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Client-Loading Conformation of the Hsp90 Molecular Chaperone Revealed in the Cryo-EM Structure of the Human Hsp90:Hop Complex

Molecular cell, 2011-06, Vol.42 (6), p.771-781

2011

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Specific Binding of Tetratricopeptide Repeat Proteins to Heat Shock Protein 70 (Hsp70) and Heat Shock Protein 90 (Hsp90) Is Regulated by Affinity and Phosphorylation

Biochemistry (Easton), 2015-12, Vol.54 (48), p.7120-7131

2015

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Ratchet-like polypeptide translocation mechanism of the AAA+ disaggregase Hsp104

Science (American Association for the Advancement of Science), 2017-07, Vol.357 (6348), p.273-279

2017

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Stacked binding of a PET ligand to Alzheimer's tau paired helical filaments

Nature communications, 2023-05, Vol.14 (1), p.3048-3048, Article 3048

2023

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The structure of an Hsp90-immunophilin complex reveals cochaperone recognition of the client maturation state

Molecular cell, 2021-09, Vol.81 (17), p.3496-3508.e5

2021

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Structural basis for substrate gripping and translocation by the ClpB AAA+ disaggregase

Nature communications, 2019-06, Vol.10 (1), p.2393-2393, Article 2393

2019

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Competing protein-protein interactions regulate binding of Hsp27 to its client protein tau

Nature communications, 2018-11, Vol.9 (1), p.4563-11, Article 4563

2018

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Spiral architecture of the Hsp104 disaggregase reveals the basis for polypeptide translocation

Nature structural & molecular biology, 2016-09, Vol.23 (9), p.830

2016

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Structural Analysis of E. coli hsp90 Reveals Dramatic Nucleotide-Dependent Conformational Rearrangements

Cell, 2006-10, Vol.127 (2), p.329-340

2006

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The Protein Targeting Factor Get3 Functions as ATP-Independent Chaperone under Oxidative Stress Conditions

Molecular cell, 2014-10, Vol.56 (1), p.116-127

2014

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Mitochondrial peroxiredoxin functions as crucial chaperone reservoir in Leishmania infantum

Proceedings of the National Academy of Sciences - PNAS, 2015-02, Vol.112 (7), p.E616-E624

2015

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Chaperone activation and client binding of a 2-cysteine peroxiredoxin

Nature communications, 2019-02, Vol.10 (1), p.659-659, Article 659

2019

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Spiraling in Control: Structures and Mechanisms of the Hsp104 Disaggregase

Cold Spring Harbor perspectives in biology, 2019-08, Vol.11 (8), p.a034033

2019

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Architecture and Nucleotide-Dependent Conformational Changes of the Rvb1-Rvb2 AAA+ Complex Revealed by Cryoelectron Microscopy

Structure (London), 2016-05, Vol.24 (5), p.657-666

2016

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KRAS Protein Stability Is Regulated through SMURF2: UBCH5 Complex-Mediated β-TrCP1 Degradation

Neoplasia (New York, N.Y.), 2014-02, Vol.16 (2), p.115-W5

2014

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Mining Disaggregase Sequence Space to Safely Counter TDP-43, FUS, and α-Synuclein Proteotoxicity

Cell reports (Cambridge), 2019-08, Vol.28 (8), p.2080-2095.e6

2019

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Cryo-EM structures reveal tau filaments from Down syndrome adopt Alzheimer’s disease fold

Acta neuropathologica communications, 2024-06, Vol.12 (1), p.94-15, Article 94

2024

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Mutational Analysis of S12 Protein and Implications for the Accuracy of Decoding by the Ribosome

Journal of molecular biology, 2007-12, Vol.374 (4), p.1065-1076

2007

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A conserved histidine modulates HSPB5 structure to trigger chaperone activity in response to stress-related acidosis

eLife, 2015-05, Vol.4

2015

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Structural insights of the p97/VCP AAA+ ATPase: How adapter interactions coordinate diverse cellular functionality

The Journal of biological chemistry, 2023-11, Vol.299 (11), p.105182-105182, Article 105182

2023

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The E3 Ubiquitin Ligase CHIP and the Molecular Chaperone Hsc70 Form a Dynamic, Tethered Complex

Biochemistry (Easton), 2013-08, Vol.52 (32), p.5354-5364

2013

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Enhancement of dynamin polymerization and GTPase activity by Arc/Arg3.1

Biochimica et biophysica acta, 2015-06, Vol.1850 (6), p.1310-1318

2015

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Polyphosphate: A Conserved Modifier of Amyloidogenic Processes

Molecular cell, 2016-09, Vol.63 (5), p.768-780

2016

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Species-Dependent Ensembles of Conserved Conformational States Define the Hsp90 Chaperone ATPase Cycle

Molecular cell, 2008-12, Vol.32 (5), p.631-640

2008

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BAG3 Is a Modular, Scaffolding Protein that physically Links Heat Shock Protein 70 (Hsp70) to the Small Heat Shock Proteins

Journal of molecular biology, 2017-01, Vol.429 (1), p.128-141

2017

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Client-Loading Conformation of the Hsp90 Molecular Chaperone Revealed in the Cryo-EM Structure of the Human Hsp90:Hop Complex

Specific Binding of Tetratricopeptide Repeat Proteins to Heat Shock Protein 70 (Hsp70) and Heat Shock Protein 90 (Hsp90) Is Regulated by Affinity and Phosphorylation

Ratchet-like polypeptide translocation mechanism of the AAA+ disaggregase Hsp104

Stacked binding of a PET ligand to Alzheimer's tau paired helical filaments

The structure of an Hsp90-immunophilin complex reveals cochaperone recognition of the client maturation state

Structural basis for substrate gripping and translocation by the ClpB AAA+ disaggregase

Competing protein-protein interactions regulate binding of Hsp27 to its client protein tau

Spiral architecture of the Hsp104 disaggregase reveals the basis for polypeptide translocation

Structural Analysis of E. coli hsp90 Reveals Dramatic Nucleotide-Dependent Conformational Rearrangements

The Protein Targeting Factor Get3 Functions as ATP-Independent Chaperone under Oxidative Stress Conditions

Mitochondrial peroxiredoxin functions as crucial chaperone reservoir in Leishmania infantum

Chaperone activation and client binding of a 2-cysteine peroxiredoxin

Spiraling in Control: Structures and Mechanisms of the Hsp104 Disaggregase

Architecture and Nucleotide-Dependent Conformational Changes of the Rvb1-Rvb2 AAA+ Complex Revealed by Cryoelectron Microscopy

KRAS Protein Stability Is Regulated through SMURF2: UBCH5 Complex-Mediated β-TrCP1 Degradation

Mining Disaggregase Sequence Space to Safely Counter TDP-43, FUS, and α-Synuclein Proteotoxicity

Cryo-EM structures reveal tau filaments from Down syndrome adopt Alzheimer’s disease fold

Mutational Analysis of S12 Protein and Implications for the Accuracy of Decoding by the Ribosome

A conserved histidine modulates HSPB5 structure to trigger chaperone activity in response to stress-related acidosis

Structural insights of the p97/VCP AAA+ ATPase: How adapter interactions coordinate diverse cellular functionality

The E3 Ubiquitin Ligase CHIP and the Molecular Chaperone Hsc70 Form a Dynamic, Tethered Complex

Enhancement of dynamin polymerization and GTPase activity by Arc/Arg3.1

Polyphosphate: A Conserved Modifier of Amyloidogenic Processes

Species-Dependent Ensembles of Conserved Conformational States Define the Hsp90 Chaperone ATPase Cycle

BAG3 Is a Modular, Scaffolding Protein that physically Links Heat Shock Protein 70 (Hsp70) to the Small Heat Shock Proteins

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