P. Goloubinoff

发表

Synechocystis HSP17 is an amphitropic protein that stabilizes heat-stressed membranes and binds denatured proteins for subsequent chaperone-mediated refolding

G. Balogh, A. Glatz, L. Vigh, 2001, Proceedings of the National Academy of Sciences of the United States of America.

Evolution of maize inferred from sequence diversity of an Adh2 gene segment from archaeological specimens.

S. Pääbo, A. Wilson, P. Goloubinoff, 1993, Proceedings of the National Academy of Sciences of the United States of America.

Identification of thermolabile Escherichia coli proteins: prevention and reversion of aggregation by DnaK and ClpB

S. Rüdiger, B. Bukau, H. Langen, 1999, The EMBO journal.

GroE heat-shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli

G. Lorimer, P. Goloubinoff, A. Gatenby, 1989, Nature.

The Small Heat-shock Protein IbpB from Escherichia coli Stabilizes Stress-denatured Proteins for Subsequent Refolding by a Multichaperone Network*

J. Buchner, P. Goloubinoff, Lea Veinger, 1998, The Journal of Biological Chemistry.

Molecular Chaperones and Associated Cellular Clearance Mechanisms against Toxic Protein Conformers in Parkinson’s Disease

P. Goloubinoff, M. Hinault, America Farina-Henriquez-Cuendet, 2011, Neurodegenerative Diseases.

Function, evolution, and structure of J-domain proteins

Jason C. Young, P. Rios, A. Barducci, 2018, Cell Stress and Chaperones.

Hsp70 chaperones accelerate protein translocation and the unfolding of stable protein aggregates by entropic pulling.

Paolo De Los Rios, P. De Los Rios, A. Azem, 2006, Proceedings of the National Academy of Sciences of the United States of America.

Fluorescence Detection of Symmetric GroEL14(GroES7)2 Heterooligomers Involved in Protein Release during the Chaperonin Cycle*

L. Vigh, Z. Török, P. Goloubinoff, 1996, The Journal of Biological Chemistry.

Cadmium Causes Misfolding and Aggregation of Cytosolic Proteins in Yeast

Markus J. Tamás, P. Christen, M. Tamás, 2017, Molecular and Cellular Biology.

In vivo visualization of F-actin structures during the development of the moss Physcomitrella patens.

D. Schaefer, J. Zrÿd, Andrija Finka, 2007, The New phytologist.

GroES binding regulates GroEL chaperonin activity under heat shock

A. Azem, C. Weiss, P. Goloubinoff, 1997, FEBS letters.

On the evolution of chaperones and co-chaperones and the exponential expansion of proteome complexity

Dan S. Tawfik, Saurav Mallik, P. Goloubinoff, 2020 .

Structural analysis of GroE chaperonin complexes using chemical cross-linking.

A. Azem, C. Weiss, P. Goloubinoff, 1998, Methods in enzymology.

On the evolution of chaperones and cochaperones and the expansion of proteomes across the Tree of Life

Dan S. Tawfik, Saurav Mallik, P. Goloubinoff, 2020, Proceedings of the National Academy of Sciences.

Size-dependent Disaggregation of Stable Protein Aggregates by the DnaK Chaperone Machinery*

B. Bukau, P. Goloubinoff, S. Diamant, 2000, The Journal of Biological Chemistry.

Enhanced expression of 70-kilodalton heat shock protein limits cell division in a sepsis-induced model of acute respiratory distress syndrome*

C. Deutschman, P. Goloubinoff, Y. Weiss, 2008, Critical care medicine.

Interdomain communication suppressing high intrinsic ATPase activity of Sse1 is essential for its co‐disaggregase activity with Ssa1

Ashish, A. Sagar, P. Goloubinoff, 2020, The FEBS journal.

In vitro evolution of uracil glycosylase towards DnaKJ and GroEL binding evolves different misfolded states.

G. Schreiber, P. Goloubinoff, Oran Melanker, 2022, Journal of molecular biology.

Membrane lipid composition affects plant heat sensing and modulates Ca2+-dependent heat shock response

M. Péter, Andrija Finka, P. Goloubinoff, 2010, Plant signaling & behavior.

Contents Vol. 8, 2011

Jane S. Paulsen, Robert P. Davis, J. L. Mesa, 2011, Neurodegenerative Diseases.

Dicarboxylic amino acids and glycine‐betaine regulate chaperone‐mediated protein‐disaggregation under stress

A. Azem, P. Goloubinoff, S. Diamant, 2003, Molecular microbiology.

Effect of free and ATP-bound magnesium and manganese ions on the ATPase activity of chaperonin GroEL14.

A. Azem, C. Weiss, P. Goloubinoff, 1995, Biochemistry.

Misfolding and aggregation of nascent proteins: a novel mode of toxic cadmium action in vivo

Markus J. Tamás, P. Christen, M. Tamás, 2017, Current Genetics.

Reactivation of protein aggregates by mortalin and Tid1—the human mitochondrial Hsp70 chaperone system

Ohad Iosefson, A. Azem, P. Goloubinoff, 2011, Cell Stress and Chaperones.

In vitro evolution of uracil glycosylase towards DnaKJ and GroEL binding evolves different misfolded states

G. Schreiber, P. Goloubinoff, Oran Melanker, 2022, bioRxiv.

Entropic Inhibition: How the Activity of a AAA+ Machine Is Modulated by Its Substrate-Binding Domain

G. Haran, I. Riven, P. Goloubinoff, 2021, ACS chemical biology.

Physical Interaction between Bacterial Heat Shock Protein (Hsp) 90 and Hsp70 Chaperones Mediates Their Cooperative Action to Refold Denatured Proteins*

H. Yoshikawa, Satoru Watanabe, Penmetcha K. R. Kumar, 2014, The Journal of Biological Chemistry.

How do plants feel the heat and survive?

P. Goloubinoff, A. Guihur, Mathieu E. Rebeaud, 2022, Trends in biochemical sciences.

Hsp70 chaperones use ATP to remodel native protein oligomers and stable aggregates by entropic pulling

P. Rios, P. Goloubinoff, 2016, Nature Structural &Molecular Biology.

Characterization of the photosystem II 32 kDa protein in Synechococcus PCC7942

R. Haselkorn, M. Edelman, J. Brusslan, 1988, Plant Molecular Biology.

Molecular chaperones are nanomachines that catalytically unfold misfolded and alternatively folded proteins

P. Goloubinoff, Rayees U. H. Mattoo, 2014, Cellular and Molecular Life Sciences.

Chaperonin-facilitated refolding of ribulosebisphosphate carboxylase and ATP hydrolysis by chaperonin 60 (groEL) are K+ dependent.

G. Lorimer, J. Reed, P. Viitanen, 1990, Biochemistry.

Second Virtual International Symposium on Cellular and Organismal Stress Responses, September 8–9, 2022

Nadinath B. Nillegoda, M. Clark, W. Houry, 2023, Cell Stress and Chaperones.

How do plants feel the heat?

R. Mittler, Andrija Finka, P. Goloubinoff, 2012, Trends in biochemical sciences.

Membrane fluidization triggers membrane remodeling which affects the thermotolerance in Escherichia coli.

G. Balogh, I. Horváth, Z. Török, 2005, Biochemical and biophysical research communications.

Heat perception and signalling in plants: a tortuous path to thermotolerance.

Andrija Finka, P. Goloubinoff, Younousse Saidi, 2011, The New phytologist.

The Heat Shock Response in Moss Plants Is Regulated by Specific Calcium-Permeable Channels in the Plasma Membrane[C][W]

F. Maathuis, Andrija Finka, P. Goloubinoff, 2009, The Plant Cell Online.

Reactivation of protein aggregates by mortalin and Tid1—the human mitochondrial Hsp70 chaperone system

Ohad Iosefson, A. Azem, P. Goloubinoff, 2011, Cell Stress and Chaperones.

Editorial: The HSP70 Molecular Chaperone Machines

P. Goloubinoff, 2017, Front. Mol. Biosci..

The kinetic parameters and energy cost of the Hsp70 chaperone as a polypeptide unfoldase.

P. Christen, P. De Los Rios, A. Lustig, 2010, Nature chemical biology.

Stable α-Synuclein Oligomers Strongly Inhibit Chaperone Activity of the Hsp70 System by Weak Interactions with J-domain Co-chaperones*

H. Lashuel, G. Dietler, P. Goloubinoff, 2010, The Journal of Biological Chemistry.

Disaggregating chaperones: an unfolding story.

P. Christen, P. Goloubinoff, Sandeep Savitaprakash Sharma, 2009, Current protein & peptide science.

The mechanism of Hsp70 chaperones: (entropic) pulling the models together.

P. De Los Rios, P. Goloubinoff, 2007, Trends in biochemical sciences.

Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network.

A. Zvi, B. Bukau, A. Mogk, 1999, Proceedings of the National Academy of Sciences of the United States of America.

The growing world of small heat shock proteins: from structure to functions

B. Brundel, H. Kampinga, C. Emanuelsson, 2017, Cell Stress and Chaperones.

The Hsp70 chaperone system: distinct roles in erythrocyte formation and maintenance

Nadinath B. Nillegoda, S. Jane, N. Nillegoda, 2021, Haematologica.

Molecular and biochemical mechanisms associated with dormancy and drought tolerance in the desert legume Retama raetam.

A. Kaplan, R. Mittler, L. Pnueli, 2002, The Plant journal : for cell and molecular biology.

The Membrane-Associated Transient Receptor Potential Vanilloid Channel Is the Central Heat Shock Receptor Controlling the Cellular Heat Shock Response in Epithelial Cells

P. Goloubinoff, Younousse Saidi, Y. Weiss, 2013, PloS one.

Evidence for a lipochaperonin: association of active protein-folding GroESL oligomers with lipids can stabilize membranes under heat shock conditions.

G. Balogh, A. Glatz, I. Horváth, 1997, Proceedings of the National Academy of Sciences of the United States of America.

Enhanced heat shock protein 70 expression alters proteasomal degradation of I&kgr;B kinase in experimental acute respiratory distress syndrome*

C. Deutschman, Y. Ben-Neriah, P. Goloubinoff, 2007, Critical care medicine.

Molecular architecture of the rapidly metabolized 32-kilodalton protein of photosystem II. Indications for COOH-terminal processing of a chloroplast membrane polypeptide.

M. Edelman, J. Marder, P. Goloubinoff, 1984, The Journal of biological chemistry.

Proteomic data from human cell cultures refine mechanisms of chaperone-mediated protein homeostasis

Andrija Finka, P. Goloubinoff, Andrija Finka, 2013, Cell Stress and Chaperones.

Characterization of a functional GroEL14(GroES7)2 chaperonin hetero-oligomer.

M. Kessel, A. Azem, P. Goloubinoff, 1994, Science.

Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and Mg-ATP

G. Lorimer, J. Christeller, P. Goloubinoff, 1989, Nature.

Activation of the heat shock response in plants by chlorophenols: transgenic Physcomitrella patens as a sensitive biosensor for organic pollutants.

J. Schwitzguébel, P. Goloubinoff, Younousse Saidi, 2007, Plant, cell & environment.

Controlled Expression of Recombinant Proteins in Physcomitrella patens by a Conditional Heat-shock Promoter: a Tool for Plant Research and Biotechnology

D. Schaefer, Andrija Finka, P. Goloubinoff, 2005, Plant Molecular Biology.

Multi-layered molecular mechanisms of polypeptide holding, unfolding and disaggregation by HSP70/HSP110 chaperones

Andrija Finka, P. Goloubinoff, Sandeep Savitaprakash Sharma, 2015, Front. Mol. Biosci..

Heavy metal ions are potent inhibitors of protein folding.

P. Christen, P. Goloubinoff, Sandeep Savitaprakash Sharma, 2008, Biochemical and biophysical research communications.

Review: mechanisms of disaggregation and refolding of stable protein aggregates by molecular chaperones.

P. Goloubinoff, A. Ben-Zvi, A. Ben-Zvi, 2001, Journal of structural biology.

Hsp110 Is a Bona Fide Chaperone Using ATP to Unfold Stable Misfolded Polypeptides and Reciprocally Collaborate with Hsp70 to Solubilize Protein Aggregates*

Andrija Finka, P. Goloubinoff, Rayees U. H. Mattoo, 2013, The Journal of Biological Chemistry.

Arsenite interferes with protein folding and triggers formation of protein aggregates in yeast

Clara Navarrete, Markus J. Tamás, Therese Jacobson, 2012, Journal of Cell Science.

The CaMV 35S promoter has a weak expression activity in dark grown tissues of moss Physcomitrella patens

D. Schaefer, Andrija Finka, P. Goloubinoff, 2009, Plant signaling & behavior.

Chloroplast-coded atrazine resistance in Solanum nigrum: psbA loci from susceptible and resistant biotypes are isogenic except for a single codon change.

M. Edelman, P. Goloubinoff, R. Hallick, 1984, Nucleic acids research.

The knock-out of ARP3a gene affects F-actin cytoskeleton organization altering cellular tip growth, morphology and development in moss Physcomitrella patens.

D. Schaefer, J. Neuhaus, Andrija Finka, 2008, Cell motility and the cytoskeleton.

Genetic dissection of the roles of chaperones and proteases in protein folding and degradation in the Escherichia coli cytosol

B. Bukau, H. Langen, A. Mogk, 2001, Molecular microbiology.

Moderate Fever Cycles as a Potential Mechanism to Protect the Respiratory System in COVID-19 Patients

P. Goloubinoff, Bruno Fauvet, Y. Weiss, 2020, Frontiers in Medicine.

Native folding of aggregation-prone recombinant proteins in Escherichia coli by osmolytes, plasmid- or benzyl alcohol–overexpressed molecular chaperones

A. de Marco, P. Goloubinoff, S. Diamant, 2005, Cell stress & chaperones.

Chaperones and proteases

P. Goloubinoff, M. Hinault, A. Ben-Zvi, 2007, Journal of Molecular Neuroscience.

Meta-analysis of heat- and chemically upregulated chaperone genes in plant and human cells

Andrija Finka, P. Goloubinoff, Rayees U. H. Mattoo, 2010, Cell Stress and Chaperones.

Quantitative proteomics of heat-treated human cells show an across-the-board mild depletion of housekeeping proteins to massively accumulate few HSPs

P. Rios, M. Quadroni, Andrija Finka, 2015, Cell Stress and Chaperones.

Recruiting Unfolding Chaperones to Solubilize Misfolded Recombinant Proteins

P. Goloubinoff, Rayees U. H. Mattoo, 2014 .

Molecular chaperones as enzymes that catalytically unfold misfolded polypeptides

P. Goloubinoff, S. Priya, Sandeep Savitaprakash Sharma, 2013, FEBS letters.

Mechanisms of protein homeostasis in health, aging and disease.

P. Goloubinoff, 2016, Swiss medical weekly.

GroEL and CCT are catalytic unfoldases mediating out-of-cage polypeptide refolding without ATP

P. De Los Rios, A. Azem, Andrija Finka, 2013, Proceedings of the National Academy of Sciences.

Protein folding: Chaperoning protein evolution.

P. De Los Rios, P. Goloubinoff, 2012, Nature chemical biology.

From minichaperone to GroEL 3: properties of an active single-ring mutant of GroEL.

A. Fersht, P. Goloubinoff, J. Chatellier, 2000, Journal of molecular biology.

Minimal and optimal mechanisms for GroE-mediated protein folding.

A. Fersht, P. Goloubinoff, J. Chatellier, 1998, Proceedings of the National Academy of Sciences of the United States of America.

The protein-folding activity of chaperonins correlates with the symmetric GroEL14(GroES7)2 heterooligomer.

M. Kessel, A. Azem, C. Weiss, 1995, Proceedings of the National Academy of Sciences of the United States of America.

Experimental Milestones in the Discovery of Molecular Chaperones as Polypeptide Unfolding Enzymes.

Andrija Finka, P. Goloubinoff, Rayees U. H. Mattoo, 2016, Annual review of biochemistry.

Heat shock response in photosynthetic organisms: membrane and lipid connections.

A. Glatz, I. Horváth, J. Harwood, 2012, Progress in lipid research.

The Novel Hydroxylamine Derivative NG-094 Suppresses Polyglutamine Protein Toxicity in Caenorhabditis elegans*

P. Haldimann, P. Goloubinoff, L. Vígh, 2011, The Journal of Biological Chemistry.

How do humans and plants feel the heat?

P. Goloubinoff, A. Guihur, B. Bourgine, 2022, Trends in plant science.

Plasma Membrane Cyclic Nucleotide Gated Calcium Channels Control Land Plant Thermal Sensing and Acquired Thermotolerance[C][W]

F. Maathuis, Andrija Finka, P. Goloubinoff, 2012, Plant Cell.

A gene trap Dissociation insertion line, associated with a RING-H2 finger gene, shows tissue specific and developmental regulated expression of the gene in Arabidopsis.

P. Genschik, E. Lechner, W. Shen, 2002, Gene.

Farming Amphetamines: Khat (Catha edulis Forsk.) a Traditional Plant with Mild Stimulating Psychoactive and Medicinal Properties

N. Dudai, S. Ben-Shabat, E. Lewinsohn, 2014 .

The enigma of the gene coding for ribosomal protein S12 in the chloroplasts of Nicotiana.

M. Edelman, P. Goloubinoff, H. Fromm, 1986, Nucleic acids research.

Tunable microsecond dynamics of an allosteric switch regulate the activity of a AAA+ disaggregation machine

N. Elad, G. Haran, Yoav Barak, 2019, Nature Communications.

Purification of mammalian mitochondrial chaperonin 60 through in vitro reconstitution of active oligomers.

M. Kessel, G. Lorimer, W. Bergmeier, 1998, Methods in enzymology.

Increased Efficiency of GroE-assisted Protein Folding by Manganese Ions (*)

A. Azem, C. Weiss, P. Goloubinoff, 1995, The Journal of Biological Chemistry.

Effect of divalent cations on the molecular structure of the GroEL oligomer.

A. Azem, P. Goloubinoff, S. Diamant, 1994, Biochemistry.

Temperature-controlled activity of DnaK-DnaJ-GrpE chaperones: protein-folding arrest and recovery during and after heat shock depends on the substrate protein and the GrpE concentration.

P. Goloubinoff, S. Diamant, 1998, Biochemistry.

Chaperones convert the energy from ATP into the nonequilibrium stabilization of native proteins

A. Barducci, P. De Los Rios, P. Goloubinoff, 2018, Nature Chemical Biology.

Molecular chaperones inject energy from ATP hydrolysis into the non-equilibrium stabilisation of native proteins

A. Barducci, P. De Los Rios, P. Goloubinoff, 2017, bioRxiv.

Mechanisms of Active Solubilization of Stable Protein Aggregates by Molecular Chaperones

P. Goloubinoff, A. Ben-Zvi, 2006 .

The Cellular Functions of Chaperonins

R. Larossa, G. Lorimer, P. Viitanen, 1990 .

Active Solubilization and Refolding of Stable Protein Aggregates By Cooperative Unfolding Action of Individual Hsp70 Chaperones*

P. De Los Rios, G. Dietler, P. Goloubinoff, 2004, Journal of Biological Chemistry.

A Mutant at Position 87 of the GroEL Chaperonin Is Affected in Protein Binding and ATP Hydrolysis (*)

C. Weiss, P. Goloubinoff, Pierre Goloubinoff, 1995, The Journal of Biological Chemistry.

Quantitative proteomic analysis to capture the role of heat‐accumulated proteins in moss plant acquired thermotolerance

M. Quadroni, Andrija Finka, P. Goloubinoff, 2020, Plant, cell & environment.

ZnJ2 Is a Member of a Large Chaperone Family in the Chloroplast of Photosynthetic Organisms that Features a DnaJ-Like Zn-Finger Domain

M. Shapira, P. Goloubinoff, Lior Doron, 2018, Front. Mol. Biosci..

Bacterial Hsp90 Facilitates the Degradation of Aggregation-Prone Hsp70–Hsp40 Substrates

M. Quadroni, Andrija Finka, P. Genevaux, 2021, Frontiers in Molecular Biosciences.

Bacterial Hsp90 mediates the degradation of aggregation-prone Hsp70-Hsp40 substrates preferentially by HslUV proteolysis

M. Quadroni, Andrija Finka, P. Genevaux, 2018, bioRxiv.

Proteomic data from human cell cultures refine mechanisms of chaperone-mediated protein homeostasis

Andrija Finka, P. Goloubinoff, 2013, Cell Stress and Chaperones.

Design of an Arabidopsis thaliana reporter line to detect heat-sensing and signaling mutants

P. Goloubinoff, A. Guihur, B. Bourgine, 2023, bioRxiv.

A fluorescent multi-domain protein reveals the unfolding mechanism of Hsp70

P. De Los Rios, P. Goloubinoff, Bruno Fauvet, 2022, Nature Chemical Biology.

Repair or Degrade: the Thermodynamic Dilemma of Cellular Protein Quality-Control

P. De Los Rios, P. Goloubinoff, Bruno Fauvet, 2021, Frontiers in Molecular Biosciences.

Chemical Chaperones Regulate Molecular Chaperones in Vitro and in Cells under Combined Salt and Heat Stresses*

P. Goloubinoff, S. Diamant, N. Eliahu, 2001, The Journal of Biological Chemistry.

Tackling the Problem of Thermal versus non Thermal Biological Effects of High Frequency Electromagnetic Radiations

F. Rachidi, P. Goloubinoff, P. Zweiacker, 2004 .

Aggregates with Hsp 70 to Solubilize Protein Polypeptides and Reciprocally Collaborate ATP to Unfold Stable Misfolded Chaperone Using Bona Fide Hsp 110 Is a Protein Structure and Folding :

Andrija Finka, P. Goloubinoff, Rayees U. H. Mattoo, 2013 .

A novel fluorescent multi-domain protein construct reveals the individual steps of the unfoldase action of Hsp70

P. De Los Rios, P. Goloubinoff, Bruno Fauvet, 2022, bioRxiv.

Non-native Proteins as Newly-Identified Targets of Heavy Metals and Metalloids

P. Christen, P. Goloubinoff, Sandeep K. Sharma, 2011 .

Quantitative proteomics of rat livers shows that unrestricted feeding is stressful for proteostasis with implications on life span

M. Quadroni, Andrija Finka, P. Goloubinoff, 2016, Aging.

Molecular chaperones are nanomachines that catalytically unfold misfolded and alternatively folded proteins

P. Goloubinoff, Rayees U. H. Mattoo, 2014, Cellular and Molecular Life Sciences.

In vitro evolution of uracil glycosylase towards DnaKJ and GroEL binding evolves different misfolded states

G. Schreiber, P. Goloubinoff, Oran Melanker, 2021, bioRxiv.

The CNGCb and CNGCd genes from Physcomitrella patens moss encode for thermosensory calcium channels responding to fluidity changes in the plasma membrane

Andrija Finka, P. Goloubinoff, 2013, Cell Stress and Chaperones.

Quantitative proteomics of heat-treated human cells show an across-the-board mild depletion of housekeeping proteins to massively accumulate few HSPs

P. Rios, M. Quadroni, Andrija Finka, 2015, Cell Stress and Chaperones.

Proteinaceous Infectious Behavior in Non-pathogenic Proteins Is Controlled by Molecular Chaperones*

P. Goloubinoff, A. Ben-Zvi, 2002, The Journal of Biological Chemistry.

Probing the different chaperone activities of the bacterial HSP70‐HSP40 system using a thermolabile luciferase substrate

P. De Los Rios, P. Goloubinoff, Sandeep K. Sharma, 2011, Proteins.

The amino terminal region delimited by Met1 and Met37 is an integral part of the 32 kDa herbicide binding protein

M. Edelman, P. Goloubinoff, Y. Eyal, 1987, Plant Molecular Biology.

Single-molecule spectroscopy reveals dynamic allostery mediated by the substrate-binding domain of a AAA+ machine

G. Haran, I. Riven, P. Goloubinoff, 2020 .

Emerging fields in chaperone proteins: A French workshop.

A. Barducci, F. Ochsenbein, E. Mileo, 2018, Biochimie.

Synergism between a foldase and an unfoldase: reciprocal dependence between the thioredoxin-like activity of DnaJ and the polypeptide-unfolding activity of DnaK

Andrija Finka, P. Goloubinoff, Rayees U. H. Mattoo, 2014, Front. Mol. Biosci..

Tunable microsecond dynamics of an allosteric switch regulate the activity of a AAA+ disaggregation machine

Nadav Elad, Gilad Haran, N. Elad, 2019, Nature Communications.

Molecular Crime and Cellular Punishment

P. Goloubinoff, M. Hinault, 2007 .

Molecular Chaperones and Associated Cellular Clearance Mechanisms against Toxic Protein Conformers in Parkinson’s Disease

P. Goloubinoff, M. Hinault, America Farina-Henriquez-Cuendet, 2011, Neurodegenerative Diseases.

Recent and future grand challenges in protein folding, misfolding, and degradation

P. Goloubinoff, 2014, Front. Mol. Biosci..

Biophysical characterization of two different stable misfolded monomeric polypeptides that are chaperone-amenable substrates.

S. Doglia, A. Natalello, P. Goloubinoff, 2013, Journal of molecular biology.

Arsenite interferes with protein folding and triggers formation of protein aggregates in yeast

Markus J. Tamás, P. Christen, C. Grant, 2012, Journal of Cell Science.

Function, evolution, and structure of J-domain proteins

Jason C. Young, Nadinath B. Nillegoda, P. Rios, 2018, Cell Stress and Chaperones.

Author Correction: A fluorescent multi-domain protein reveals the unfolding mechanism of Hsp70

P. De Los Rios, P. Goloubinoff, Bruno Fauvet, 2023, Nature Chemical Biology.

THE RESPONSE OF PLANTS TO SALINITY: FROM TURGOR ADJUSTMENTS TO GENOME MODIFICATION

P. Goloubinoff, G. N. Amzallag, H. R. Lerner, 1994 .

Autorepression of yeast Hsp70 cochaperones by intramolecular interactions involving their J-domains

P. De Los Rios, P. Goloubinoff, Bruno Fauvet, 2024, bioRxiv.

J-domain proteins: From molecular mechanisms to diseases

Nadinath B. Nillegoda, L. Joachimiak, H. Kampinga, 2023, Cell stress & chaperones.

Stable -Synuclein Oligomers Strongly Inhibit Chaperone Activity of the Hsp70 System by Weak Interactions with

P. Goloubinoff, M. Hinault, Rayees U. H. Mattoo, 2010 .

Stress biology: Complexity and multifariousness in health and disease

Marc L. Mendillo, G. Chiosis, L. Sistonen, 2024, Cell stress & chaperones.