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GroEL‐Mediated protein folding

Protein science, 1997-04, Vol.6 (4), p.743-760

1997

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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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Residues in chaperonin GroEL required for polypeptide binding and release

Nature (London), 1994-10, Vol.371 (6498), p.614-619

1994

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A Polypeptide Bound by the Chaperonin groEL is Localized Within a Central Cavity

Proceedings of the National Academy of Sciences - PNAS, 1993-05, Vol.90 (9), p.3978-3982

1993

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Hepadnavirus envelope proteins regulate covalently closed circular DNA amplification

Journal of Virology, 1990-06, Vol.64 (6), p.2819-2824

1990

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TCP1 complex is a molecular chaperone in tubulin biogenesis

Nature (London), 1992-07, Vol.358 (6383), p.245-248

1992

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Folding in vivo of bacterial cytoplasmic proteins: Role of GroEL

Cell, 1993-09, Vol.74 (5), p.909-917

1993

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Prevention of Protein Denaturation Under Heat Stress by the Chaperonin Hsp60

Science (American Association for the Advancement of Science), 1992-11, Vol.258 (5084), p.995-998

1992

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Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis

Nature (London), 1989-09, Vol.341 (6238), p.125-130

1989

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Release of both native and non-native proteins from a cis -only GroEL ternary complex

Nature (London), 1996-09, Vol.383 (6595), p.96-99

1996

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Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria

Nature (London), 1989-02, Vol.337 (6208), p.620-625

1989

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Global unfolding of a substrate protein by the Hsp100 chaperone ClpA

Nature (London), 1999-09, Vol.401 (6748), p.90-93

1999

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ATP-Bound States of GroEL Captured by Cryo-Electron Microscopy

Cell, 2001-12, Vol.107 (7), p.869-879

2001

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Linkage Mapping of a Mouse Gene, iv, that Controls Left-Right Asymmetry of the Heart and Viscera

Proceedings of the National Academy of Sciences - PNAS, 1989-07, Vol.86 (13), p.5035-5038

1989

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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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Deadly Conformations—Protein Misfolding in Prion Disease

Cell, 1997-05, Vol.89 (4), p.499-510

1997

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GroEL-GroES Cycling: ATP and Nonnative Polypeptide Direct Alternation of Folding-Active Rings

Cell, 1999-04, Vol.97 (3), p.325-338

1999

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Chaperone Rings in Protein Folding and Degradation

Proceedings of the National Academy of Sciences - PNAS, 1999-09, Vol.96 (20), p.11033-11040

1999

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GroEL/GroES-Mediated Folding of a Protein Too Large to Be Encapsulated

Cell, 2001-10, Vol.107 (2), p.235-246

2001

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Multivalent Binding of Nonnative Substrate Proteins by the Chaperonin GroEL

Cell, 2000-03, Vol.100 (5), p.561-573

2000

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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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Heat shock proteins and molecular chaperones: Mediators of protein conformation and turnover in the cell

Cell, 1994-08, Vol.78 (3), p.365-372

1994

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The mitochondrial chaperonin hsp60 is required for its own assembly

Nature (London), 1990-11, Vol.348 (6300), p.455-458

1990

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A leader peptide is sufficient to direct mitochondrial import of a chimeric protein

The EMBO journal, 1985-05, Vol.4 (5), p.1129-1135

1985

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Two related genes encoding extremely hydrophobic proteins suppress a lethal mutation in the yeast mitochondrial processing enhancing protein

The Journal of biological chemistry, 1992-12, Vol.267 (34), p.24625-24633

1992

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GroEL‐Mediated protein folding

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

Residues in chaperonin GroEL required for polypeptide binding and release

A Polypeptide Bound by the Chaperonin groEL is Localized Within a Central Cavity

Hepadnavirus envelope proteins regulate covalently closed circular DNA amplification

TCP1 complex is a molecular chaperone in tubulin biogenesis

Folding in vivo of bacterial cytoplasmic proteins: Role of GroEL

Prevention of Protein Denaturation Under Heat Stress by the Chaperonin Hsp60

Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis

Release of both native and non-native proteins from a cis -only GroEL ternary complex

Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria

Global unfolding of a substrate protein by the Hsp100 chaperone ClpA

ATP-Bound States of GroEL Captured by Cryo-Electron Microscopy

Linkage Mapping of a Mouse Gene, iv, that Controls Left-Right Asymmetry of the Heart and Viscera

STRUCTURE AND FUNCTION IN GroEL-MEDIATED PROTEIN FOLDING

Deadly Conformations—Protein Misfolding in Prion Disease

GroEL-GroES Cycling: ATP and Nonnative Polypeptide Direct Alternation of Folding-Active Rings

Chaperone Rings in Protein Folding and Degradation

GroEL/GroES-Mediated Folding of a Protein Too Large to Be Encapsulated

Multivalent Binding of Nonnative Substrate Proteins by the Chaperonin GroEL

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

Heat shock proteins and molecular chaperones: Mediators of protein conformation and turnover in the cell

The mitochondrial chaperonin hsp60 is required for its own assembly

A leader peptide is sufficient to direct mitochondrial import of a chimeric protein

Two related genes encoding extremely hydrophobic proteins suppress a lethal mutation in the yeast mitochondrial processing enhancing protein

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