| Year |
Citation |
Score |
| 2024 |
Mayer MP, Blair L, Blatch GL, Borges TJ, Chadli A, Chiosis G, de Thonel A, Dinkova-Kostova A, Ecroyd H, Edkins AL, Eguchi T, Fleshner M, Foley KP, Fragkostefanakis S, Gestwicki J, ... Goloubinoff P, et al. Stress Biology: Complexity and Multifariousness in Health and Disease. Cell Stress & Chaperones. PMID 38311120 DOI: 10.1016/j.cstres.2024.01.006 |
0.373 |
|
| 2023 |
Guihur A, Bourgine B, Rebeaud ME, Goloubinoff P. Design of an Arabidopsis thaliana reporter line to detect heat-sensing and signaling mutants. Plant Methods. 19: 56. PMID 37291595 DOI: 10.1186/s13007-023-01033-x |
0.705 |
|
| 2022 |
Tiwari S, Fauvet B, Assenza S, De Los Rios P, Goloubinoff P. A fluorescent multi-domain protein reveals the unfolding mechanism of Hsp70. Nature Chemical Biology. PMID 36266349 DOI: 10.1038/s41589-022-01162-9 |
0.338 |
|
| 2022 |
Guihur A, Rebeaud ME, Goloubinoff P. How do plants feel the heat and survive? Trends in Biochemical Sciences. PMID 35660289 DOI: 10.1016/j.tibs.2022.05.004 |
0.77 |
|
| 2022 |
Guihur A, Rebeaud ME, Bourgine B, Goloubinoff P. How do humans and plants feel the heat? Trends in Plant Science. PMID 35361524 DOI: 10.1016/j.tplants.2022.03.006 |
0.68 |
|
| 2021 |
Fauvet B, Rebeaud ME, Tiwari S, De Los Rios P, Goloubinoff P. Repair or Degrade: the Thermodynamic Dilemma of Cellular Protein Quality-Control. Frontiers in Molecular Biosciences. 8: 768888. PMID 34778379 DOI: 10.3389/fmolb.2021.768888 |
0.766 |
|
| 2021 |
Rebeaud ME, Mallik S, Goloubinoff P, Tawfik DS. 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. PMID 34001607 DOI: 10.1073/pnas.2020885118 |
0.775 |
|
| 2021 |
Fauvet B, Finka A, Castanié-Cornet MP, Cirinesi AM, Genevaux P, Quadroni M, Goloubinoff P. Bacterial Hsp90 Facilitates the Degradation of Aggregation-Prone Hsp70-Hsp40 Substrates. Frontiers in Molecular Biosciences. 8: 653073. PMID 33937334 DOI: 10.3389/fmolb.2021.653073 |
0.383 |
|
| 2021 |
Mathangasinghe Y, Fauvet B, Jane SM, Goloubinoff P, Nillegoda NB. The Hsp70 chaperone system: distinct roles in erythrocyte formation and maintenance. Haematologica. PMID 33832207 DOI: 10.3324/haematol.2019.233056 |
0.351 |
|
| 2020 |
Guihur A, Fauvet B, Finka A, Quadroni M, Goloubinoff P. Quantitative proteomic analysis to capture the role of heat-accumulated proteins in moss plant acquired thermotolerance. Plant, Cell & Environment. PMID 33314263 DOI: 10.1111/pce.13975 |
0.804 |
|
| 2020 |
Guihur A, Rebeaud ME, Fauvet B, Tiwari S, Weiss YG, Goloubinoff P. Moderate Fever Cycles as a Potential Mechanism to Protect the Respiratory System in COVID-19 Patients. Frontiers in Medicine. 7: 564170. PMID 33043037 DOI: 10.3389/Fmed.2020.564170 |
0.733 |
|
| 2019 |
Kumar V, Peter JJ, Sagar A, Ray A, Jha MP, Rebeaud ME, Tiwari S, Goloubinoff P, Ashish, Mapa K. Inter-domain communication suppressing high intrinsic ATPase activity of Sse1 is essential for its co-dissaggregase activity with Ssa1. The Febs Journal. PMID 31423733 DOI: 10.1111/Febs.15045 |
0.752 |
|
| 2019 |
Mazal H, Iljina M, Barak Y, Elad N, Rosenzweig R, Goloubinoff P, Riven I, Haran G. Tunable microsecond dynamics of an allosteric switch regulate the activity of a AAA+ disaggregation machine. Nature Communications. 10: 1438. PMID 30926805 DOI: 10.1038/S41467-019-09474-6 |
0.33 |
|
| 2018 |
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, et al. Function, evolution, and structure of J-domain proteins. Cell Stress & Chaperones. PMID 30478692 DOI: 10.1007/S12192-018-0948-4 |
0.406 |
|
| 2018 |
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. Emerging fields in chaperone proteins: A French workshop. Biochimie. 151: 159-165. PMID 29890204 DOI: 10.1016/J.Biochi.2018.06.004 |
0.385 |
|
| 2018 |
Goloubinoff P, Sassi AS, Fauvet B, Barducci A, De Los Rios P. Chaperones convert the energy from ATP into the nonequilibrium stabilization of native proteins. Nature Chemical Biology. PMID 29507388 DOI: 10.1038/S41589-018-0013-8 |
0.394 |
|
| 2018 |
Doron L, Goloubinoff P, Shapira M. ZnJ2 Is a Member of a Large Chaperone Family in the Chloroplast of Photosynthetic Organisms that Features a DnaJ-Like Zn-Finger Domain. Frontiers in Molecular Biosciences. 5: 2. PMID 29497613 DOI: 10.3389/Fmolb.2018.00002 |
0.379 |
|
| 2017 |
Tamás MJ, Fauvet B, Christen P, Goloubinoff P. Misfolding and aggregation of nascent proteins: a novel mode of toxic cadmium action in vivo. Current Genetics. PMID 28936749 DOI: 10.1007/S00294-017-0748-X |
0.336 |
|
| 2017 |
Jacobson T, Priya S, Sharma SK, Andersson S, Jakobsson S, Tanghe R, Ashouri A, Rauch S, Goloubinoff P, Christen P, Tamás MJ. Cadmium causes misfolding and aggregation of cytosolic proteins in yeast. Molecular and Cellular Biology. PMID 28606932 DOI: 10.1128/Mcb.00490-16 |
0.405 |
|
| 2017 |
Carra S, Alberti S, Arrigo PA, Benesch JL, Benjamin IJ, Boelens W, Bartelt-Kirbach B, Brundel BJ, Buchner J, Bukau B, Carver JA, Ecroyd H, Emanuelsson C, Finet S, Golenhofen N, ... Goloubinoff P, et al. The growing world of small heat shock proteins: from structure to functions. Cell Stress & Chaperones. PMID 28364346 DOI: 10.1007/S12192-017-0787-8 |
0.489 |
|
| 2017 |
Goloubinoff P. Editorial: The HSP70 Molecular Chaperone Machines. Frontiers in Molecular Biosciences. 4: 1. PMID 28174697 DOI: 10.3389/Fmolb.2017.00001 |
0.329 |
|
| 2016 |
De Los Rios P, Goloubinoff P. Hsp70 chaperones use ATP to remodel native protein oligomers and stable aggregates by entropic pulling. Nature Structural & Molecular Biology. 23: 766-9. PMID 27605203 DOI: 10.1038/Nsmb.3283 |
0.453 |
|
| 2016 |
Finka A, Mattoo RU, Goloubinoff P. Experimental Milestones in the Discovery of Molecular Chaperones as Polypeptide Unfolding Enzymes. Annual Review of Biochemistry. 85: 715-42. PMID 27050154 DOI: 10.1146/Annurev-Biochem-060815-014124 |
0.491 |
|
| 2016 |
Goloubinoff P. Mechanisms of protein homeostasis in health, aging and disease. Swiss Medical Weekly. 146: w14306. PMID 27045704 DOI: 10.4414/Smw.2016.14306 |
0.371 |
|
| 2015 |
Finka A, Sharma SK, Goloubinoff P. Multi-layered molecular mechanisms of polypeptide holding, unfolding and disaggregation by HSP70/HSP110 chaperones. Frontiers in Molecular Biosciences. 2: 29. PMID 26097841 DOI: 10.3389/Fmolb.2015.00029 |
0.514 |
|
| 2015 |
Finka A, Sood V, Quadroni M, Rios Pde L, Goloubinoff P. Quantitative proteomics of heat-treated human cells show an across-the-board mild depletion of housekeeping proteins to massively accumulate few HSPs. Cell Stress & Chaperones. 20: 605-20. PMID 25847399 DOI: 10.1007/S12192-015-0583-2 |
0.516 |
|
| 2014 |
Mattoo RU, Farina Henriquez Cuendet A, Subanna S, Finka A, Priya S, Sharma SK, Goloubinoff P. Synergism between a foldase and an unfoldase: reciprocal dependence between the thioredoxin-like activity of DnaJ and the polypeptide-unfolding activity of DnaK. Frontiers in Molecular Biosciences. 1: 7. PMID 25988148 DOI: 10.3389/Fmolb.2014.00007 |
0.393 |
|
| 2014 |
Goloubinoff P. Recent and future grand challenges in protein folding, misfolding, and degradation. Frontiers in Molecular Biosciences. 1: 1. PMID 25988142 DOI: 10.3389/Fmolb.2014.00001 |
0.445 |
|
| 2014 |
Mattoo RU, Goloubinoff P. Molecular chaperones are nanomachines that catalytically unfold misfolded and alternatively folded proteins. Cellular and Molecular Life Sciences : Cmls. 71: 3311-25. PMID 24760129 DOI: 10.1007/S00018-014-1627-Y |
0.45 |
|
| 2014 |
Nakamoto H, Fujita K, Ohtaki A, Watanabe S, Narumi S, Maruyama T, Suenaga E, Misono TS, Kumar PK, Goloubinoff P, Yoshikawa H. Physical interaction between bacterial heat shock protein (Hsp) 90 and Hsp70 chaperones mediates their cooperative action to refold denatured proteins. The Journal of Biological Chemistry. 289: 6110-9. PMID 24415765 DOI: 10.1074/Jbc.M113.524801 |
0.516 |
|
| 2014 |
Finka A, Goloubinoff P. The CNGCb and CNGCd genes from Physcomitrella patens moss encode for thermosensory calcium channels responding to fluidity changes in the plasma membrane. Cell Stress & Chaperones. 19: 83-90. PMID 23666745 DOI: 10.1007/S12192-013-0436-9 |
0.528 |
|
| 2013 |
Mattoo RU, Sharma SK, Priya S, Finka A, Goloubinoff P. Hsp110 is a bona fide chaperone using ATP to unfold stable misfolded polypeptides and reciprocally collaborate with Hsp70 to solubilize protein aggregates. The Journal of Biological Chemistry. 288: 21399-411. PMID 23737532 DOI: 10.1074/Jbc.M113.479253 |
0.471 |
|
| 2013 |
Priya S, Sharma SK, Goloubinoff P. Molecular chaperones as enzymes that catalytically unfold misfolded polypeptides Febs Letters. 587: 1981-1987. PMID 23684649 DOI: 10.1016/J.Febslet.2013.05.014 |
0.463 |
|
| 2013 |
Priya S, Sharma SK, Sood V, Mattoo RU, Finka A, Azem A, De Los Rios P, Goloubinoff P. GroEL and CCT are catalytic unfoldases mediating out-of-cage polypeptide refolding without ATP. Proceedings of the National Academy of Sciences of the United States of America. 110: 7199-204. PMID 23584019 DOI: 10.1073/Pnas.1219867110 |
0.339 |
|
| 2013 |
Bromberg Z, Goloubinoff P, Saidi Y, Weiss YG. The membrane-associated transient receptor potential vanilloid channel is the central heat shock receptor controlling the cellular heat shock response in epithelial cells. Plos One. 8: e57149. PMID 23468922 DOI: 10.1371/Journal.Pone.0057149 |
0.521 |
|
| 2013 |
Finka A, Goloubinoff P. Proteomic data from human cell cultures refine mechanisms of chaperone-mediated protein homeostasis. Cell Stress & Chaperones. 18: 591-605. PMID 23430704 DOI: 10.1007/S12192-013-0413-3 |
0.481 |
|
| 2013 |
Natalello A, Mattoo RU, Priya S, Sharma SK, Goloubinoff P, Doglia SM. Biophysical characterization of two different stable misfolded monomeric polypeptides that are chaperone-amenable substrates. Journal of Molecular Biology. 425: 1158-71. PMID 23306033 DOI: 10.1016/J.Jmb.2012.12.025 |
0.386 |
|
| 2013 |
Bromberg Z, Goloubinoff P, Saidi Y, Weiss YG. Capsaicin and capsazepine effects on heat shock protein expression in HEK293e, MLE-12, MCF-7 and HT-29 cells. Plos One. DOI: 10.1371/Journal.Pone.0057149.G001 |
0.406 |
|
| 2012 |
Jacobson T, Navarrete C, Sharma SK, Sideri TC, Ibstedt S, Priya S, Grant CM, Christen P, Goloubinoff P, Tamás MJ. Arsenite interferes with protein folding and triggers formation of protein aggregates in yeast. Journal of Cell Science. 125: 5073-83. PMID 22946053 DOI: 10.1242/Jcs.107029 |
0.409 |
|
| 2012 |
Finka A, Cuendet AF, Maathuis FJ, Saidi Y, Goloubinoff P. Plasma membrane cyclic nucleotide gated calcium channels control land plant thermal sensing and acquired thermotolerance. The Plant Cell. 24: 3333-48. PMID 22904147 DOI: 10.1105/Tpc.112.095844 |
0.432 |
|
| 2012 |
Horváth I, Glatz A, Nakamoto H, Mishkind ML, Munnik T, Saidi Y, Goloubinoff P, Harwood JL, Vigh L. Heat shock response in photosynthetic organisms: membrane and lipid connections. Progress in Lipid Research. 51: 208-20. PMID 22484828 DOI: 10.1016/J.Plipres.2012.02.002 |
0.507 |
|
| 2012 |
De Los Rios P, Goloubinoff P. Protein folding: Chaperoning protein evolution. Nature Chemical Biology. 8: 226-8. PMID 22337093 DOI: 10.1038/Nchembio.791 |
0.423 |
|
| 2012 |
Mittler R, Finka A, Goloubinoff P. How do plants feel the heat? Trends in Biochemical Sciences. 37: 118-25. PMID 22236506 DOI: 10.1016/J.Tibs.2011.11.007 |
0.44 |
|
| 2012 |
Iosefson O, Sharon S, Goloubinoff P, Azem A. Reactivation of protein aggregates by mortalin and Tid1--the human mitochondrial Hsp70 chaperone system. Cell Stress & Chaperones. 17: 57-66. PMID 21811887 DOI: 10.1007/S12192-011-0285-3 |
0.481 |
|
| 2011 |
Sharma SK, De Los Rios P, Goloubinoff P. Probing the different chaperone activities of the bacterial HSP70-HSP40 system using a thermolabile luciferase substrate. Proteins. 79: 1991-8. PMID 21488102 DOI: 10.1002/Prot.23024 |
0.486 |
|
| 2011 |
Haldimann P, Muriset M, Vígh L, Goloubinoff P. The novel hydroxylamine derivative NG-094 suppresses polyglutamine protein toxicity in Caenorhabditis elegans. The Journal of Biological Chemistry. 286: 18784-94. PMID 21471208 DOI: 10.1074/Jbc.M111.234773 |
0.455 |
|
| 2011 |
Hinault MP, Farina-Henriquez-Cuendet A, Goloubinoff P. Molecular chaperones and associated cellular clearance mechanisms against toxic protein conformers in Parkinson's disease. Neuro-Degenerative Diseases. 8: 397-412. PMID 21411979 DOI: 10.1159/000324514 |
0.364 |
|
| 2011 |
Saidi Y, Finka A, Goloubinoff P. Heat perception and signalling in plants: a tortuous path to thermotolerance. The New Phytologist. 190: 556-65. PMID 21138439 DOI: 10.1111/J.1469-8137.2010.03571.X |
0.544 |
|
| 2011 |
Finka A, Mattoo RU, Goloubinoff P. Meta-analysis of heat- and chemically upregulated chaperone genes in plant and human cells. Cell Stress & Chaperones. 16: 15-31. PMID 20694844 DOI: 10.1007/S12192-010-0216-8 |
0.523 |
|
| 2010 |
Saidi Y, Peter M, Finka A, Cicekli C, Vigh L, Goloubinoff P. Membrane lipid composition affects plant heat sensing and modulates Ca(2+)-dependent heat shock response. Plant Signaling & Behavior. 5: 1530-3. PMID 21139423 DOI: 10.4161/Psb.5.12.13163 |
0.483 |
|
| 2010 |
Sharma SK, De los Rios P, Christen P, Lustig A, Goloubinoff P. The kinetic parameters and energy cost of the Hsp70 chaperone as a polypeptide unfoldase. Nature Chemical Biology. 6: 914-20. PMID 20953191 DOI: 10.1038/Nchembio.455 |
0.405 |
|
| 2010 |
Hinault MP, Cuendet AF, Mattoo RU, Mensi M, Dietler G, Lashuel HA, Goloubinoff P. Stable alpha-synuclein oligomers strongly inhibit chaperone activity of the Hsp70 system by weak interactions with J-domain co-chaperones. The Journal of Biological Chemistry. 285: 38173-82. PMID 20847048 DOI: 10.1074/Jbc.M110.127753 |
0.416 |
|
| 2009 |
Saidi Y, Schaefer DG, Goloubinoff P, Zrÿd JP, Finka A. The CaMV 35S promoter has a weak expression activity in dark grown tissues of moss Physcomitrella patens. Plant Signaling & Behavior. 4: 457-9. PMID 19816109 DOI: 10.4161/Psb.4.5.8541 |
0.4 |
|
| 2009 |
Saidi Y, Finka A, Muriset M, Bromberg Z, Weiss YG, Maathuis FJ, Goloubinoff P. The heat shock response in moss plants is regulated by specific calcium-permeable channels in the plasma membrane. The Plant Cell. 21: 2829-43. PMID 19773386 DOI: 10.1105/Tpc.108.065318 |
0.46 |
|
| 2009 |
Sharma SK, Christen P, Goloubinoff P. Disaggregating chaperones: an unfolding story. Current Protein & Peptide Science. 10: 432-46. PMID 19538153 DOI: 10.2174/138920309789351930 |
0.485 |
|
| 2008 |
Bromberg Z, Raj N, Goloubinoff P, Deutschman CS, Weiss YG. 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: 246-55. PMID 17989570 DOI: 10.1097/01.Ccm.0000295473.56522.Ef |
0.395 |
|
| 2007 |
Weiss YG, Bromberg Z, Raj N, Raphael J, Goloubinoff P, Ben-Neriah Y, Deutschman CS. Enhanced heat shock protein 70 expression alters proteasomal degradation of IkappaB kinase in experimental acute respiratory distress syndrome. Critical Care Medicine. 35: 2128-38. PMID 17855826 DOI: 10.1097/01.Ccm.0000278915.78030.74 |
0.342 |
|
| 2007 |
Goloubinoff P, De Los Rios P. The mechanism of Hsp70 chaperones: (entropic) pulling the models together. Trends in Biochemical Sciences. 32: 372-80. PMID 17629485 DOI: 10.1016/J.Tibs.2007.06.008 |
0.428 |
|
| 2007 |
Saidi Y, Domini M, Choy F, Zryd JP, Schwitzguebel JP, Goloubinoff P. Activation of the heat shock response in plants by chlorophenols: transgenic Physcomitrella patens as a sensitive biosensor for organic pollutants. Plant, Cell & Environment. 30: 753-63. PMID 17470151 DOI: 10.1111/J.1365-3040.2007.01664.X |
0.461 |
|
| 2007 |
Finka A, Schaefer DG, Saidi Y, Goloubinoff P, Zrÿd JP. In vivo visualization of F-actin structures during the development of the moss Physcomitrella patens. The New Phytologist. 174: 63-76. PMID 17335498 DOI: 10.1111/J.1469-8137.2007.01989.X |
0.301 |
|
| 2007 |
Hinault MP, Goloubinoff P. 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: 47-54. PMID 17205674 DOI: 10.1007/978-0-387-39975-1_5 |
0.391 |
|
| 2006 |
Hinault MP, Ben-Zvi A, Goloubinoff P. Chaperones and proteases: Cellular fold-controlling factors of proteins in neurodegenerative diseases and aging Journal of Molecular Neuroscience. 30: 249-265. PMID 17401151 DOI: 10.1385/Jmn:30:3:249 |
0.427 |
|
| 2006 |
De Los Rios P, Ben-Zvi A, Slutsky O, Azem A, Goloubinoff P. 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: 6166-6171. PMID 16606842 DOI: 10.1073/Pnas.0510496103 |
0.469 |
|
| 2005 |
De Marco A, Vigh L, Diamant S, Goloubinoff P. Native folding of aggregation-prone recombinant proteins in Escherichia coli by osmolytes, plasmid- or benzyl alcohol-overexpressed molecular chaperones Cell Stress and Chaperones. 10: 329-339. PMID 16333986 DOI: 10.1379/Csc-139R.1 |
0.462 |
|
| 2005 |
Saidi Y, Finka A, Chakhporanian M, Zrÿd JP, Schaefer DG, Goloubinoff P. Controlled expression of recombinant proteins in Physcomitrella patens by a conditional heat-shock promoter: a tool for plant research and biotechnology. Plant Molecular Biology. 59: 697-711. PMID 16270224 DOI: 10.1007/S11103-005-0889-Z |
0.492 |
|
| 2005 |
Shigapova N, Török Z, Balogh G, Goloubinoff P, Vígh L, Horváth I. Membrane fluidization triggers membrane remodeling which affects the thermotolerance in Escherichia coli. Biochemical and Biophysical Research Communications. 328: 1216-23. PMID 15708006 DOI: 10.1016/J.Bbrc.2005.01.081 |
0.424 |
|
| 2004 |
Ben-Zvi A, De Los Rios P, Dietler G, Goloubinoff P. Active solubilization and refolding of stable protein aggregates by cooperative unfolding action of individual Hsp70 chaperones Journal of Biological Chemistry. 279: 37298-37303. PMID 15201275 DOI: 10.1074/Jbc.M405627200 |
0.439 |
|
| 2003 |
Diamant S, Rosenthal D, Azem A, Eliahu N, Ben-Zvi AP, Goloubinoff P. Dicarboxylic amino acids and glycine-betaine regulate chaperone-mediated protein-disaggregation under stress Molecular Microbiology. 49: 401-410. PMID 12828638 DOI: 10.1046/J.1365-2958.2003.03553.X |
0.475 |
|
| 2002 |
Ben-Zvi AP, Goloubinoff P. Proteinaceous infectious behavior in non-pathogenic proteins is controlled by molecular chaperones Journal of Biological Chemistry. 277: 49422-49427. PMID 12377766 DOI: 10.1074/Jbc.M209163200 |
0.436 |
|
| 2002 |
Pnueli L, Hallak-Herr E, Rozenberg M, Cohen M, Goloubinoff P, Kaplan A, Mittler R. Molecular and biochemical mechanisms associated with dormancy and drought tolerance in the desert legume Retama raetam. The Plant Journal : For Cell and Molecular Biology. 31: 319-30. PMID 12164811 DOI: 10.1046/J.1365-313X.2002.01364.X |
0.481 |
|
| 2002 |
Lechner E, Goloubinoff P, Genschik P, Shen WH. 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. PMID 12062802 DOI: 10.1016/S0378-1119(02)00556-5 |
0.343 |
|
| 2002 |
Merquiol E, Pnueli L, Cohen M, Simovitch M, Rachmilevitch S, Goloubinoff P, Kaplan A, Mittler R. Seasonal and diurnal variations in gene expression in the desert legume Retama raetam Plant, Cell and Environment. 25: 1627-1638. DOI: 10.1046/J.1365-3040.2002.00938.X |
0.46 |
|
| 2001 |
Ben-Zvi AP, Goloubinoff P. Review: Mechanisms of disaggregation and refolding of stable protein aggregates by molecular chaperones Journal of Structural Biology. 135: 84-93. PMID 11580258 DOI: 10.1006/Jsbi.2001.4352 |
0.423 |
|
| 2001 |
Diamant S, Eliahu N, Rosenthal D, Goloubinoff P. Chemical Chaperones Regulate Molecular Chaperones in Vitro and in Cells under Combined Salt and Heat Stresses Journal of Biological Chemistry. 276: 39586-39591. PMID 11517217 DOI: 10.1074/Jbc.M103081200 |
0.53 |
|
| 2001 |
Tomoyasu T, Mogk A, Langen H, Goloubinoff P, Bukau B. Genetic dissection of the roles of chaperones and proteases in protein folding and degradation in the Escherichia coli cytosol Molecular Microbiology. 40: 397-413. PMID 11309122 DOI: 10.1046/J.1365-2958.2001.02383.X |
0.432 |
|
| 2001 |
Török Z, Goloubinoff P, Horváth I, Tsvetkova NM, Glatz A, Balogh G, Varvasovszki V, Los DA, Vierling E, Crowe JH, Vigh L. Synechocystis HSP17 is an amphitropic protein that stabilizes heat-stressed membranes and binds denatured proteins for subsequent chaperone-mediated refolding. Proceedings of the National Academy of Sciences of the United States of America. 98: 3098-103. PMID 11248038 DOI: 10.1073/Pnas.051619498 |
0.467 |
|
| 1999 |
Mogk A, Tomoyasu T, Goloubinoff P, Rüdiger S, Röder D, Langen H, Bukau B. Identification of thermolabile Escherichia coli proteins: Prevention and reversion of aggregation by DnaK and ClpB Embo Journal. 18: 6934-6949. PMID 10601016 DOI: 10.1093/Emboj/18.24.6934 |
0.493 |
|
| 1999 |
Goloubinoff P, Mogk A, Ben Zvi AP, Tomoyasu T, Bukau B. Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network Proceedings of the National Academy of Sciences of the United States of America. 96: 13732-13737. PMID 10570141 DOI: 10.1073/Pnas.96.24.13732 |
0.415 |
|
| 1998 |
Ben-Zvi AP, Chatellier J, Fersht AR, Goloubinoff P. Minimal and optimal mechanisms for GroE-mediated protein folding Proceedings of the National Academy of Sciences of the United States of America. 95: 15275-15280. PMID 9860959 DOI: 10.1073/Pnas.95.26.15275 |
0.351 |
|
| 1998 |
Diamant S, Goloubinoff P. 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 Biochemistry. 37: 9688-9694. PMID 9657681 DOI: 10.1021/Bi980338U |
0.538 |
|
| 1998 |
Veinger L, Diamant S, Buchner J, Goloubinoff P. The small heat-shock protein IbpB from Escherichia coli stabilizes stress-denatured proteins for subsequent refolding by a multichaperone network Journal of Biological Chemistry. 273: 11032-11037. PMID 9556585 DOI: 10.1074/Jbc.273.18.11032 |
0.489 |
|
| 1997 |
Goloubinoff P, Diamant S, Weiss C, Azem A. GroES binding regulates GroEL chaperonin activity under heat shock Febs Letters. 407: 215-219. PMID 9166902 DOI: 10.1016/S0014-5793(97)00348-7 |
0.517 |
|
| 1997 |
Török Z, Horváth I, Goloubinoff P, Kovács E, Glatz A, Balogh G, Vígh L. Evidence for a lipochaperonin: association of active protein-folding GroESL oligomers with lipids can stabilize membranes under heat shock conditions. Proceedings of the National Academy of Sciences of the United States of America. 94: 2192-7. PMID 9122170 DOI: 10.1073/Pnas.94.6.2192 |
0.407 |
|
| 1996 |
Török Z, Vigh L, Goloubinoff P. Fluorescence detection of symmetric GroEL14(GroES7)2 heterooligomers involved in protein release during the chaperonin cycle. The Journal of Biological Chemistry. 271: 16180-6. PMID 8663256 DOI: 10.1074/Jbc.271.27.16180 |
0.318 |
|
| 1994 |
Azem A, Kessel M, Goloubinoff P. Characterization of a functional GroEL14(GroES7)2 chaperonin hetero-oligomer. Science (New York, N.Y.). 265: 653-6. PMID 7913553 DOI: 10.1126/Science.7913553 |
0.326 |
|
| 1994 |
Lerner HR, Amzallag GN, Friedman Y, Goloubinoff P. The response of plants to salinity: From turgor adjustments to genome modification Israel Journal of Plant Sciences. 42: 285-300. DOI: 10.1080/07929978.1994.10676581 |
0.345 |
|
| 1989 |
Goloubinoff P, Christeller JT, Gatenby AA, Lorimer GH. Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and Mg-ATP Nature. 342: 884-889. PMID 10532860 DOI: 10.1038/342884A0 |
0.383 |
|
| 1989 |
Goloubinoff P, Gatenby AA, Lorimer GH. GroE heat-shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli Nature. 337: 44-47. PMID 2562907 DOI: 10.1038/337044A0 |
0.485 |
|
| 1988 |
Goloubinoff P, Brusslan J, Golden SS, Haselkorn R, Edelman M. Characterization of the photosystem II 32 kDa protein in Synechococcus PCC7942. Plant Molecular Biology. 11: 441-7. PMID 24272401 DOI: 10.1007/Bf00039025 |
0.407 |
|
| 1987 |
Eyal Y, Goloubinoff P, Edelman M. The amino terminal region delimited by Met1 and Met 37 is an integral part of the 32 kDa herbicide binding protein. Plant Molecular Biology. 8: 337-43. PMID 24301196 DOI: 10.1007/Bf00021313 |
0.318 |
|
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