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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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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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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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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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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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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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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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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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Global Aggregation of Newly Translated Proteins in an Escherichia coli Strain Deficient of the Chaperonin GroEL

Proceedings of the National Academy of Sciences - PNAS, 2006-10, Vol.103 (43), p.15800-15805

2006

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Chaperonin-mediated protein folding: fate of substrate polypeptide

Quarterly reviews of biophysics, 2003-05, Vol.36 (2), p.229-256

2003

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Folding trajectories of human dihydrofolate reductase inside the GroEL-GroES chaperonin cavity and free in solution

Proceedings of the National Academy of Sciences - PNAS, 2007-12, Vol.104 (52), p.20788-20792

2007

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Perturbed ATPase Activity and Not "Close Confinement" of Substrate in the Cis Cavity Affects Rates of Folding by Tail-Multiplied GroEL

Proceedings of the National Academy of Sciences - PNAS, 2007-03, Vol.104 (13), p.5342-5347

2007

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Hsp110 mitigates α-synuclein pathology in vivo

Proceedings of the National Academy of Sciences - PNAS, 2019-11, Vol.116 (48), p.24310-24316

2019

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STRUCTURE AND FUNCTION IN GroEL-MEDIATED PROTEIN FOLDING

Annual review of biochemistry, 1998-01, Vol.67 (1), p.581-608

1998

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Requirement for binding multiple ATPs to convert a GroEL ring to the folding-active state

Proceedings of the National Academy of Sciences - PNAS, 2008-12, Vol.105 (49), p.19205-19210

2008

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Substrate Polypeptide Presents a Load on the Apical Domains of the Chaperonin GroEL

Proceedings of the National Academy of Sciences - PNAS, 2004-10, Vol.101 (42), p.15005-15012

2004

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

Nature (London), 1997-08, Vol.388 (6644), p.792-798

1997

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GroEL−GroES-Mediated Protein Folding

Chemical reviews, 2006-05, Vol.106 (5), p.1917-1930

2006

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ClpA Mediates Directional Translocation of Substrate Proteins into the ClpP Protease

Proceedings of the National Academy of Sciences - PNAS, 2001-03, Vol.98 (7), p.3768-3772

2001

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Transfer of pathogenic and nonpathogenic cytosolic proteins between spinal cord motor neurons in vivo in chimeric mice

Proceedings of the National Academy of Sciences - PNAS, 2017-04, Vol.114 (15), p.E3139-E3148

2017

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

Cell, 1996-02, Vol.84 (3), p.481-490

1996

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Chaperonin-assisted protein folding: a chronologue

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

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

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

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

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

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

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

Global Aggregation of Newly Translated Proteins in an Escherichia coli Strain Deficient of the Chaperonin GroEL

Chaperonin-mediated protein folding: fate of substrate polypeptide

Folding trajectories of human dihydrofolate reductase inside the GroEL-GroES chaperonin cavity and free in solution

Perturbed ATPase Activity and Not "Close Confinement" of Substrate in the Cis Cavity Affects Rates of Folding by Tail-Multiplied GroEL

Hsp110 mitigates α-synuclein pathology in vivo

STRUCTURE AND FUNCTION IN GroEL-MEDIATED PROTEIN FOLDING

Requirement for binding multiple ATPs to convert a GroEL ring to the folding-active state

Substrate Polypeptide Presents a Load on the Apical Domains of the Chaperonin GroEL

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

GroEL−GroES-Mediated Protein Folding

ClpA Mediates Directional Translocation of Substrate Proteins into the ClpP Protease

Transfer of pathogenic and nonpathogenic cytosolic proteins between spinal cord motor neurons in vivo in chimeric mice

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

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