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Structural basis for intersubunit signaling in a protein disaggregating machine

Proceedings of the National Academy of Sciences - PNAS, 2012-07, Vol.109 (31), p.12515-12520

2012

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Molecular chaperones: guardians of the proteome in normal and disease states [version 1; peer review: 2 approved]

F1000 research, 2015, Vol.4, p.1448

2015

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Structural basis of preinitiation complex assembly on human Pol II promoters

The EMBO journal, 2000-01, Vol.19 (1), p.25-36

2000

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The M-Domain Controls Hsp104 Protein Remodeling Activity in an Hsp70/Hsp40-Dependent Manner

Journal of molecular biology, 2010-09, Vol.402 (1), p.30-37

2010

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Cryo-EM Structures of the Hsp104 Protein Disaggregase Captured in the ATP Conformation

Cell reports (Cambridge), 2019-01, Vol.26 (1), p.29-36.e3

2019

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CryoEM structure of Hsp104 and its mechanistic implication for protein disaggregation

Proceedings of the National Academy of Sciences - PNAS, 2010-05, Vol.107 (18), p.8135-8140

2010

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Electron Cryomicroscopy Structure of a Membrane-anchored Mitochondrial AAA Protease

The Journal of biological chemistry, 2011-02, Vol.286 (6), p.4404-4411

2011

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An Intersubunit Signaling Network Coordinates ATP Hydrolysis by m-AAA Proteases

Molecular cell, 2009-09, Vol.35 (5), p.574-585

2009

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Visualizing the ATPase Cycle in a Protein Disaggregating Machine: Structural Basis for Substrate Binding by ClpB

Molecular cell, 2007-01, Vol.25 (2), p.261-271

2007

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Structural determinants for protein unfolding and translocation by the Hsp104 protein disaggregase

Bioscience reports, 2017-12, Vol.37 (6)

2017

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Thermotolerance Requires Refolding of Aggregated Proteins by Substrate Translocation through the Central Pore of ClpB

Cell, 2004-11, Vol.119 (5), p.653-665

2004

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The Structure of ClpB: A Molecular Chaperone that Rescues Proteins from an Aggregated State

Cell, 2003-10, Vol.115 (2), p.229-240

2003

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Enniatin A inhibits the chaperone Hsp90 and unleashes the immune system against triple-negative breast cancer

iScience, 2023-12, Vol.26 (12), p.108308, Article 108308

2023

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Structural and Functional Conservation of Mycobacterium tuberculosis GroEL Paralogs Suggests that GroEL1 Is a Chaperonin

Journal of molecular biology, 2011-01, Vol.405 (3), p.831-839

2011

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Pharmacogenetic characterization of naturally occurring germline NT5C1A variants to chemotherapeutic nucleoside analogs

Pharmacogenetics and genomics, 2016-06, Vol.26 (6), p.271-279

2016

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The ClpB/Hsp104 molecular chaperone—a protein disaggregating machine

Journal of structural biology, 2004-04, Vol.146 (1), p.99-105

2004

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Coordination between aminoacylation and editing to protect against proteotoxicity

Nucleic acids research, 2023-10, Vol.51 (19), p.10606-10618

2023

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Mapping interactions with the chaperone network reveals factors that protect against tau aggregation

Nature structural & molecular biology, 2018-05, Vol.25 (5), p.384-393

2018

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Molecular chaperones in protein quality control

BMB reports, 2005-05, Vol.38 (3), p.259-265

2005

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Deciphering the mechanism and function of Hsp100 unfoldases from protein structure

Biochemical Society transactions, 2022-12, Vol.50 (6), p.1725-1736

2022

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The mitochondrial HSP90 paralog TRAP1 forms an OXPHOS-regulated tetramer and is involved in mitochondrial metabolic homeostasis

BMC biology, 2020-01, Vol.18 (1), p.10-10, Article 10

2020

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Atomic structure of the Leishmania spp. Hsp100 N‐domain

Proteins, structure, function, and bioinformatics, 2022-06, Vol.90 (6), p.1242-1246

2022

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Structural basis of impaired disaggregase function in the oxidation-sensitive SKD3 mutant causing 3-methylglutaconic aciduria

Nature communications, 2023-04, Vol.14 (1), p.2028-2028, Article 2028

2023

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Crystal Structure of the YcjX Stress Protein Reveals a Ras-Like GTP-Binding Protein

Journal of molecular biology, 2019-08, Vol.431 (17), p.3179-3190

2019

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Heat shock protein (Hsp) 70 is an activator of the Hsp104 motor

Proceedings of the National Academy of Sciences - PNAS, 2013-05, Vol.110 (21), p.8513-8518

2013

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Structural basis for intersubunit signaling in a protein disaggregating machine

Molecular chaperones: guardians of the proteome in normal and disease states [version 1; peer review: 2 approved]

Structural basis of preinitiation complex assembly on human Pol II promoters

The M-Domain Controls Hsp104 Protein Remodeling Activity in an Hsp70/Hsp40-Dependent Manner

Cryo-EM Structures of the Hsp104 Protein Disaggregase Captured in the ATP Conformation

CryoEM structure of Hsp104 and its mechanistic implication for protein disaggregation

Electron Cryomicroscopy Structure of a Membrane-anchored Mitochondrial AAA Protease

An Intersubunit Signaling Network Coordinates ATP Hydrolysis by m-AAA Proteases

Visualizing the ATPase Cycle in a Protein Disaggregating Machine: Structural Basis for Substrate Binding by ClpB

Structural determinants for protein unfolding and translocation by the Hsp104 protein disaggregase

Thermotolerance Requires Refolding of Aggregated Proteins by Substrate Translocation through the Central Pore of ClpB

The Structure of ClpB: A Molecular Chaperone that Rescues Proteins from an Aggregated State

Enniatin A inhibits the chaperone Hsp90 and unleashes the immune system against triple-negative breast cancer

Structural and Functional Conservation of Mycobacterium tuberculosis GroEL Paralogs Suggests that GroEL1 Is a Chaperonin

Pharmacogenetic characterization of naturally occurring germline NT5C1A variants to chemotherapeutic nucleoside analogs

The ClpB/Hsp104 molecular chaperone—a protein disaggregating machine

Coordination between aminoacylation and editing to protect against proteotoxicity

Mapping interactions with the chaperone network reveals factors that protect against tau aggregation

Molecular chaperones in protein quality control

Deciphering the mechanism and function of Hsp100 unfoldases from protein structure

The mitochondrial HSP90 paralog TRAP1 forms an OXPHOS-regulated tetramer and is involved in mitochondrial metabolic homeostasis

Atomic structure of the Leishmania spp. Hsp100 N‐domain

Structural basis of impaired disaggregase function in the oxidation-sensitive SKD3 mutant causing 3-methylglutaconic aciduria

Crystal Structure of the YcjX Stress Protein Reveals a Ras-Like GTP-Binding Protein

Heat shock protein (Hsp) 70 is an activator of the Hsp104 motor

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