Journals
2022
Guihur A., Rebeaud M.E., Bourgine B., Goloubinoff P., 2022/07. How do humans and plants feel the heat? Trends in plant science, 27 (7) pp. 630-632. Peer-reviewed.
Guihur Anthony, Rebeaud Mathieu E., Goloubinoff Pierre, 2022/06. How do plants feel the heat and survive? Trends in Biochemical Sciences. Peer-reviewed.
2021
Mathangasinghe Y., Fauvet B., Jane S.M., Goloubinoff P., Nillegoda N.B., 2021/06/01. The Hsp70 chaperone system: distinct roles in erythrocyte formation and maintenance. Haematologica, 106 (6) pp. 1519-1534. Peer-reviewed.
Rebeaud M.E., Mallik S., Goloubinoff P., Tawfik D.S., 2021/05/25. On the evolution of chaperones and cochaperones and the expansion of proteomes across the Tree of Life. Proceedings of the National Academy of Sciences of the United States of America, 118 (21) pp. e2020885118. Peer-reviewed.
Iljina M., Mazal H., Goloubinoff P., Riven I., Haran G., 2021/04/16. Entropic Inhibition: How the Activity of a AAA+ Machine Is Modulated by Its Substrate-Binding Domain. ACS chemical biology, 16 (4) pp. 775-785. Peer-reviewed.
Fauvet B., Finka A., Castanié-Cornet M.P., Cirinesi A.M., Genevaux P., Quadroni M., Goloubinoff P., 2021. Bacterial Hsp90 Facilitates the Degradation of Aggregation-Prone Hsp70-Hsp40 Substrates. Frontiers in molecular biosciences, 8 p. 653073. Peer-reviewed.
2020
Guihur A., Fauvet B., Finka A., Quadroni M., Goloubinoff P., 2020/12/21. Quantitative proteomic analysis to capture the role of heat-accumulated proteins in moss plant acquired thermotolerance. Plant, cell & environment, 44 (7) pp. 2117-2133. Peer-reviewed.
Kumar V., Peter J.J., Sagar A., Ray A., Jha M.P., Rebeaud M.E., Tiwari S., Goloubinoff P., Ashish F., Mapa K., 2020/02. Interdomain communication suppressing high intrinsic ATPase activity of Sse1 is essential for its co-disaggregase activity with Ssa1. The FEBS journal, 287 (4) pp. 671-694. Peer-reviewed.
Guihur A., Rebeaud M.E., Fauvet B., Tiwari S., Weiss Y.G., Goloubinoff P., 2020. Moderate Fever Cycles as a Potential Mechanism to Protect the Respiratory System in COVID-19 Patients. Frontiers in medicine, 7 p. 564170. Peer-reviewed.
2019
Mazal H., Iljina M., Barak Y., Elad N., Rosenzweig R., Goloubinoff P., Riven I., Haran G., 2019/03/29. Tunable microsecond dynamics of an allosteric switch regulate the activity of a AAA+ disaggregation machine. Nature communications, 10 (1) p. 1438. Peer-reviewed.
Kampinga H.H., Andreasson C., Barducci A., Cheetham M.E., Cyr D., Emanuelsson C., Genevaux P., Gestwicki J.E., Goloubinoff P., Huerta-Cepas J. et al., 2019/01. Function, evolution, and structure of J-domain proteins. Cell stress & chaperones, 24 (1) pp. 7-15. Peer-reviewed.
2018
Goloubinoff, P., Sassi, A.S., Fauvet, B., Barducci, A. & De Los Rios, P. (2018). Chaperones convert the energy from ATP into the nonequilibrium stabilization of native proteins. Nature Chemical Biology (2018). https://doi.org/10.1038/s41589-018-0013-8
Tamás MJ, Fauvet B, Christen P, Goloubinoff P. Misfolding and aggregation of nascent proteins: a novel mode of toxic cadmium action in vivo. Curr Genet. 2018 Feb;64(1):177-181.DOI:10.1007/s00294-017-0748-x. Epub 2017 Sep 21. Review.
2017
Goloubinoff P. (2017). The HSP70 molecular chaperone machines. Frontiers in Molecular Biosciences, https://doi.org/10.3389/fmolb.2017.00001
Carra S., Alberti S., Arrigo P., Benesch J., Benjamin I., Boelens W. , Bartelt-Kirbach B., Bianca J., Brundel B., Johannes Buchner J., Bukau B., Carver J., Ecroyd H., Emanuelsson C., Finet S., Golenhofen N., Goloubinoff P., Gusev N., Haslbeck M., Hightower H., Kampinga H., Klevit R., Liberek K., Hassane S., Mchaourab H. Kathryn A. McMenimen K., Poletti A., Quinlan R., Strelkov S., Melinda E., Toth M., Vierling E., Tanguay R. (2017). The growing world of small heat shock proteins: from structure to functions. Cell Stress and Chaperones DOI:10.1007/s12192-017-0787-8
Jacobson T., Priya S., Sharma SK., Andersson S., Jakobsson S., Tanghe R., Ashouri A., Rauch S., Goloubinoff P., Christen P. and Tamás MJ. Cadmium causes misfolding and aggregation of cytosolic proteins in yeast. Mol Cell Biol. 2017 Aug 11;37(17). pii: e00490-16. DOI:10.1128/MCB.00490-16
2016
Goloubinoff P. (2016). Mechanisms of protein homeostasis in health aging and disease. Swiss Med Wkly. 2016 Apr 5;146:w14306. eCollection 2016. https://doi.org/10.4414/smw.2016.14306
Finka A., Mattoo RUH and Goloubinoff P (2016). Experimental milestones in the discovery of molecular chaperones as polypeptide unfolding enzymes. Annual Reviews of Biochemistry. 2016 Jun 2;85:715-742. https://doi.org/10.1146/annurev-biochem-060815-014124
De Los Rios P, Goloubinoff P. (2016). Hsp70 chaperones use ATP to remodel native protein oligomers and stable aggregates by entropic pulling. Nat Struct Mol Biol. 2016 Sep 6;23(9):766-9. DOI:10.1038/nsmb.3283
Gat-Yablonski G, Finka A, Pinto G, Quadroni M, Shtaif B, Goloubinoff P. Quantitative proteomics of rat livers shows that unrestricted feeding is stressful for proteostasis with implications on life span. Aging (Albany NY). 2016 Aug 9. https://doi.org/10.18632/aging.101009
2015
Finka A, Sharma SK and Goloubinoff P. (2015). Multi-layered Molecular Mechanisms of polypeptide Holding, Unfolding and Disaggregation by HSP70/HSP110 chaperones. Frontiers in Molecular Biosciences 2, 29. doi: 10.3389/fmolb.2015.00029
Finka A, Sood V, Quadroni M, De Los Rios P and Goloubinoff P (2015). Quantitative proteomics of heat-treated human cells show an across-the-board mild depletion of housekeeping proteins to massively accumulate few HSPs. Cell Stress and Chaperones. 2015 Jul;20(4):605-20. doi: 10.1007/s12192-015-0583-2
2014
Mattoo, RUH. and Goloubinoff, P. (2014). Molecular chaperones are nano-machines that catalytically unfold misfolded and alter-natively folded proteins. Cell. and Mol. Life Sc. 2014 Sep;71(17):3311-25. doi: 10.1007/s00018-014-1627-y.
Mattoo RUH and Goloubinoff P. (2014). Recruiting unfolding chaperones to solubilize misfolded recombinant proteins. in Protein Aggregation in Bacteria: Functional and Structural Properties of Inclusion Bodies in Bacterial Cells. pp 63-75. eds. Lotti M and Doglia S., John Wiley & Sons, Inc.
Mattoo, RUH, Farina-Henriquez-Cuendet, A, Subbanna S, Andrija F, Smriti P, Sharma, S.K and Goloubinoff, P. (2014) Synergism between a foldase and an unfoldase: Reciprocal dependence between the thioredoxin-like activity of DnaJ and the polypeptide-unfolding activity of DnaK. Front. Mol. Biosci. DOI: 10.3389/fmolb.2014.00007
Finka, A. and Goloubinoff, P. (2014). The CNGCb and CNGCd genes from Physcomitrella Patens moss encode for thermo-sensory calcium channels responding to fluidity changes in the plasma membrane". Cell Stress and Chaperones, 19: 83-90. [Pubmed]
Nakamoto, H., Fujita, K., Ohtaki, A., Watanabe, S., Narumi, S., Maruyama, T., Suenaga, E., Misono, TS., Kumar, PK., Goloubinoff, P. and Yoshikawa, H. (2014). Physical Interaction between Bacterial Heat Shock Protein 90 (Hsp90) and Hsp70 Chaperones Mediates Their Cooperative Action to Refold Denatured Proteins. Journal of Biological Chemistry, 289, 6110-6119. [Pubmed]
Goloubinoff, P. (2014). Recent and future grand challenges in protein folding, misfolding, and degradation. Front. Mol. Biosci. 1:1. doi: 10.3389/fmolb.2014.00001
Mattoo, RUH. and Goloubinoff, P. (2014). Molecular chaperones are nano-machines that catalytically unfold misfolded and alter-natively folded proteins. Cell. and Mol. Life Sc. In press DOI: 10.1007/s00018-014-1627-y
2013
Natalello, N., Mattoo, RUH., Priya, S., Sharma S.K., Goloubinoff, P. and Doglia S. M. (2013). Biophysical Characterization of Two Different Stable Misfolded Monomeric Polypeptides That Are Chaperone-Amenable Substrates. J Mol Biol. 2013 Apr 12;425(7):1158-1171.
Bromberg, Z., Goloubinoff, P., Saidi, Y. and Weiss, YG (2013). The Membrane-Associated Transient Receptor Potential Vanilloid Channel is The Central Heat Shock Receptor Controlling The Cellular Heat Shock Response In Epithelial Cells. PlosOne, February 2013, Volume 8, Issue 2, e57149
Finka, A and Goloubinoff, P. (2013). Proteomic Data From Human Cell Cultures Refine Mechanisms of Chaperone-Mediated Protein homeostasis. Cell Stress and Chaperones, Sep;18(5):591-605. doi: 10.1007/s12192-013-0413-3. Recommended by the “Faculty of 1000”
Priya, S., Sharma, SK., Sood, V., Mattoo, RUH., Finka, A, Azem, A., De Los Rios, P. and Goloubinoff, P. (2013). GroEL and CCT are catalytic unfoldases mediating out-of-cage polypeptide refolding without ATP. Proc Natl Acad Sci U S A. 110(18):7199-204. doi: 10.1073/pnas.1219867110.
Priya S, Sharma, SK. and Goloubinoff, P. (2013). Molecular chaperones as enzymes that catalytically unfold misfolded polypeptides. FEBS Lett. 587(13):1981-7.
Mattoo, RUH., Sharma, SK., Priya S, Finka A, Goloubinoff P. (2013). Hsp110 is a bona fide chaperone using ATP to unfold stable misfolded polypeptides and reciprocally collaborate with Hsp70 to solubilize protein aggregates. J. Biol. Chem. Jul 19;288(29):21399-411. doi: 10.1074/jbc.M113.479253. Epub 2013 Jun 4.
2012
A. Finka, A. Farina Henriquez Cuendet, F.J.M Maathuis, Y. Saidi and P. Goloubinoff. The Plant Cell. 2012.
De Los Rios P., Goloubinoff P. (2012). Protein folding: Chaperoning protein evolution. Nature Chemical Biology 8(3), pp. 226-228, 2012. [DOI] [Web of Science] [Pubmed] 
Iosefson O., Sharon S., Goloubinoff P., Azem A. (2012). Reactivation of protein aggregates by mortalin and Tid1-the human mitochondrial Hsp70 chaperone system. Cell Stress and Chaperones 17(1), pp. 57-66, 2012. [DOI] [Web of Science] [Pubmed]
Horváth I, Glatz A, Nakamoto H, Mishkind ML, Munnik T, Saidi Y, Pierre Goloubinoff. (2012). Heat shock response in photosynthtic organism:membrane and lipid connections. Prog Lipid Res. 2012; 2012 Jul;51(3):208-20.http://www.ncbi.nlm.nih.gov/pubmed/22484828
2011
Sharma S.K., De Los Rios P., Goloubinoff P. (2011). Probing the different chaperone activities of the bacterial HSP70-HSP40 system using a thermolabile luciferase substrate. Proteins 79(6), pp. 1991-1998, 2011. [DOI] [Web of Science] [Pubmed]
Haldimann P., Muriset M., Vígh L., Goloubinoff P. (2011). The novel hydroxylamine derivative NG-094 suppresses polyglutamine protein toxicity in Caenorhabditis elegans. Journal of Biological Chemistry 286(21), pp. 18784-18794, 2011. [DOI] [Web of Science] [Pubmed]
Finka A., Mattoo R.U., Goloubinoff P. (2011). Meta-analysis of heat- and chemically upregulated chaperone genes in plant and human cells. Cell Stress and Chaperones 16(1), pp. 15-31, 2011. [DOI] [Web of Science] [Pubmed]
Hinault M.P., Farina-Henriquez-Cuendet A., Goloubinoff P. (2011). Molecular chaperones and associated cellular clearance mechanisms against toxic protein conformers in Parkinson's disease. Neuro-degenerative Diseases 8(6), pp. 397-412, 2011. [DOI] [Web of Science] [Pubmed]
Saidi Y., Finka A., Goloubinoff P. (2011). Heat perception and signalling in plants: a tortuous path to thermotolerance. New Phytologist 190(3), pp. 556-565, 2011. [DOI] [Web of Science] [Pubmed]
2010
Hinault M.P., Farina Henriquez Cuendet A.F., Mattoo R.U., Mensi M., Dietler G., Lashuel H.A., Goloubinoff P. (2010). Stable alpha-synuclein oligomers strongly inhibit chaperone activity of the Hsp70 system by weak interactions with J-domain co-chaperones. Journal of Biological Chemistry 285(49), pp. 38173-38182, 2010. [DOI] [Web of Science] [Pubmed]
Sharma S.K., De los Rios P., Christen P., Lustig A., Goloubinoff P. (2010). The kinetic parameters and energy cost of the Hsp70 chaperone as a polypeptide unfoldase. Nature Chemical Biology 6(12), pp. 914-920, 2010. [DOI] [Web of Science] [Pubmed]
Saidi Y., Peter M., Finka A., Cicekli C., Vigh L., Goloubinoff P. (2010). Membrane lipid composition affects plant heat sensing and modulates Ca ( 2+) -dependent heat shock response. Plant Signaling and Behavior 5(12), pp. 1530-1533, 2010. [DOI] [Pubmed]
2009
Saidi Y., Finka A., Muriset M., Bromberg Z., Weiss Y.G., Maathuis F.J., Goloubinoff P. (2009). The heat shock response in moss plants is regulated by specific calcium-permeable channels in the plasma membrane. Plant Cell 21(9), pp. 2829-2843, 2009. [DOI] [Web of Science] [Pubmed]
Saidi Y., Schaefer D.G., Goloubinoff P., Zrÿd J.P., Finka A. (2009). The CaMV 35S promoter has a weak expression activity in dark grown tissues of moss Physcomitrella patens. Plant Signaling and Behavior 4(5), pp. 457-459, 2009. [DOI] [Pubmed] .
Sharma S.K., Christen P., Goloubinoff P. (2009). Disaggregating chaperones: an unfolding story. Current Protein and Peptide Science 10(5), pp. 432-446, 2009. [DOI] [Web of Science] [Pubmed] .
2008
Finka A., Saidi Y., Goloubinoff P., Neuhaus J.M., Zrÿd J.P., Schaefer D.G. (2008). The knock-out of ARP3a gene affects F-actin cytoskeleton organization altering cellular tip growth, morphology and development in moss Physcomitrella patens. Cell Motility and the Cytoskeleton 65(10), pp. 769-784, 2008. [DOI] [Web of Science] [Pubmed]
Sharma S.K., Goloubinoff P., Christen P. (2008). Heavy metal ions are potent inhibitors of protein folding. Biochemical and Biophysical Research Communications 372(2), pp. 341-345, 2008. [DOI] [Web of Science] [Pubmed]
Bromberg Z., Raj N., Goloubinoff P., Deutschman C.S., Weiss Y.G. (2008). Enhanced expression of 70-kilodalton heat shock protein limits cell division in a sepsis-induced model of acute respiratory distress syndrome. Critical Care Medicine 36(1), pp. 246-255, 11-2008. [DOI] [Web of Science] [Pubmed]
2007
Finka A., Schaefer D.G., Saidi Y., Goloubinoff P., Zrÿd J.P. (2007). In vivo visualization of F-actin structures during the development of the moss Physcomitrella patens. New Phytologist 174(1), pp. 63-76, 2007. [DOI] [Web of Science] [Pubmed].
Goloubinoff, P., De Los Rios P. (2007). The mechanism of Hsp70 chaperones: (entropic) pulling the models together. Trends in Biochemical Sciences 32(8), pp. 372-80, 08-2007.
Hinault M. P., Goloubinoff P. (2007). Molecular crime and cellular punishment: active detoxification of misfolded and aggregated proteins in the cell by the chaperone and protease networks. Advances in Experimental Medicine and Biology 594, pp. 47-54, 2007.
Saidi Y., Domini M., Choy F., Zryd J.P., Schwitzguebel J.P., Goloubinoff P. (2007) Activation of the heat shock response in plants by chlorophenols: transgenic Physcomitrella patens as a sensitive biosensor for organic pollutants. Plant, Cell and Environment 30(6), pp. 753-763, 2007. [DOI] [Web of Science] [Pubmed].
Weiss Y.G., Bromberg Z., Raj N., Raphael J., Goloubinoff P., Ben-Neriah Y., Deutschman C.S. (2007) Enhanced heat shock protein 70 expression alters proteasomal degradation of IkappaB kinase in experimental acute respiratory distress syndrome. Critical Care Medicine 35(9), pp. 2128-2138, 2007. [DOI] [Web of Science] [Pubmed].
2006
Hinault M.-P., Ben-Zi, A. and Goloubinoff, P. (2006). Chaperones and Protease: Cellular Folding Controlling Factors of Proteins in Neurodegenerative Disease and Aging. Journal of Molecular Neurosciences 30, 293-310.
Hinault M.-P. and Goloubinoff, P. (2006). Molecular crime and cellular punishment in Molecular aspects of the strees response: Chaperones, membranes and networks. Adv. Exp. Med. Biol. 594:47-54.
Horvath I., Balogi Z., Giese K., Chergy O., Glatz A., Vass I., Goloubinoff P., Vierling E., Vigh L. (2006). Small heat shock proteins interact with membranes and affect membrane physical state and function. FEBS Journal 273, pp. 81-81, 06-2006. [Web of Science]
De Los Rios P., Ben-Zvi A., Slutsky O., Azem A., Goloubinoff P. (2006). Hsp70 chaperones accelerate protein translocation and the unfolding of stable protein aggregates by entropic pulling. Proceedings of the National Academy of Sciences of the United States of America 103(16), pp. 6166-71, 04-2006. [DOI] [Web of Science] [Pubmed].
Sharma S.K., Christen P., Goloubinoff P. (2006). Disaggregating chaperones: an unfolding story. Current Protein and Peptide Science 10(5), pp. 432-446, 2009. [DOI] [Web of Science] [Pubmed]
2005
Shigapova, N., Török, S., Balogh, G., Goloubinoff, P., Vigh, L. and Horvath, I. (2005). Membrane fluidization triggers membrane remodeling which affects the thermotolerance in Escherichia coli. Biochem Biophys Res Commun. 328, 1216-23.
Saidi, Y., Finka, A., Zryd, J.P., Schaefer, D.G, and Goloubinoff, P. (2005). Controlled expression of recombinant proteins in Physcomitrella Patens by a conditional heat-shock promoter: a tool for plant research and biotechnology. Plant Molocular Biology. 59, issue 5, 695-709.
de Marco A., Vigh L., Diamant S., Goloubinoff P. (2005). Native folding of aggregation-prone recombinant proteins in Escherichia coli by osmolytes, plasmid- or benzyl alcohol-overexpressed molecular chaperones. Cell Stress and Chaperones 10(4), pp. 329-39, 2005. [DOI] [Web of Science] [Pubmed].
Balogi Z., Glatz A., Balogh G., Nagy E., Liberek K., Debreczeny M., Goloubinoff P., Horvath I., Vigh L. (2005). The emerging role for small heat-shock proteins in the regulation of lipid composition and dynamics of cell membranes. FEBS Journal 272, pp. 358-358, 07-2005. [Web of Science]
2004
Ben-Zvi, A., De Los Rios, P., Dietler, G. and Goloubinoff, P. (2004). Active solubilization and refolding of stable protein aggregates by cooperative unfolding action of individual HSP70 chaperones. J. Biol. Chem. 279, 37298-303.
2003
Diamant, S. Rosenthal D., Azem, A., Eliahu, N., Peres Ben-Zvi, A. and Goloubinoff, P.(2003). Dicarboxylic Amino-Acids and Glycine-Betaine Regulate Chaperone-Mediated Protein-Disaggregation Under Stress. Mol. Microbiol. 49 (2), 401-410.
Amzallag, G.N. and Goloubinoff, P. (2003). Effects of the Hsp90-inhibitor geldanamycin on steroid stress-signaling in soybean. Plant Biology. 2, 143-150.
2002
Pnueli, L., Hallak-Herr, E., Rozenberg, M., Cohen, M., Goloubinoff, P., Kaplan, A. and Mittler, R. (2002) Molecular and biochemical mechanisms associated with dormancy and drought tolerance in the desert legume Retama raetam. Plant J. 2002 Aug; 31(3):319-330.
Lechner, E., Goloubinoff, P., Genschik, P. and Shen, W-H. (2002). 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, 63-71.
Merquiol, E, Pnueli, L., Cohen, M., Simovitch, M., Rachmilevitch, S., Goloubinoff, P. and Mittler, R. (2002). Seasonal and diurnal variations in gene expression in the desert legume Retama raetam. Plant Cell and Env. 25, 1627-1638.
Ben Zvi, A. and Goloubinoff, P. (2002). Proteinaceous Infectious Behavior in non-Pathogenic proteins is controlled by molecular chaperones". J. Biol. Chem. 277 (51), 49422-49427.
2001
Ben Zvi, A. and Goloubinoff, P. (2001). Mechanisms of chaperone-mediated protein disaggregation. J. Struct. Biol. 135, 84-93.
Török, Z., Goloubinoff, P., Horváth, I., Tsvetkova, N.M., Glatz. A., Balogh, G., Varvasovszki, V., Vierling, E., Crowe J.H. and Vígh, L. (2001). "HSP17 from Synechocystis 6803 is an amphitropic protein with chaperone activity for membranes and proteins under heat-stress. Proc. Natn. Acad. Sci. U.S.A. 98, 3098-3103.
Tomoyasu, T, Mogk, A, Langen, H, Goloubinoff, P. and Bukau, B. (2001). Genetic dissection of the roles of chaperones and proteases in protein folding and degradation in the E. coli cytosol. Mol. Biol. 40, 397-413.
Diamant, S., Rosental, D., Elyahu, N. and Goloubinoff, P. (2001). Chemical Chaperones Regulate Molecular Chaperones in vitro and in Cells under Combined Salt and Heat Stresses. J. Biol. Chem. 276: 39586-39591.
2000
Diamant, S., Peres Ben-Zvi, A., Bukau B. and Goloubinoff, P. (2000). Size-Dependent Disaggregation Of Aggregated Protein Particles By The DnaK Chaperone Machinery of Escherichia coli. J. Biol. Chem. 275, 21107-21113.
Chatellier, J., Hill, F., Foster N. W., Goloubinoff, P. and Fersht, A. R. (2000). From minichaperone to GroEL: Properties of an active single-ring mutant of GroEL. J. Mol Biol. 304, 897-910.
1999
Goloubinoff, P., Mogk, A., Peres Ben Zvi, A., Tomoyasu, T. and Bukau, B. (1999). Sequential Mechanism of Solubilization and Refolding of Stable Protein Aggregates By a Bi-Chaperone Network. Proc. Natn. Acad. Sci. U.S.A. 96, 13732-13737.
Mogk, A., Tomoyasu, T., Goloubinoff, P., Rüdiger, R, Röder, D., Langen, H. and Bukau, B. (1999). Identification of thermolabile E. coli proteins: Prevention and reversion of aggregation by DnaK and ClpB. EMBO J. 18, 6934-6949.
1998
Azem, A., Weiss, C. and Goloubinoff, P. (1998). Chemical crosslinking as a method for the structural analysis of GroE chaperonin complexes. Methods in Enzymology. vol. 290, 253-268. Eds Lorimer & Baldwin.
Viitanen, P., Lorimer, G., Bergmeier, W., Weiss, C. and Goloubinoff, P. (1998). Purification, stability and characterization of mammalian mitochondrial chaperonin 60 through in vitro reconstitution of active oligomers. Methods in Enzymology. vol. 290. 203-217. Eds Lorimer & Baldwin.
Veinger, L., Diamant, S., Buchner, J. and Goloubinoff, P. (1998). The Small Heat-Shock Protein IbpB from Escherichia coli Stabilizes Stress-Denatured Proteins for Subsequent Refolding by a Multi-Chaperone Network. J. Biol Chem. 273, 11032-11037.
Diamant, S. and Goloubinoff, P.(1998). Temperature-controlled Activity of DnaK-DnaJ-GrpE Chaperones: Protein-Folding Arrest and Recovery During and After Heat-Shock Depends on Substrate Protein and GrpE concentration. Biochemistry 37, 9688-9694.
Peres Ben-Zvi, A., Chatellier, J., Fersht, A. R. and Goloubinoff, P. (1998). Minimal and optimal mechanisms for GroEL-mediated protein folding. Proc. Natn. Acad. Sci. U.S.A 95, 15275-15280.
1997
Török, S., Horvath, I., Goloubinoff, P., Kovacs, E., Glatz, A., Balogh, G. and Vigh, L. (1997). Evidence for a lipochaperonin: association of active protein-folding GroESL oligomers with lipids stabilize membranes under heat-shock conditions. Proc. Natn. Acad. Sci. U.S.A. 94, 2192-2197.
Goloubinoff, P., Diamant., S., Weiss, C. and Azem, A (1997). GroES binding regulates GroEL chaperonin activity under heat-shock. Febs Lett. 407, 215-219.
1996
Török, S., Vigh, L. and Goloubinoff, P. (1996). Fluorescence Detection of Symmetric GroEL14(GroES7)2 Hetero-oligomers Involved in Protein-Release During The Chaperonin Cycle. J. Biol Chem. 271, 16180-16186.
1995
Diamant, S., Azem, A., Weiss, C. and Goloubinoff, P. (1995). Effect of Free and ATP-bound Magnesium and Manganese ions on the ATPase Activity of Chaperonin GroEL14. Biochemistry. 34, 273-277.
Weiss, C. and Goloubinoff, P.(1995). A Mutant at Position 87 of the GroEL Chaperonin is Affected in ATP Hydrolysis and Protein Binding. J. Biol. Chem. 270, 13956-13960.
1994
Lerner, H.R, Amzallag, G.N., Friedman, Y. and Goloubinoff, P. (1994). The response of plants to salinity: from turgor adjustments to genome modification. Israel J. Plant Sci. 42, 285-300.
Azem, A., Diamant, S. and Goloubinoff, P. (1994). Effect of Divalent Cations on the Molecular Structure of the GroEL Oligomer. Biochemistry. 33, 6671-6675.
Azem, A., Kessel, M. and Goloubinoff, P. (1994). Characterization of a Functional GroEL14(GroES7)2 Chaperonin Hetero-oligomer. Science. 265, 654-656.
1993
Goloubinoff, P., Pääbo, S. and Wilson, A. C. (1993). Evolution of Maize According to Nuclear DNA Sequences from Archaeological Specimens. Proc. Natn. Acad. Sci. U.S.A. 90, 1997-2001.
1990
Viitanen, P.V., Lubben, T.H., Reed-Scioli, J., Goloubinoff, P., O'Keefe, D.P. and Lorimer, G.H. (1990). Chaperonin-facilitated refolding of Ribulose bisphosphate carboxylase and ATP-hydrolysis by chaperonin 60 (groEL) are K+-dependent. Biochemistry 29, 5665-5671.
1989
Goloubinoff, P., Gatenby, A.A. and Lorimer, G.H. (1989). GroE heat-shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli. Nature. 337, 44-47.
Goloubinoff, P., Christeller, J.T., Gatenby, A.A. and Lorimer, G.H. (1989). Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and Mg-ATP. Nature. 342, 884-889.
1988
Goloubinoff, P., Golden, S.S., Brusslan, J., Haselkorn, R. and Edelman, M. (1988). Characterization of the photosystem II 32kDa protein in Synechococcus PCC7942. Plant Molec. Biol. 11, 441-447.
1987
Eyal, Y., Goloubinoff, P. and Edelman, M. (1987). The amino terminal region delimited by Met1 and Met37 is an integral part of the 32kDa herbicide binding protein. Plant Molec. Biol. 8, 337-343.
1986
Fromm, H., Edelman, M., Koller, B., Goloubinoff, P. and Galun, E. (1986). The enigma of the gene coding for ribosomal protein S12 in the chloroplasts of Nicotiana. Nucleic. Acid Res. 14, 883-898
1984
Goloubinoff, P., Edelman, M. and Hallick, R.B. (1984). Chloroplast-coded atrazine resistance in Solanum nigrum; psbA loci from susceptible and resistant biotypes are isogenic except for a single codon change. Nucleic Acid Res. 24, 9489-9496.
Marder, J.B., Goloubinoff, P., and Edelman, M. (1984). Molecular architecture of the rapidly metabolized 32-kilodalton protein of photosystem II: Indications for COOH-terminal processing of a chloroplast membrane polypeptide. J. Biol. Chem. 259, 3900-3908.
