Prof Pierre Goloubinoff
Current affiliation: Universite de Lausanne
Subject: Life Sciences
Primary location: Switzerland
Biophysical Characterization of Two Different Stable Misfolded Monomeric Polypeptides That Are Chaperone-Amenable Substrates
Published in:Journal of Molecular Biology
Publication date:2013-04-01
Disaggregating Chaperones: An Unfolding Story
Published in:Current Protein and Peptide Science
Publication date:2009-10-01
Molecular Crime and Cellular Punishment
Published in:Advances in Experimental Medicine and Biology
Publication date:Not available
Molecular Chaperones as Polypeptide Unfolding Enzymes
Published in:Annual Review of Biochemistry
Publication date:2016-06-02
How do plants feel the heat?
Published in:Trends in Biochemical Sciences
Publication date:2012-03-01
Heat perception and signalling in plants: a tortuous path to thermotolerance
Published in:New Phytologist
Publication date:2010-12-07Minireview
In vivovisualization of F-actin structures during the development of the mossPhyscomitrella patens
Published in:New Phytologist
Publication date:2007-01-15
Multi-layered molecular mechanisms of polypeptide holding, unfolding and disaggregation by HSP70/HSP110 chaperones
Published in:Frontiers in Molecular Biosciences
Publication date:2015-06-05
Meta-analysis of heat- and chemically upregulated chaperone genes in plant and human cells
Published in:Cell Stress and Chaperones
Publication date:2010-08-09
Quantitative proteomics of heat-treated human cells show an across-the-board mild depletion of housekeeping proteins to massively accumulate few HSPs
Published in:Cell Stress and Chaperones
Publication date:2015-04-08
Membrane lipid composition affects plant heat sensing and modulates Ca2+-dependent heat shock response
Published in:Plant Signaling & Behavior
Publication date:2010-12-01
Controlled Expression of Recombinant Proteins in Physcomitrella patens by a Conditional Heat-shock Promoter: a Tool for Plant Research and Biotechn...
Published in:Plant Molecular Biology
Publication date:2005-11-01
The Heat Shock Response in Moss Plants Is Regulated by Specific Calcium-Permeable Channels in the Plasma Membrane
Published in:The Plant Cell
Publication date:2009-09-01
Recent and future grand challenges in protein folding, misfolding, and degradation
Published in:Frontiers in Molecular Biosciences
Publication date:2014-03-27
Mechanisms of Active Solubilization of Stable Protein Aggregates by Molecular Chaperones
Published in:Protein Misfolding, Aggregation, and Conformational Diseases
Publication date:Not available
Effect of Divalent Cations on the Molecular Structure of the GroEL Oligomer
Published in:Biochemistry
Publication date:1994-05-01
Protein folding: Chaperoning protein evolution
Published in:Nature Chemical Biology
Publication date:2012-02-15
Non-native Proteins as Newly-Identified Targets of Heavy Metals and Metalloids
Published in:Cellular Effects of Heavy Metals
Publication date:2011-01-01
[22] Structural analysis of GroE chaperonin complexes using chemical cross-linking
Published in:Methods in Enzymology
Publication date:1998-01-01
GroES binding regulates GroEL chaperonin activity under heat shock
Published in:FEBS Letters
Publication date:1997-04-28
Molecular chaperones as enzymes that catalytically unfold misfolded polypeptides
Published in:FEBS Letters
Publication date:2013-05-16
Chaperones and Proteases: Cellular Fold-Controlling Factors of Proteins in Neurodegenerative Diseases and Aging
Published in:Journal of Molecular Neuroscience
Publication date:2006-01-01
Molecular Chaperones and Associated Cellular Clearance Mechanisms against Toxic Protein Conformers in Parkinson’s Disease
Published in:Neurodegenerative Diseases
Publication date:2011-01-01
Effect of divalent cations on the molecular structure of the GroEL oligomer. [Erratum to document cited in CA120:317960]
Published in:Biochemistry
Publication date:1994-10-01
Effect of Free and ATP-bound Magnesium and Manganese Ions on the ATPase Activity of Chaperonin GroEL14
Published in:Biochemistry
Publication date:1995-01-01
The Cellular Functions of Chaperonins
Published in:Stress Proteins
Publication date:1990-01-01
GroE heat-shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli
Published in:Nature
Publication date:1989-01-05
Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and Mg-ATP
Published in:Nature
Publication date:1989-12-28
Characterization of a functional GroEL14(GroES7)2 chaperonin hetero-oligomer
Published in:Science
Publication date:1994-07-29
Hsp110 Is a Bona Fide Chaperone Using ATP to Unfold Stable Misfolded Polypeptides and Reciprocally Collaborate with Hsp70 to Solubilize Protein Agg...
Published in:Journal of Biological Chemistry
Publication date:2013-06-04
The Small Heat-shock Protein IbpB from Escherichia coli Stabilizes Stress-denatured Proteins for Subsequent Refolding by a Multichaperone Network
Published in:Journal of Biological Chemistry
Publication date:1998-05-01
Chemical Chaperones Regulate Molecular Chaperones in Vitro and in Cells under Combined Salt and Heat Stresses
Published in:Journal of Biological Chemistry
Publication date:2001-08-21
The Membrane-Associated Transient Receptor Potential Vanilloid Channel Is the Central Heat Shock Receptor Controlling the Cellular Heat Shock Respo...
Published in:PLoS ONE
Publication date:2013-02-27
Activation of the heat shock response in plants by chlorophenols: transgenic Physcomitrella patens as a sensitive biosensor for organic pollutants
Published in:Plant Cell & Environment
Publication date:2007-06-01
Temperature-Controlled Activity of DnaK−DnaJ−GrpE Chaperones: Protein-Folding Arrest and Recovery during and after Heat Shock Depends on the Subs...
Published in:Biochemistry
Publication date:1998-07-01
Evidence for a lipochaperonin: Association of active proteinfolding GroESL oligomers with lipids can stabilize membranes under heat shock conditions
Published in:Proceedings of the National Academy of Sciences
Publication date:1997-03-18
Physical Interaction between Bacterial Heat Shock Protein (Hsp) 90 and Hsp70 Chaperones Mediates Their Cooperative Action to Refold Denatured Proteins
Published in:Journal of Biological Chemistry
Publication date:2014-01-12
Heat shock response in photosynthetic organisms: Membrane and lipid connections
Published in:Progress in Lipid Research
Publication date:2012-07-01
Enhanced heat shock protein 70 expression alters proteasomal degradation of IκB kinase in experimental acute respiratory distress syndrome*
Published in:Critical Care Medicine
Publication date:2007-09-01
Enhanced expression of 70-kilodalton heat shock protein limits cell division in a sepsis-induced model of acute respiratory distress syndrome*
Published in:Critical Care Medicine
Publication date:2008-01-01
Synechocystis HSP17 is an amphitropic protein that stabilizes heat-stressed membranes and binds denatured proteins for subsequent chaperone-mediate...
Published in:Proceedings of the National Academy of Sciences
Publication date:2001-02-27
A gene trap Dissociation insertion line, associated with a RING-H2 finger gene, shows tissue specific and developmental regulated expression of the...
Published in:Gene
Publication date:2002-05-01