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

Mazal H, Iljina M, Barak Y, Elad N, Rosenzweig R, Goloubinoff P, Riven I, Haran G.

Nat Commun. 2019 Mar 29;10(1):1438. doi: 10.1038/s41467-019-09474-6.


Function, evolution, and structure of J-domain proteins.

Kampinga HH, Andreasson C, Barducci A, Cheetham ME, Cyr D, Emanuelsson C, Genevaux P, Gestwicki JE, Goloubinoff P, Huerta-Cepas J, Kirstein J, Liberek K, Mayer MP, Nagata K, Nillegoda NB, Pulido P, Ramos C, De Los Rios P, Rospert S, Rosenzweig R, Sahi C, Taipale M, Tomiczek B, Ushioda R, Young JC, Zimmermann R, Zylicz A, Zylicz M, Craig EA, Marszalek J.

Cell Stress Chaperones. 2019 Jan;24(1):7-15. doi: 10.1007/s12192-018-0948-4. Epub 2018 Nov 26. Review.


Emerging fields in chaperone proteins: A French workshop.

Mileo E, Ilbert M, Barducci A, Bordes P, Castanié-Cornet MP, Garnier C, Genevaux P, Gillet R, Goloubinoff P, Ochsenbein F, Richarme G, Iobbi-Nivol C, Giudici-Orticoni MT, Gontero B, Genest O.

Biochimie. 2018 Aug;151:159-165. doi: 10.1016/j.biochi.2018.06.004. Epub 2018 Jun 8.


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

Goloubinoff P, Sassi AS, Fauvet B, Barducci A, De Los Rios P.

Nat Chem Biol. 2018 Apr;14(4):388-395. doi: 10.1038/s41589-018-0013-8. Epub 2018 Mar 5.


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

Doron L, Goloubinoff P, Shapira M.

Front Mol Biosci. 2018 Feb 15;5:2. doi: 10.3389/fmolb.2018.00002. eCollection 2018.


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

Tamás MJ, Fauvet B, Christen P, Goloubinoff P.

Curr Genet. 2018 Feb;64(1):177-181. doi: 10.1007/s00294-017-0748-x. Epub 2017 Sep 21. Review.


Cadmium Causes Misfolding and Aggregation of Cytosolic Proteins in Yeast.

Jacobson T, Priya S, Sharma SK, Andersson S, Jakobsson S, Tanghe R, Ashouri A, Rauch S, Goloubinoff P, Christen P, Tamás MJ.

Mol Cell Biol. 2017 Aug 11;37(17). pii: e00490-16. doi: 10.1128/MCB.00490-16. Print 2017 Sep 1.


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

Carra S, Alberti S, Arrigo PA, Benesch JL, Benjamin IJ, Boelens W, Bartelt-Kirbach B, Brundel BJJM, Buchner J, Bukau B, Carver JA, Ecroyd H, Emanuelsson C, Finet S, Golenhofen N, Goloubinoff P, Gusev N, Haslbeck M, Hightower LE, Kampinga HH, Klevit RE, Liberek K, Mchaourab HS, McMenimen KA, Poletti A, Quinlan R, Strelkov SV, Toth ME, Vierling E, Tanguay RM.

Cell Stress Chaperones. 2017 Jul;22(4):601-611. doi: 10.1007/s12192-017-0787-8. Epub 2017 Mar 31. Review.


Editorial: The HSP70 Molecular Chaperone Machines.

Goloubinoff P.

Front Mol Biosci. 2017 Jan 24;4:1. doi: 10.3389/fmolb.2017.00001. eCollection 2017. No abstract available.


Corrigendum to 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 [Gene 290 (2002): 63-71].

Lechner E, Goloubinoff P, Genschik P, Shen WH.

Gene. 2017 Mar 20;605:131. doi: 10.1016/j.gene.2016.12.019. Epub 2017 Jan 3. No abstract available.


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

De Los Rios P, Goloubinoff P.

Nat Struct Mol Biol. 2016 Sep 6;23(9):766-9. doi: 10.1038/nsmb.3283. No abstract available.


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

Gat-Yablonski G, Finka A, Pinto G, Quadroni M, Shtaif B, Goloubinoff P.

Aging (Albany NY). 2016 Aug;8(8):1735-58. doi: 10.18632/aging.101009.


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

Finka A, Mattoo RU, Goloubinoff P.

Annu Rev Biochem. 2016 Jun 2;85:715-42. doi: 10.1146/annurev-biochem-060815-014124. Epub 2016 Mar 31. Review.


Mechanisms of protein homeostasis in health, aging and disease.

Goloubinoff P.

Swiss Med Wkly. 2016 Apr 5;146:w14306. doi: 10.4414/smw.2016.14306. eCollection 2016. Review.


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

Finka A, Sharma SK, Goloubinoff P.

Front Mol Biosci. 2015 Jun 5;2:29. doi: 10.3389/fmolb.2015.00029. eCollection 2015. Review.


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

Finka A, Sood V, Quadroni M, Rios Pde L, Goloubinoff P.

Cell Stress Chaperones. 2015 Jul;20(4):605-20. doi: 10.1007/s12192-015-0583-2. Epub 2015 Apr 8.


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

Mattoo RU, Goloubinoff P.

Cell Mol Life Sci. 2014 Sep;71(17):3311-25. doi: 10.1007/s00018-014-1627-y. Epub 2014 Apr 24. Review.


Physical interaction between bacterial heat shock protein (Hsp) 90 and Hsp70 chaperones mediates their cooperative action to refold denatured proteins.

Nakamoto H, Fujita K, Ohtaki A, Watanabe S, Narumi S, Maruyama T, Suenaga E, Misono TS, Kumar PK, Goloubinoff P, Yoshikawa H.

J Biol Chem. 2014 Feb 28;289(9):6110-9. doi: 10.1074/jbc.M113.524801. Epub 2014 Jan 12.


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

Mattoo RU, Farina Henriquez Cuendet A, Subanna S, Finka A, Priya S, Sharma SK, Goloubinoff P.

Front Mol Biosci. 2014 Jul 31;1:7. doi: 10.3389/fmolb.2014.00007. eCollection 2014.


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

Goloubinoff P.

Front Mol Biosci. 2014 Mar 27;1:1. doi: 10.3389/fmolb.2014.00001. eCollection 2014. No abstract available.


Hsp110 is a bona fide chaperone using ATP to unfold stable misfolded polypeptides and reciprocally collaborate with Hsp70 to solubilize protein aggregates.

Mattoo RU, Sharma SK, Priya S, Finka A, Goloubinoff P.

J Biol Chem. 2013 Jul 19;288(29):21399-411. doi: 10.1074/jbc.M113.479253. Epub 2013 Jun 4.


Molecular chaperones as enzymes that catalytically unfold misfolded polypeptides.

Priya S, Sharma SK, Goloubinoff P.

FEBS Lett. 2013 Jun 27;587(13):1981-7. doi: 10.1016/j.febslet.2013.05.014. Epub 2013 May 16. Review.


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

Finka A, Goloubinoff P.

Cell Stress Chaperones. 2014 Jan;19(1):83-90. doi: 10.1007/s12192-013-0436-9. Epub 2013 May 12.


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

Priya S, Sharma SK, Sood V, Mattoo RU, Finka A, Azem A, De Los Rios P, Goloubinoff P.

Proc Natl Acad Sci U S A. 2013 Apr 30;110(18):7199-204. doi: 10.1073/pnas.1219867110. Epub 2013 Apr 12.


The membrane-associated transient receptor potential vanilloid channel is the central heat shock receptor controlling the cellular heat shock response in epithelial cells.

Bromberg Z, Goloubinoff P, Saidi Y, Weiss YG.

PLoS One. 2013;8(2):e57149. doi: 10.1371/journal.pone.0057149. Epub 2013 Feb 27.


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

Finka A, Goloubinoff P.

Cell Stress Chaperones. 2013 Sep;18(5):591-605. doi: 10.1007/s12192-013-0413-3. Epub 2013 Feb 21.


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

Natalello A, Mattoo RU, Priya S, Sharma SK, Goloubinoff P, Doglia SM.

J Mol Biol. 2013 Apr 12;425(7):1158-71. doi: 10.1016/j.jmb.2012.12.025. Epub 2013 Jan 7.


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

Jacobson T, Navarrete C, Sharma SK, Sideri TC, Ibstedt S, Priya S, Grant CM, Christen P, Goloubinoff P, Tamás MJ.

J Cell Sci. 2012 Nov 1;125(Pt 21):5073-83. doi: 10.1242/jcs.107029. Epub 2012 Sep 3.


Plasma membrane cyclic nucleotide gated calcium channels control land plant thermal sensing and acquired thermotolerance.

Finka A, Cuendet AF, Maathuis FJ, Saidi Y, Goloubinoff P.

Plant Cell. 2012 Aug;24(8):3333-48. Epub 2012 Aug 17.


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

Horváth I, Glatz A, Nakamoto H, Mishkind ML, Munnik T, Saidi Y, Goloubinoff P, Harwood JL, Vigh L.

Prog Lipid Res. 2012 Jul;51(3):208-20. doi: 10.1016/j.plipres.2012.02.002. Epub 2012 Mar 29. Review.


Protein folding: Chaperoning protein evolution.

De Los Rios P, Goloubinoff P.

Nat Chem Biol. 2012 Feb 15;8(3):226-8. doi: 10.1038/nchembio.791. No abstract available.


How do plants feel the heat?

Mittler R, Finka A, Goloubinoff P.

Trends Biochem Sci. 2012 Mar;37(3):118-25. doi: 10.1016/j.tibs.2011.11.007. Epub 2012 Jan 9. Review.


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

Iosefson O, Sharon S, Goloubinoff P, Azem A.

Cell Stress Chaperones. 2012 Jan;17(1):57-66. doi: 10.1007/s12192-011-0285-3. Epub 2011 Aug 3.


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

Sharma SK, De Los Rios P, Goloubinoff P.

Proteins. 2011 Jun;79(6):1991-8. doi: 10.1002/prot.23024. Epub 2011 Apr 12.


The novel hydroxylamine derivative NG-094 suppresses polyglutamine protein toxicity in Caenorhabditis elegans.

Haldimann P, Muriset M, Vígh L, Goloubinoff P.

J Biol Chem. 2011 May 27;286(21):18784-94. doi: 10.1074/jbc.M111.234773. Epub 2011 Apr 6.


Molecular chaperones and associated cellular clearance mechanisms against toxic protein conformers in Parkinson's disease.

Hinault MP, Farina-Henriquez-Cuendet A, Goloubinoff P.

Neurodegener Dis. 2011;8(6):397-412. doi: 10.1159/000324514. Epub 2011 Mar 16. Review.


Membrane lipid composition affects plant heat sensing and modulates Ca(2+)-dependent heat shock response.

Saidi Y, Peter M, Finka A, Cicekli C, Vigh L, Goloubinoff P.

Plant Signal Behav. 2010 Dec;5(12):1530-3. Epub 2010 Dec 1.


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

Saidi Y, Finka A, Goloubinoff P.

New Phytol. 2011 May;190(3):556-65. doi: 10.1111/j.1469-8137.2010.03571.x. Epub 2010 Dec 7. Review.


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

Sharma SK, De los Rios P, Christen P, Lustig A, Goloubinoff P.

Nat Chem Biol. 2010 Dec;6(12):914-20. doi: 10.1038/nchembio.455. Epub 2010 Oct 17.


Stable alpha-synuclein oligomers strongly inhibit chaperone activity of the Hsp70 system by weak interactions with J-domain co-chaperones.

Hinault MP, Cuendet AF, Mattoo RU, Mensi M, Dietler G, Lashuel HA, Goloubinoff P.

J Biol Chem. 2010 Dec 3;285(49):38173-82. doi: 10.1074/jbc.M110.127753. Epub 2010 Sep 16.


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

Finka A, Mattoo RU, Goloubinoff P.

Cell Stress Chaperones. 2011 Jan;16(1):15-31. doi: 10.1007/s12192-010-0216-8. Epub 2010 Aug 9.


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

Saidi Y, Schaefer DG, Goloubinoff P, Zrÿd JP, Finka A.

Plant Signal Behav. 2009 May;4(5):457-9. Epub 2009 May 24.


The heat shock response in moss plants is regulated by specific calcium-permeable channels in the plasma membrane.

Saidi Y, Finka A, Muriset M, Bromberg Z, Weiss YG, Maathuis FJ, Goloubinoff P.

Plant Cell. 2009 Sep;21(9):2829-43. doi: 10.1105/tpc.108.065318. Epub 2009 Sep 22.


Disaggregating chaperones: an unfolding story.

Sharma SK, Christen P, Goloubinoff P.

Curr Protein Pept Sci. 2009 Oct;10(5):432-46. Review.


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

Finka A, Saidi Y, Goloubinoff P, Neuhaus JM, Zrÿd JP, Schaefer DG.

Cell Motil Cytoskeleton. 2008 Oct;65(10):769-84. doi: 10.1002/cm.20298.


Heavy metal ions are potent inhibitors of protein folding.

Sharma SK, Goloubinoff P, Christen P.

Biochem Biophys Res Commun. 2008 Jul 25;372(2):341-5. doi: 10.1016/j.bbrc.2008.05.052. Epub 2008 May 21.


Enhanced heat shock protein 70 expression alters proteasomal degradation of IkappaB kinase in experimental acute respiratory distress syndrome.

Weiss YG, Bromberg Z, Raj N, Raphael J, Goloubinoff P, Ben-Neriah Y, Deutschman CS.

Crit Care Med. 2007 Sep;35(9):2128-38.


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

Goloubinoff P, De Los Rios P.

Trends Biochem Sci. 2007 Aug;32(8):372-80. Epub 2007 Jul 12. Review.


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

Saidi Y, Domini M, Choy F, Zryd JP, Schwitzguebel JP, Goloubinoff P.

Plant Cell Environ. 2007 Jun;30(6):753-63.

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