis

Coupling between allosteric transitions in GroEL and assisted folding of a substrate protein

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