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Chaperonin-assisted protein folding: a chronologue

Quarterly reviews of biophysics, 2020-01, Vol.53, p.e4-e4, Article e4

2020

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ATP-Triggered Conformational Changes Delineate Substrate-Binding and -Folding Mechanics of the GroEL Chaperonin

Cell, 2012-03, Vol.149 (1), p.113-123

2012

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Structure and Allostery of the Chaperonin GroEL

Journal of molecular biology, 2013-05, Vol.425 (9), p.1476-1487

2013

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Extended survival of misfolded G85R SOD1-linked ALS mice by transgenic expression of chaperone Hsp110

Proceedings of the National Academy of Sciences - PNAS, 2016-05, Vol.113 (19), p.5424-5428

2016

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Two families of chaperonin: physiology and mechanism

Annual review of cell and developmental biology, 2007-01, Vol.23 (1), p.115-145

2007

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Chaperonin-mediated protein folding: using a central cavity to kinetically assist polypeptide chain folding

Quarterly reviews of biophysics, 2009-05, Vol.42 (2), p.83-116

2009

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Selective degeneration of a physiological subtype of spinal motor neuron in mice with SOD1-linked ALS

Proceedings of the National Academy of Sciences - PNAS, 2014-11, Vol.111 (47), p.16883-16888

2014

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RNA-Seq profiling of spinal cord motor neurons from a presymptomatic SOD1 ALS mouse

PloS one, 2013-01, Vol.8 (1), p.e53575-e53575

2013

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Recessive loss of function of the neuronal ubiquitin hydrolase UCHL1 leads to early-onset progressive neurodegeneration

Proceedings of the National Academy of Sciences - PNAS, 2013-02, Vol.110 (9), p.3489-3494

2013

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Absence of lipofuscin in motor neurons of SOD1-linked ALS mice

Proceedings of the National Academy of Sciences - PNAS, 2014-07, Vol.111 (30), p.11055-11060

2014

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An ALS-linked mutant SOD1 produces a locomotor defect associated with aggregation and synaptic dysfunction when expressed in neurons of Caenorhabditis elegans

PLoS genetics, 2009-01, Vol.5 (1), p.e1000350

2009

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Chaperonin chamber accelerates protein folding through passive action of preventing aggregation

Proceedings of the National Academy of Sciences - PNAS, 2008-11, Vol.105 (45), p.17351-17355

2008

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The GroEL/GroES cis cavity as a passive anti-aggregation device

FEBS letters, 2009-08, Vol.583 (16), p.2654-2662

2009

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Loops in the Central Channel of ClpA Chaperone Mediate Protein Binding, Unfolding, and Translocation

Cell, 2005-07, Vol.121 (7), p.1029-1041

2005

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Molecular chaperone Hsp110 rescues a vesicle transport defect produced by an ALS-associated mutant SOD1 protein in squid axoplasm

Proceedings of the National Academy of Sciences - PNAS, 2013-04, Vol.110 (14), p.5428-5433

2013

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Molecular chaperones in cellular protein folding: the birth of a field

Cell, 2014-04, Vol.157 (2), p.285-288

Horwich, Arthur L

2014

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NMR analysis of a 900K GroEL-GroES complex

Nature (London), 2002-07, Vol.418 (6894), p.207-211

2002

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Progressive aggregation despite chaperone associations of a mutant SOD1-YFP in transgenic mice that develop ALS

Proceedings of the National Academy of Sciences - PNAS, 2009-02, Vol.106 (5), p.1392-1397

2009

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

Nature (London), 1997-08, Vol.388 (6644), p.741-750

1997

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Translational Diffusion of Macromolecular Assemblies Measured Using Transverse-Relaxation-Optimized Pulsed Field Gradient NMR

Journal of the American Chemical Society, 2011-10, Vol.133 (41), p.16354-16357

2011

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Allosteric signaling of ATP hydrolysis in GroEL-GroES complexes

Nature structural & molecular biology, 2006-02, Vol.13 (2), p.147-152

2006

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Chaperonin studies: faith, luck, and a little help from our friends

Molecular biology of the cell, 2017-11, Vol.28 (22), p.2915-2918

Horwich, Arthur L

2017

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ClpS, a Substrate Modulator of the ClpAP Machine

Molecular cell, 2002-03, Vol.9 (3), p.673-683

2002

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GroEL/GroES cycling: ATP binds to an open ring before substrate protein favoring protein binding and production of the native state

Proceedings of the National Academy of Sciences - PNAS, 2009-12, Vol.106 (48), p.20264-20269

2009

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Double mutant MBP refolds at same rate in free solution as inside the GroEL/GroES chaperonin chamber when aggregation in free solution is prevented

FEBS letters, 2011-06, Vol.585 (12), p.1969-1972

2011

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Chaperonin-assisted protein folding: a chronologue

ATP-Triggered Conformational Changes Delineate Substrate-Binding and -Folding Mechanics of the GroEL Chaperonin

Structure and Allostery of the Chaperonin GroEL

Extended survival of misfolded G85R SOD1-linked ALS mice by transgenic expression of chaperone Hsp110

Two families of chaperonin: physiology and mechanism

Chaperonin-mediated protein folding: using a central cavity to kinetically assist polypeptide chain folding

Selective degeneration of a physiological subtype of spinal motor neuron in mice with SOD1-linked ALS

RNA-Seq profiling of spinal cord motor neurons from a presymptomatic SOD1 ALS mouse

Recessive loss of function of the neuronal ubiquitin hydrolase UCHL1 leads to early-onset progressive neurodegeneration

Absence of lipofuscin in motor neurons of SOD1-linked ALS mice

An ALS-linked mutant SOD1 produces a locomotor defect associated with aggregation and synaptic dysfunction when expressed in neurons of Caenorhabditis elegans

Chaperonin chamber accelerates protein folding through passive action of preventing aggregation

The GroEL/GroES cis cavity as a passive anti-aggregation device

Loops in the Central Channel of ClpA Chaperone Mediate Protein Binding, Unfolding, and Translocation

Molecular chaperone Hsp110 rescues a vesicle transport defect produced by an ALS-associated mutant SOD1 protein in squid axoplasm

Molecular chaperones in cellular protein folding: the birth of a field

NMR analysis of a 900K GroEL-GroES complex

Progressive aggregation despite chaperone associations of a mutant SOD1-YFP in transgenic mice that develop ALS

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

Translational Diffusion of Macromolecular Assemblies Measured Using Transverse-Relaxation-Optimized Pulsed Field Gradient NMR

Allosteric signaling of ATP hydrolysis in GroEL-GroES complexes

Chaperonin studies: faith, luck, and a little help from our friends

ClpS, a Substrate Modulator of the ClpAP Machine

GroEL/GroES cycling: ATP binds to an open ring before substrate protein favoring protein binding and production of the native state

Double mutant MBP refolds at same rate in free solution as inside the GroEL/GroES chaperonin chamber when aggregation in free solution is prevented

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