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Inorganic polyphosphate, a multifunctional polyanionic protein scaffold

The Journal of biological chemistry, 2019-02, Vol.294 (6), p.2180-2190

2019

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Maintaining a Healthy Proteome during Oxidative Stress

Molecular cell, 2018-01, Vol.69 (2), p.203-213

2018

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Thiol-based redox switches in eukaryotic proteins

Antioxidants & redox signaling, 2009-05, Vol.11 (5), p.997

2009

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Bacterial Responses to Reactive Chlorine Species

Annual review of microbiology, 2013-01, Vol.67 (1), p.141-160

2013

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Bile salts act as effective protein-unfolding agents and instigators of disulfide stress in vivo

Proceedings of the National Academy of Sciences - PNAS, 2014-04, Vol.111 (16), p.E1610-E1619

2014

Volltextzugriff (PDF)

Quantitative In Vivo Redox Sensors Uncover Oxidative Stress as an Early Event in Life

Molecular cell, 2012-09, Vol.47 (5), p.767-776

2012

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Quantifying changes in the thiol redox proteome upon oxidative stress in vivo

Proceedings of the National Academy of Sciences - PNAS, 2008-06, Vol.105 (24), p.8197-8202

2008

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Copper Induces Protein Aggregation, a Toxic Process Compensated by Molecular Chaperones

mBio, 2022-04, Vol.13 (2), p.e0325121-21

2022

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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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HdeB Functions as an Acid-protective Chaperone in Bacteria

The Journal of biological chemistry, 2015-01, Vol.290 (1), p.65-75

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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Comprehensive characterization of the Hsp70 interactome reveals novel client proteins and interactions mediated by posttranslational modifications

PLoS biology, 2022-10, Vol.20 (10), p.e3001839-e3001839

2022

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Protein thiol modifications visualized in vivo

PLoS biology, 2004-11, Vol.2 (11), p.e333-e333

2004

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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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Redox heterogeneity in mouse embryonic stem cells individualizes cell fate decisions

Developmental cell, 2024-08, Vol.59 (16), p.2118-2133.e8

2024

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Mutations in nucleotide metabolism genes bypass proteasome defects in png-1/NGLY1-deficient Caenorhabditis elegans

PLoS biology, 2024-07, Vol.22 (7), p.e3002720

2024

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Transcellular chaperone signaling is an intercellular stress-response distinct from the HSF-1-mediated heat shock response

PLoS biology, 2023-02, Vol.21 (2), p.e3001605-e3001605

2023

Volltextzugriff (PDF)

Comprehensive structural characterization of the human AAA+ disaggregase CLPB in the apo- and substrate-bound states reveals a unique mode of action driven by oligomerization

PLoS biology, 2023-02, Vol.21 (2), p.e3001987-e3001987

2023

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The redox-switch domain of Hsp33 functions as dual stress sensor

Nature structural & molecular biology, 2007-06, Vol.14 (6), p.556-563

2007

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Protein unfolding as a switch from self-recognition to high-affinity client binding

Nature communications, 2016-01, Vol.7 (1), p.10357-10357, Article 10357

2016

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Yeast derlin Dfm1 employs a chaperone-like function to resolve misfolded membrane protein stress

PLoS biology, 2023-01, Vol.21 (1), p.e3001950

2023

Volltextzugriff (PDF)

Severe Oxidative Stress Causes Inactivation of DnaK and Activation of the Redox-Regulated Chaperone Hsp33

Molecular cell, 2005-02, Vol.17 (3), p.381-392

2005

Volltextzugriff (PDF)

Get3 is a holdase chaperone and moves to deposition sites for aggregated proteins when membrane targeting is blocked

Journal of cell science, 2013-01, Vol.126 (Pt 2), p.473-483

2013

Volltextzugriff (PDF)

An essential thioredoxin-type protein of Trypanosoma brucei acts as redox-regulated mitochondrial chaperone

PLoS pathogens, 2019-09, Vol.15 (9), p.e1008065-e1008065

2019

Volltextzugriff (PDF)

Mycobacterium tuberculosis Rv0991c Is a Redox-Regulated Molecular Chaperone

mBio, 2020-08, Vol.11 (4)

2020

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Inorganic polyphosphate, a multifunctional polyanionic protein scaffold

Maintaining a Healthy Proteome during Oxidative Stress

Thiol-based redox switches in eukaryotic proteins

Bacterial Responses to Reactive Chlorine Species

Bile salts act as effective protein-unfolding agents and instigators of disulfide stress in vivo

Quantitative In Vivo Redox Sensors Uncover Oxidative Stress as an Early Event in Life

Quantifying changes in the thiol redox proteome upon oxidative stress in vivo

Copper Induces Protein Aggregation, a Toxic Process Compensated by Molecular Chaperones

Mitochondrial peroxiredoxin functions as crucial chaperone reservoir in Leishmania infantum

HdeB Functions as an Acid-protective Chaperone in Bacteria

Chaperone activation and client binding of a 2-cysteine peroxiredoxin

Comprehensive characterization of the Hsp70 interactome reveals novel client proteins and interactions mediated by posttranslational modifications

Protein thiol modifications visualized in vivo

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

Redox heterogeneity in mouse embryonic stem cells individualizes cell fate decisions

Mutations in nucleotide metabolism genes bypass proteasome defects in png-1/NGLY1-deficient Caenorhabditis elegans

Transcellular chaperone signaling is an intercellular stress-response distinct from the HSF-1-mediated heat shock response

Comprehensive structural characterization of the human AAA+ disaggregase CLPB in the apo- and substrate-bound states reveals a unique mode of action driven by oligomerization

The redox-switch domain of Hsp33 functions as dual stress sensor

Protein unfolding as a switch from self-recognition to high-affinity client binding

Yeast derlin Dfm1 employs a chaperone-like function to resolve misfolded membrane protein stress

Severe Oxidative Stress Causes Inactivation of DnaK and Activation of the Redox-Regulated Chaperone Hsp33

Get3 is a holdase chaperone and moves to deposition sites for aggregated proteins when membrane targeting is blocked

An essential thioredoxin-type protein of Trypanosoma brucei acts as redox-regulated mitochondrial chaperone

Mycobacterium tuberculosis Rv0991c Is a Redox-Regulated Molecular Chaperone

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