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Structural Analysis of Macromolecular Assemblies by Electron Microscopy

Chemical reviews, 2011-12, Vol.111 (12), p.7710-7748

2011

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Chaperonin complex with a newly folded protein encapsulated in the folding chamber

Nature, 2009-01, Vol.457 (7225), p.107-110

2009

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Dependence on solution conditions of aggregation and amyloid formation by an SH3 domain

Journal of molecular biology, 2001-08, Vol.311 (2), p.325-340

2001

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Structural Basis of Pore Formation by the Bacterial Toxin Pneumolysin

Cell, 2005-04, Vol.121 (2), p.247-256

2005

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Hsp26: a temperature-regulated chaperone

The EMBO journal, 1999-12, Vol.18 (23), p.6744-6751

1999

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Three conformations of an archaeal chaperonin, TF55 from Sulfolobus shibatae

Journal of molecular biology, 2000-02, Vol.296 (3), p.813-819

2000

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Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing

The EMBO journal, 1999-02, Vol.18 (4), p.815-821

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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A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state

The EMBO journal, 1997-02, Vol.16 (3), p.659-671

1997

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Conformational changes studied by cryo-electron microscopy

Nature structural & molecular biology, 2000-09, Vol.7 (9), p.711-714

Saibil, Helen R

2000

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ATP induces large quaternary rearrangements in a cage-like chaperonin structure

Current biology, 1993-05, Vol.3 (5), p.265-273

1993

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

Cell, 1996-10, Vol.87 (2), p.241-251

1996

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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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Elongated Oligomers Assemble into Mammalian PrP Amyloid Fibrils

Journal of molecular biology, 2006-03, Vol.357 (3), p.975-985

2006

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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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P117 3D cryo-electron microscopic analysis of the disease mechanism of 1-antitrypsin deficiency

Thorax, 2011-12, Vol.66 (Suppl 4), p.A115-A115

2011

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Structure determination of macromolecular assemblies by single-particle analysis of cryo-electron micrographs

Current opinion in structural biology, 2004-10, Vol.14 (5), p.584-590

2004

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Location of a folding protein and shape changes in GroEL-GroES complexes imaged by cryo-electron microscopy

Nature (London), 1994-09, Vol.371 (6494), p.261-264

1994

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Chaperonins

Biochemical journal, 1998-07, Vol.333 ( Pt 2) (2), p.233-242

1998

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Structural diversity of ex vivo amyloid fibrils studied by cryo-electron microscopy

Journal of molecular biology, 2001-08, Vol.311 (2), p.241-247

2001

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Two Structural Transitions in Membrane Pore Formation by Pneumolysin, the Pore-Forming Toxin of Streptococcus pneumoniae

Cell, 1999-05, Vol.97 (5), p.647-655

1999

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Macromolecular structure determination by cryo-electron microscopy

Acta crystallographica. Section D, Biological crystallography., 2000-10, Vol.56 (10), p.1215-1222

Saibil, Helen R.

2000

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Mechanism of GroEL action: Productive release of polypeptide from a sequestered position under groes

Cell, 1995-11, Vol.83 (4), p.577-587

1995

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An Expanded Protein Folding Cage in the GroEL–gp31 Complex

Journal of molecular biology, 2006-05, Vol.358 (3), p.905-911

2006

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Atypical AAA+ Subunit Packing Creates an Expanded Cavity for Disaggregation by the Protein-Remodeling Factor Hsp104

Cell, 2007-12, Vol.131 (7), p.1366-1377

2007

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Structural Analysis of Macromolecular Assemblies by Electron Microscopy

Chaperonin complex with a newly folded protein encapsulated in the folding chamber

Dependence on solution conditions of aggregation and amyloid formation by an SH3 domain

Structural Basis of Pore Formation by the Bacterial Toxin Pneumolysin

Hsp26: a temperature-regulated chaperone

Three conformations of an archaeal chaperonin, TF55 from Sulfolobus shibatae

Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing

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

A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state

Conformational changes studied by cryo-electron microscopy

ATP induces large quaternary rearrangements in a cage-like chaperonin structure

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

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

Elongated Oligomers Assemble into Mammalian PrP Amyloid Fibrils

Multivalent Binding of Nonnative Substrate Proteins by the Chaperonin GroEL

P117 3D cryo-electron microscopic analysis of the disease mechanism of 1-antitrypsin deficiency

Structure determination of macromolecular assemblies by single-particle analysis of cryo-electron micrographs

Location of a folding protein and shape changes in GroEL-GroES complexes imaged by cryo-electron microscopy

Chaperonins

Structural diversity of ex vivo amyloid fibrils studied by cryo-electron microscopy

Two Structural Transitions in Membrane Pore Formation by Pneumolysin, the Pore-Forming Toxin of Streptococcus pneumoniae

Macromolecular structure determination by cryo-electron microscopy

Mechanism of GroEL action: Productive release of polypeptide from a sequestered position under groes

An Expanded Protein Folding Cage in the GroEL–gp31 Complex

Atypical AAA+ Subunit Packing Creates an Expanded Cavity for Disaggregation by the Protein-Remodeling Factor Hsp104

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