Prof. Pierre Goloubinoff

Pierre A. Goloubinoff
April 4, 1957, France
Department of Plant Molecular Biology, 
University of Lausanne, Switzerland, Tel:+41-76-4117084.

ORCID iD: 0000-0002-4802-0807
https://scholar.google.ch/citations?user=4Twe74wAAAAJ&hl=en
133 citations. H factor 54
https://en.wikipedia.org/wiki/Pierre_Goloubinoff 
https://fr.wikipedia.org/wiki/Pierre_Goloubinoff
https://he.wikipedia.org/wiki/%D7%A4%D7%99%D7%99%D7%A8_%D7%92%D7%95%D7%9C%D7%95%D7%91%D7%99%D7%A0%D7%95%D7%A3

•    Education 

B.Sc - 1981 University of Lausanne, Plant Physiology, Microbiology, Biochemistry
Ph.D. – 1988 Weizmann Institute of Science, Plant Molecular Biology 
Adviser: Prof. M. Edelman
Title: Molecular analysis of the chloroplast and cyanobacterial psbA gene and its gene product
 

•    Employment History

2020-Present 
Associate Professor 
University of Tel Aviv (TAU), Israel  

2022-Present 
Professor Emeritus 
University of Lausanne (UNIL), Switzerland 

2001-2022    
Associate Professor 
University of Lausanne (UNIL), Switzerland 

1999- 2003    
Associate Professor 
Hebrew University of Jerusalem, Israel

1995-1999    
Senior Lecturer 
Hebrew University of Jerusalem

1991-1995    
Lecturer 
Hebrew University of Jerusalem

1990-1991     
Research associate, 
Adviser: Prof. A. C. Wilson 
University of California, Berkeley
 
1988-1990     
Visiting scientist (Post Doctorate) 
Adviser: Dr. George Lorimer
I.E. DuPont de Nemours 

•    Professional Activities

(a) Positions in academic administration
2010-present    Founding and member of the Faculty of Biology and Medicine, UNIL doctoral school 
2009-2017     Member of the “commission de la restauration de l’université de Lausanne"
2008-2012     Elected member representing the FBM professors at the "commission du personnel"     (COPERS) of UNIL
2007-2010     President of faculty awards committee, Faculty of Biology and Medicine, UNIL
2004-2006     Member of awards committee, Faculty of Biology and Medicine, UNIL
1999-2001    Chair of the plant science department, Hebrew University of Jerusalem.
1999-2000        Chair of the curriculum for plant science studies, Hebrew University of Jerusalem
1997-1998        Chair of the curriculum for plant science studies, Hebrew University of Jerusalem

(b) Professional functions outside universities/institutions
2014         Member of the evaluating commission of Lausanne Faculty of Biology and Medicine
2013-2018     Elected member of the “Conseil de faculté de la Faculty of Biology and Medicine”
2003-2008     Member of the Herbette grant selecting commission

(c) Significant professional consulting
2011-present     Scientific/academic consulting to the groups of Prof Maya Schuldiner, Prof Dan Tawfik, Prof Gideon Schreiber and Prof. Gilad Haran (see Mazal et al., Nat Commun. 2019 Mar 29;10(1):1438. doi: 10.1038/s41467-019-09474-6), Weizmann Institute of Science. Subject: mechanisms of molecular chaperones.
2013-2017     Scientific consulting to the group of Prof Mikhal Shapira, BGU. Subject: mechanisms of molecular chaperones.
2001-2014     Scientific consulting to the group of Prof Yoram Weiss, Hadassa Medical school, HUJI. Subject: the role of molecular chaperones is stress signaling.

(d) Editor or member of editorial board of scientific or professional journal
Frontiers in Molecular Biosciences (IF 3.565, cite score 3.55): since 2014, Founding and specialty Chief Editor of specialty section “Protein folding misfolding and degradation. See 
https://www.frontiersin.org/journals/molecular-biosciences/sections/protein-folding-misfolding-and-degradation#about
 
(e) Ad-hoc reviewer for journals
Nature Structural Biology, Nature Chemical Biology, Frontiers in Molecular Biosciences, Plant Journal, Molecular and Cellular Biology, Journal of Biological Chemistry, Archives of Microbiology, Nature Communications, Plant Physiology, Cell Stress and Chaperones, Plant Molecular Biology, PNAS, Biophysical Journal, Physiologia Plantarum, Plos Genetics, Biochimie, Scientific Reports, Frontiers in Neurosciences, Journal of Molecular Biology. Plant Cell, FEBS Journal, Trends in Biochemical Sciences, Nucleic Acid Research, PlosOne, Trends in Plant Sciences, Cell Molecular Life Sciences.

(f) Membership in professional/scientific societies
    2002- present Life member of the Cell Stress Society International
     (http://www.cellstress.uconn.edu/aboutcssi.html)
    2021 Elected fellow of the Cell Stress Society International.

•    Educational Activities

Teaching
(a) Courses taught
1990-1991    Protein folding for Graduate Students- Division of Biochemistry and Molecular Biology, University of California, Berkeley (Co-lecturer with Prof. Jack Kirsch)
1992-1993    Seminar course on Protein structure and function, for B.Sc. and M.Sc. – The Hebrew University of Jerusalem (Co-lecturer with Prof. M Rigbi)
1993-2001    Seminars course in Selected subjects in Botany, for B.Sc. and M.Sc. – The Hebrew University of Jerusalem (Co-directed with Prof. A. Kaplan)
1993-2001    Extended course in Botany, Chloroplast genome organization, evolution of the photosynthetic apparatus, stress proteins in plants for B.Sc. and M.Sc. – The Hebrew University of Jerusalem (Co-lecturer with Prof. R. Nehushtai)
1994-2001    Seminars course in Selected subjects in Plant Sciences, for B.Sc. and M.Sc. – The Hebrew University of Jerusalem
1995-2001    Protein folding and stress proteins, for M. Sc. and Graduate students – The Hebrew University of Jerusalem
1995-2001    Recombinant DNA as a tool for biological research; Laboratory course for advanced B.Sc. students – The Hebrew University of Jerusalem
1998-2001    Tutorial for selected top 5 % students of Biology of the ETGAR program – The Hebrew University of Jerusalem
2001-2007    Plant Biology for first year biology and pharmacy students - Lausanne University
2001-2007    Plant Biochemistry for third year biology students - Lausanne University
2001-2007    Plant genetics for fourth year biology students - Lausanne University
2006-present    Protein misfolding diseases for first year graduate students - Lausanne University
2007-present    Protein biochemistry to second year biology students - - Lausanne University
2007-present    Biology of stress to fourth year students - Lausanne University
2007-present    Protein Homeostasis to third year students - Lausanne University

(b) Research students
Post Docs
Abdussalam Azem     1991-1995
Barbara Despes     2001-2004
Pierre Haldimann     2006-2011
Andrija Finka     2008-2016
Smriti Priya     2013-2017
Sandeep Kumar Sharma     2009-2014
Bruno Fauvet     2015-2021
Anthony Guihur     2016-present
Satyam Tiwari     2017-present

PhD
Celeste Weiss     PhD, 1996, HUJI
Anat Ben-Zvi    PhD, 2003, HUJI
Cyril Cicekli     PhD, 2010, UNIL
Younousse Saidi     PhD, 2011, UNIL (co-supervised with Prof. JP Zryd)
Marie Pierre Hinault     PhD, 2011, UNIL
Rayees Hassan Mattoo     PhD 2015, UNIL
Mathieu Rebeaud     PhD, 2017-present, UNIL
Baptiste Bourgine     PhD, 2017-2022, UNIL

MSc
Lea Veinger     MSc     1998, HUJI
Fleur Choy    MSc     2007, UNIL
Jean-Daniel Wurlod     MSc    2011, UNIL
Jerome Lugrin     MSc    2012, UNIL
 

 

 

a) H-index = 45 ISI / 5 GS

b) Total number of citations of all articles: 7,757 ISI / 11,226 GS

c) Total number of citations without self-citations: 7,155 ISI

 

(a)        Authored books

(b)       Editorship of collective volumes

 

(c)        Refereed chapters in collective volumes, Conference proceedings, Festschrifts

1. Edelman(PI), M., Goloubinoff(S), P., Marder(S) J.B., Fromm(S), H., Devic(PD), M., Fluhr(S), R. and Mattoo(PI), A.K. (1984). Structure-function relationships and regulation of the 32 kDa protein in the photosynthetic membranes. In: Molecular form and function of the plant genome (ed. Van Vloten-Doting, L.). Plenum, New York, pp 291-300.
2. Marder(S), J.B., Mattoo(PI), A.K. Goloubinoff(S), P. and Edelman(PI), M. (1984). Structure and physiological control of the rapidly metabolized 32,000-dalton chloroplast membrane protein. In: Biosynthesis of the photosynthetic apparatus: in Molecular biology, development and regulation (eds. Hallick, R., Staelin, A. and Thornber, P.) Liss Inc., New York.
3. Gatenby(C), A.A., Goloubinoff(PD), P., Lubben(C), T.H. and Lorimer(PI), G.H. (1989). The assembly of ribulose bisphosphate carboxylase in Escherichia coli and isolated chloroplasts. In: Photosynthesis, Alan, R. Liss inc., pp 299-309.
4. Gatenby(C), A.A., Donaldson(C), G.K., Goloubinoff(PD), P., LaRossa(PI), R.A, Lorimer(PI), G.H. Lubben(C), T.H., Van Dyk(PD) T.K, and Viitanen(C), P.V. (1990). The cellular function of Chaperonins (eds. Schlesinger, Santoro and Garaci), Sprinder. pp. 57-69.
5. Goloubinoff(PD), P., Pääbo(PI), S. and Wilson(PI), A. C. (1993). Molecular Characterization of ancient Maize: potentials and pit-falls. In Corn and culture in the prehistoric New World, West view Press. Johannessen, S. and Hastorf, C. A. (eds), pp. 113-125.
6. Azem(PD), A., Weiss(S), C. and Goloubinoff(PI), P. (1998). Structural analysis of GroE chaperonin complexes using chemical crosslinking. Methods in Enzymology vol. 290, 253-268. Eds Lorimer & Baldwin (20 citations; IF 1.862; JR 57/79; Q3).
7. Viitanen, P., Lorimer(PI), G., Bergmeier, W., Weiss(S), C. and Goloubinoff(PI), P. (1998). Purification, of mammalian mitochondrial chaperonin 60 through in vitro reconstitution of active oligomers. Methods in Enzymology vol. 290. 203-217. Eds Lorimer & Baldwin (31 citations; IF 1.862; JR 57/79; Q3).
8. Despres(PD), B. and Goloubinoff(PI), P. (2003). The role of molecular chaperones in plants during stress. In the Encyclopedia of Plant & Crop Science. Ed Robert M. Goodman (Madison, WIS), pp. 1002-1005.
9. Goloubinoff(PI), P. and Ben-Zvi(S), A, (2004). Review. Mechanisms of Active Solubilization of Stable Protein Aggregates by Molecular Chaperones. In "Protein Misfolding, Aggregation and Conformational Diseases". Eds Uversky, V. and Fink, AL (Kluwer Academic / Plenum Publishers).
10. Goloubinoff(PI), P. (2004). ATPase-Chaperones and Proteases as Molecular Machines That Unfold Toxic Protein Aggregates” In 1er Séminaire Transalpin de Physique “Living matter: a new challenge to physicists?” eds. Paolo De Los rios, Giovanni Dietler, Bertrand Fourcade and Cristiana Peroni. Frontier Group (France), pp. 55-64.
11. Hinault(S), M-P. and Goloubinoff(PI), P. (2006). "Molecular crime and cellular punishment" in Molecular aspects of the stress response: Chaperones, membranes and networks" Adv Exp Med Biol. 594 :47-54.
12. Ben Shabat, S., Goloubinoff(PI), P., Dudai(PI), N. and Lewinsohn(PI), E. (2014). Farming amphetamines. Review book on “Khat (Catha edulis Forsk.) a traditional plant with psychoactive and medicinal properties.” Ed. Efraim Lewinsohn Medicinal and Aromatic Plants of the World Volume 2, 2014, pp 181-197. DOI 10.1007/978-94-017-9276-9_9
13. Mattoo(S), RUH and Goloubinoff(PI) 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.

 

 

(d)       Refereed articles and refereed letters in scientific journals, running numbers

 

1. Goloubinoff(S), P., Edelman(PI), M. and Hallick(PI), 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 (85 citations; IF 11.147; JR 14/299; Q1).
2. Marder(S), J.B., Goloubinoff(S), P. and Edelman(PI), 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 (150 citations; IF 4.106; JR 81/299; Q2).
3. Fromm(S), H., Edelman(PI), M., Koller(PI), B., Goloubinoff(S), P. and Galun(PI), E. (1986). The enigma of the gene coding for ribosomal protein S12 in the chloroplasts of Nicotiana. Nucleic. Acid Res. 14, 883-898 (44 citations; IF 11.147; JR 14/299; Q1).
4. Eyal(S), Y., Goloubinoff(S), P. and Edelman(PI), 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 (12 citations; IF 3.928; JR 24/228; Q1).
5. Goloubinoff(S), P., Golden(S), S.S., Brusslan(S), J., Haselkorn(PI), R. and Edelman(PI), M. (1988). Characterization of the photosystem II 32kDa protein in Synechococcus PCC7942. Plant Molec. Biol. 11, 441-447 (30 citations; IF 3.928; JR 24/228; Q1).
6. Mattoo(PI), A.K. Callahan(PI), F.E., Greenberg(PD), B.M., Goloubinoff(S), P. and Edelman(PI), M. (1988). Molecular dynamics of the 32,000-dalton photosystem II herbicide-binding protein. In: Biotechnology for crops. ACS Symposium series, 379: 248-257. (0 citations; IF 0.566; JR 87/125; Q3).
7. Goloubinoff(PD), P., Gatenby(C), A.A. and Lorimer(PI), G.H. (1989). GroE heat-shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli. Nature 337, 44-47 (595 citations; IF 43.07; JR 1/69; Q1).
8. Goloubinoff(PD), P., Christeller(C), J.T., Gatenby(C), A.A. and Lorimer(PI), 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 (624 citations; IF 43.07; JR 1/69; Q1).
9. Viitanen(C), P.V., Lubben(C), T.H., Reed-Scioli(S), J., Goloubinoff(PD), P., O'Keefe(C), D.P. and Lorimer(PI), G.H. (1990). Chaperonin-facilitated refolding of Ribulose bisphosphate carboxylase and ATP-hydrolysis by chaperonin 60 (groEL) are K+-dependent. Biochemistry 29, 5665-5671 (353 citations; IF 2.952; JR 142/299; Q2).
10. Goloubinoff(PD), P., Gatenby(C). A.A, and Lorimer(PI), G. (1991). Role of Chaperonins in protein folding. American Chemical Society Series 470, 110-118 (3 citations; IF 0.566; JR 87/125; Q3).
11. Goloubinoff(PD), P., Pääbo(PD), S. and Wilson(PI), A. C. (1993). Evolution of Maize According to Nuclear DNA Sequences from Archaeological Specimens. Proc. Nat. Acad. Sci. U.S.A. 90, 1997-2001 (101 citations; IF 9.58; JR 7/69; Q1).
12.  Azem(PD), A., Diamant(T), S. and Goloubinoff(PI), P. (1994). Effect of Divalent Cations on the Molecular Structure of the GroEL Oligomer. Biochemistry 33, 6671-6675 (52 citations; IF 2.952; JR 142/299; Q2).
13. Azem(PD), A., Kessel(C), M. and Goloubinoff(PI), P. (1994). Characterization of a Functional GroEL14(GroES7)2 Chaperonin Hetero-oligomer. Science 265, 654-656 (143 citations; IF 41.063; JR 2/69; Q1).
14. Diamant(T), S., Azem(PD), A., Weiss(S), C and Goloubinoff(PI), P. (1995). Effect of Free and ATP-bound Magnesium and Manganese ions on the ATPase Activity of Chaperonin GroEL14. Biochemistry, 34, 273-277 (23 citations; IF 2.952; JR 142/299; Q2).
15. Lerner(PI), H. R, Amzallag(S), G. N., Friedman(S), Y. and Goloubinoff(PI), P. (1994). The response of plants to salinity: from turgor adjustments to genome modification. Israel J. Plant Sci. 42, 285-300 (7 citations; IF 0.908; JR 174/228; Q4).
16. Weiss(S), C. and Goloubinoff(PI), 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 (19 citations; IF 4.106; JR 81/299; Q2).
17. Azem(PD), A., Diamant(T), S, Kessel(C), M. Weiss(S), C. and Goloubinoff(PI), P. (1995). The Protein-Folding Activity of Chaperonins Correlates with The Symmetric GroEL14(GroES7)2 Hetero-oligomer. Proc. Natn. Acad. Sci. U.S.A 92, 12021-12025 (76 citations; IF 9.58; JR 7/69; Q1).
18. Diamant(T), S. Azem(PD), A., Weiss(S), C. and Goloubinoff(PI), P. (1995). Increased Efficiency of GroE-Assisted Protein Folding by Manganese ions. J. Biol. Chem. 270, 28387-28391 (29 citations; IF 4.106; JR 81/299; Q2).
19. Török(PD), S., Vigh(PI), L. and Goloubinoff(PI), 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 (25 citations; IF 4.106; JR 81/299; Q2).
20. Török(PD), S., Horvath(C), I., Goloubinoff(PI), P., Kovacs(PD), E., Glatz(PD), A., Balogh(S), G. and Vigh(PI), 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 (164 citations; IF 9.58; JR 7/69; Q1).
21. Goloubinoff(PI), P., Diamant(T), S., Weiss(S), C. and Azem(PD), A (1997). GroES binding regulates GroEL chaperonin activity under heat-shock. FEBS Lett. 407, 215-219 (34 citations; IF 2.675; JR 160/299; Q3).
22. Veinger(S), L., Diamant(T), S., Buchner(PI), J. and Goloubinoff(PI) 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 (260 citations; IF 4.106; JR 81/299; Q2).
23. Diamant(T), S. and Goloubinoff(PI), 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 11037 (47 citations; IF 4.106; JR 81/299; Q2).
24. Ben-Zvi(S), A.P., Chatellier(PD), J., Fersht(PI), A. R. and Goloubinoff(PI), P. (1998). Minimal and optimal mechanisms for GroEL-mediated protein folding. Proc. Nat. Acad. Sci. U.S.A 95, 15275-15280 (39 citations; IF 9.58; JR 7/69; Q1).
25. Goloubinoff(PI), P., Mogk(PD), A., Ben-Zvi(S), A.P., Tomoyasu(PD), T. and Bukau(PI), B. (1999). Sequential Mechanism of Solubilization and Refolding of Stable Protein Aggregates by a Bi-Chaperone Network. Proc. Nat. Acad. Sci. U.S.A. 96, 13732-13737 (433 citations; IF 9.58; JR 7/69; Q1).
26. Mogk(PD), A., Tomoyasu(PD), T., Goloubinoff(PI), P., Rüdiger(PD), R, Röder(S), D., Langen(PD), H. and Bukau(PI), B. (1999). Identification of thermolabile E. coli proteins: Prevention and reversion of aggregation by DnaK and ClpB. EMBO J. 18, 6934-6949 (432 citations; IF 11.227; JR 13/299; Q1).
27. Diamant(T), S., Ben-Zvi(S), A.P., Bukau(PI), B and Goloubinoff(PI), P. (2000). Size-Dependent Disaggregation of Aggregated Protein Particles by the DnaK Chaperone Machinery of Escherichia coli. J. Biol. Chem. 275, 21107-21113 (168 citations; IF 4.106; JR 81/299; Q2).
28. Chatellier(PD), J., Hill(PD), F., Foster(PD), N. W., Goloubinoff(PI), P., and Fersht(PI), A. R. (2000). From minichaperone to GroEL: Properties of an active single-ring mutant of GroEL. J. Mol Biol. 304, 897-910 (28 citations; IF 5.067; JR 47/299; Q1).
29. Ben-Zvi(S), A.P. and Goloubinoff(PI), P. (2001). Review: Mechanisms of disaggregation and refolding of stable protein aggregates by molecular chaperones. J. Struct. Biol. 135, 84-93 (172 citations; IF 3.754; JR 102/299; Q2).
30. Török(PD), Z., Goloubinoff(PI), P., Horváth (C), I., Tsvetkova(S), NM., Glatz(PD). A., Balogh(PD), G., Varvasovszki(S), V., Vierling(PI), E., Crowe(PI) JH. and Vígh(PI), L. (2001). HSP17 from Synechocystis 6803 is an amphitropic protein with chaperone activity for membranes and proteins under heat-stress. Proc. Nat. Acad. Sci. U.S.A 98, 3098-3103 (178 citations; IF 9.58; JR 7/69; Q1).
31. Tomoyasu(PD), T, Mogk(PD), A, Langen(PD), H, Goloubinoff(PI), P. and Bukau(PI), 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 (239 citations; IF 3.649; JR 107/299; Q2).
32. Diamant(T), S., Rosental(S), D., Elyahu(S), N. and Goloubinoff(PI), P. (2001). Chemical chaperones regulate Molecular chaperones in vitro and in cells under combined salt and heat stresses. J. Biol. Chem. 276: 39586-39591 (250 citations; IF 4.106; JR 81/299; Q2).
33. Pnueli(S), L., Hallak-Herr(S), E., Rozenberg(S), M., Cohen(S), M., Goloubinoff(PI), P., Kaplan(PI), A., Mittler(PI), R. (2002). Molecular and biochemical mechanisms associated with dormancy and drought tolerance in the desert legume Retama raetam. Plant J. 31(3):319-330 (133 citations; IF 5.726; JR 11/228; Q1).
34. Lechner(S), E., Goloubinoff(PI), P., Genschik(PI), P. and Shen(S), 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 (15 citations; IF 2.638; JR 821742; Q2).
35. Merquiol(S), E., Pnueli(S), L., Cohen(S), M., Simovitch(S), M., Rachmilevitch(S), S., Goloubinoff(PI), P. and Mittler(PI), R. (2002). Seasonal and diurnal variations in gene expression in the desert legume Retama raetam. Plant Cell and Env. 25, 1627-1638 (13 citations; IF 5.624; JR 12/228; Q1).
36. Ben-Zvi(S), A.P. and Goloubinoff(PI), P. (2002). Proteinaceous Infectious Behavior in non-Pathogenic proteins is controlled by molecular chaperones” J. Biol. Chem. 277 (51), 49422-49427 (32 citations; IF 4.106; JR 81/299; Q2).
37. Amzallag(S), GN. and Goloubinoff(PI), P. (2003). Effects of the Hsp90-inhibitor geldanamycin on steroid stress-signaling in soybean. Plant Biology, 2, 143-150 (8 citations; IF 2.393; JR 68/228; Q2).
38. Diamant(T), S., Rosenthal(S), D., Azem(PI), A., Eliahu(S), N., Ben-Zvi(S), A.P. and Goloubinoff(PI), P. (2003). Dicarboxylic Amino-Acids and Glycine-Betaine Regulate Chaperone-Mediated Protein-Disaggregation Under Stress. Mol. Microbiol., 49 (2), 401-410 (61 citations; IF 3.649; JR 107/299; Q2).
39. Ben-Zvi(S) A., De Los Rios(PI), P., Dietler(PI), G. and Goloubinoff(PI), P. (2004). Active solubilization and refolding of stable protein aggregates by cooperative unfolding action of individual HSP70 chaperones. J. Biol. Chem. 279, 37298-303 (64 citations; IF 4.106; JR 81/299; Q2).
40. Shigapova(S), N., Török(PD), S., Balogh(S), G., Goloubinoff(PI), P., Vigh(PI), L. and Horvath(C), I. (2005). Membrane fluidization triggers membrane remodeling which affects the thermotolerance in Escherichia coli. Biochem Biophys Res Commun. 328, 1216-23 (59 citations; IF 2.705; JR 157/299; Q3).
41. Saidi(S), Y., Schaefer(PD), D., Finka(PD), A., Zryd(PI), JP. and Goloubinoff(PI), P. (2005). 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, issue 5, 695-709 (63 citations; IF 3.928; JR 24/228; Q1).
42. De Marco(C), A., Vigh(PI), L., Diamant(T), S. and Goloubinoff(PI), P. (2005). Native folding of aggregation-prone recombinant proteins in Escherichia coli by osmolytes, plasmid- or benzyl alcohol over-expressed molecular chaperones. Cell Stress and Chaperones 10:329-39 (93 citations; IF 2.903; JR 122/193; Q3).
43. De Los Rios(PI) P., Ben-Zvi(S) A., Slutsky(S) O., Azem(PI) A. and Goloubinoff(PI) P. (2006). Hsp70 chaperones accelerate protein translocation and the unfolding of stable protein aggregates by entropic pulling. Proc. Natl. Acad. Sci. U S A. 103, 6166-6171 (134 citations; IF 9.58; JR 7/69; Q1).
44. Hinault(S), M-P. and Goloubinoff(PI), P. (2006). L'agrégation toxique des protéines: une forme de "délinquance moléculaire" activement combattue dans la cellule par les chaperones moléculaires et les protéases. Annales de cardiologie et d’angéiologie. 55 (2), 74-78.
45. Hinault(S), M-P., Ben-Zvi(S), A. and Goloubinoff(PI), P. (2006). Chaperones and proteases: cellular fold-controlling factors of proteins in neurodegenerative diseases and aging. Journal of Molecular Neurosciences. 30, 293-310 (70 citations; IF 2.577; JR 166/299; Q3).
46. Finka(PD), A., Schaefer(PD), D.G., Saidi(S), Y., Goloubinoff(PI), P. and Zrÿd(PI), J.-P. (2007). In vivo visualization of F-actin structures during the development of the moss Physcomitrella patens. New Phytologist 174, 63-76 (24 citations; IF 7.299; JR 8/228; Q1).
47. Saidi(S), Y., Domini(S), M., Choy(S), F., Zryd(PI), JP., Schwitzguebel(PI), JP. and Goloubinoff(PI), P. (2007). Activation of the heat shock response in plants by chlorophenols: transgenic Physcomitrella patens as a sensitive biosensor for organic pollutants. Plant Cell Environ. 30, 753-763 (39 citations; IF 5.624; JR 13/228; Q1).
48. Weiss(PI), Y., Bromberg(S), Z., Raj(C), M, Rephael(T), J., Goloubinoff(PI), P. and Ben Neria(PI), H. (2007). Enhanced Hsp70 expression alters proteasomal degradation of IkB kinase in experimental ARDS. Critical Care Medicine. Volume 35(9):2128-2138 (72 citations; IF 6.971; JR 5/33; Q1).
49. Goloubinoff(PI), P. and De Los Rios(PI), P. (2007). The Mechanism of Hsp70 Chaperones: (entropic) pulling the models together. Trends in Biochemical Sci. 32(8):372-80 (109 citations; IF 16.889; JR 4/299; Q1).
50. Bromberg(S), Z., Raj(C), N., Goloubinoff(PI), P., Deutschman(PI), CS. and Weiss(PI)YG. (2007). Enhanced Expression of Hsp70 Limits Cell Division in a Sepsis-Induced Model of ARDS. Critical Care Medicine. Jan;36(1): 246-5 (22 citations; IF 6.971; JR 5/33; Q1).
51. Sharma(PD), SK., Goloubinoff(PI), P. and Christen(PI), P. (2008). Heavy metal ions are potent inhibitors of protein folding. Biochem Biophys Res Commun. 372(2):341-345 (90 citations; IF 2.705; JR 157/299; Q3).
52. Finka(PD), A., Saidi(S), Y., Goloubinoff(PI) P., Neuhaus(PI), JM., Zrÿd (PI), JP. and Schaefer(PD), DG (2008). The knock-out of ARP3a gene affects F-actin cytoskeleton organization altering cellular tip growth, morphology and development in moss Physcomitrella patens. Cell Motil Cytoskeleton 65(10):769-784 (19 citations; IF 4.194; JR 103/228; Q2).
53. Saidi(S), Y., Schaefer(PD), DG., Goloubinoff(PI), P., Zrÿd(PI), JP. and Finka(PD), A. (2009). The CaMV 35S promoter has a weak expression activity in dark grown tissues of moss Physcomitrella patens. Plant Signaling & Behavior May;4(5): 457-459 (12 citations (GS); IF 1.644; JR 75/290; Q2).
54. Sharma(PD), SK., Christen(PI), P. and Goloubinoff(PI), P. (2009). Disaggregating chaperones: an unfolding story. Current Protein and Peptide Science ed. Uverski V. I. The small Hsps Curr. Protein Pept. Sci. 10(5):432-446 (66 citations; IF 1.885; JR 230/299; Q4).
55. Saidi(S), Y., Finka(PD), A., Muriset(T), M., Bromberg(S), Z., Weiss(PI), YG., Maathuis(PI), FJM, and Goloubinoff(PI), P. (2009). The Heat Shock Response in Moss Plants is Regulated by Specific Calcium-Permeable Channels in the Plasma Membrane. Plant Cell. 21(9):2829-43 (135 citations; IF 8.631; JR 6/228; Q1).
56. Saidi(S), Y., Peter, M., Finka(PD), A., Cicekli(S), C., Vigh (PI), L. and Goloubinoff(PI), P (2010). Membrane lipid composition affects plant heat sensing and modulates Ca2+-dependent heat shock response. Plant Signal Behav. Dec 1;5(12): 1530-1533 (68 citations (GS); IF 1.644; JR 75/290; Q2).
57. Hinault(S), MP., Farina-Henriquez-Cuendet(T), A, Mattoo(S), RUH, Mensi(S), M., Dietler(PI), G., Lashuel(PI), HA., Goloubinoff(PI), P. (2010). Stable a-synuclein oligomers strongly inhibit chaperone activity of the HSP70 system by weak interactions with J-domain co-chaperones. J Biol Chem. 285, 49 38173-82 (45 citations; IF 4.106; JR 81/299; Q2).
58. Sharma(PD), SK., Christen(PI), S., De Los Rios(PI), P., Lustig(T), A. and Goloubinoff(PI), P. (2010). The kinetic parameters and energy cost of the Hsp70 chaperone as a protein unfoldase. Nat Chem Biol. 6. 914-920 (105 citations; IF 12.154; JR 8/299; Q1).
59. Finka(PD), A., Mattoo(S), RUH and Goloubinoff(PI), P. (2011). Meta-analysis of heat- and chemically-upregulated chaperone genes in plant and human cells Cell Stress Chaperones 16(1), 15-31 (66 citations; IF 2.903; JR 122/193; Q3).
60. Hinault(S), MP., Farina-Henriquez-Cuendet(T), A. and Goloubinoff(PI), P. (2011). Molecular chaperones and associated cellular clearance mechanisms against toxic protein conformers in Parkinson's disease. Neurodegenerative Diseases, 8(6):397-412 (15 citations; IF 2.798; JR 141/267; Q3).
61. Sharma(PD), SK., De Los Rios(PI), P. and Goloubinoff(PI), P. (2011). Probing the different chaperone activities of the bacterial HSP70-HSP40 system using a thermolabile luciferase substrate. Proteins-Structure Function and Bioinformatics. 79(6):1991-8 (18 citations; IF 2.501; JR 179/299; Q3).
62. Saidi(S), Y., Finka(PD), F. and Goloubinoff(PI), P. (2011). “Heat perception and signaling in plants: a tortuous path to thermotolerance” New Phytologist 190;556-565 (114 citations; IF 7.299; JR 8/228; Q1).
63. Haldimann(PD), P., Muriset(T), M., Vígh(PI), L. and Goloubinoff(PI), P. (2011). The novel hydroxylamine derivative NG-094 suppresses polyglutamine protein toxicity in Caenorhabditis elegans. J Biol Chem. 286(21):18784-18794 (24 citations; IF 4.106; JR 81/299; Q2).
64. Iosefson(S), O., Sharon(S), S., Goloubinoff(PI), P. and Azem(PI), A. (2012). Reactivation of protein aggregates by mortalin and Tid1-the human mitochondrial Hsp70 chaperone system. Cell Stress Chaperones. 1:57-66 (22 citations; IF 2.903; JR 122/193; Q3).
65. Mittler(PI), R., Finka(PD), A. and Goloubinoff(PI), P. (2012). How do plants feel the heat? Trends in Biochemical Sci. 2012 Mar;37(3):118-25 (332 citations; IF 16.889; JR 4/299; Q1).
66. De Los Rios(PI), P. and Goloubinoff(PI), P. (2012). Chaperoning protein evolution. Nature Chemical Biology. 8, 226–228. doi:10.1038/nchembio.791 (12 citations; IF 12.154; JR 8/299; Q1).
67. Finka(PD) A., Farina Cuendet (T) A.H, Maathuis (PI), FJM., Saidi(S), Y. and Goloubinoff (PI), P., (2012). Plasma Membrane Cyclic Nucleotide Gated Calcium Channels Control Land Plant Thermal Sensing and Acquired Thermotolerance. Plant Cell, August; 24 (8): 3333-3348 (106 citations; IF 8.631; JR 6/228; Q1).
68. Jacobson(S), T., Navarrete (S), C, Sharma (PD) SK, Sideri(S), T.C., Ibstedt(S), S., Priya (PD), S., Grant (S), CM., Christen (PI), P., Goloubinoff(PI), P. and Tamás(PI), MJ. (2012). Arsenite interferes with protein folding and triggers formation of toxic protein aggregates in yeast. J Cell Sci. 125(21): 5073-5083 (62 citations; IF 4.517; JR 65/193; Q2).
69. Horvath(C), I., Nakamoto(PI), H., Teun(S), Mishkind(S), Saidi(S), Y., Goloubinoff(PI), P., and Vigh(PI), L. (2012). Heat shock response in photosynthetic organisms: membrane and lipid connections. Progress in Lipid Research; 51(3):208-220 (77 citations; IF 12.54; JR 7/299; Q1).
70. Natalello(PD), N., Mattoo(S), RUH., Priya(PD), S., Sharma(PD) S.K., Goloubinoff(PI), P. and Doglia(PI) S. M. (2013). Biophysical Characterization of Two Different Stable Misfolded Monomeric Polypeptides That Are Chaperone-Amenable Substrates. J Mol Biol. 425(7):1158-1171 (16 citations; IF 5.067; JR 47/299; Q1).
71. Bromberg(S), Z., Goloubinoff(PI), P., Saidi(S), Y. and Weiss(PI), 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 (18 citations; IF 2.776; JR 24/69; Q2).
72. Finka(PD), A and Goloubinoff(PI), P. (2013). Proteomic data from human cell cultures refine mechanisms of chaperone-mediated protein homeostasis. Cell Stress and Chaperones, 18(5):591-605 (85 citations; IF 2.903; JR 122/193; Q3). Recommended by the “Faculty of 1000”.
73. Priya(PD), S., Sharma(PD), SK., Sood(PD), V., Mattoo(S), RUH., Finka(PD), A, Azem(PI), A., De Los Rios(PI), P. and Goloubinoff(PI), 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 (39 citations; IF 9.58; JR 7/69; Q1).
74. Priya(PD) S, Sharma(PD), SK. and Goloubinoff(PI), P. (2013). Molecular chaperones as enzymes that catalytically unfold misfolded polypeptides. FEBS Lett. 587(13):1981-7 (45 citations; IF 2.675; JR 160/299; Q3).
75. Mattoo(S), RUH., Sharma(PD), SK., Priya(PD) S, Finka(PD) A, Goloubinoff(PI), 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. 288(29):21399-411 (83 citations; IF 4.106; JR 81/299; Q2).
76. Finka(PD), A. and Goloubinoff(PI), 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 (9 citations; IF 2.903; JR 122/193; Q3).
77. Nakamoto (PI), H., Fujita (S), K., Ohtaki (S), A., Watanabe(S), S., Narumi(S), S., Maruyama(S), T., Suenaga(S), E., Misono(S), TS., Kumar(S), PK., Goloubinoff(PI), P. and Yoshikawa(C), 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 (36 citations; IF 4.106; JR 81/299; Q2).
78. Mattoo(S), RUH. and Goloubinoff(PI), P. (2014). Molecular chaperones are nano-machines that catalytically unfold misfolded and alter-natively folded proteins. Cell. and Mol. Life Sc. 71(17):3311-25 (57 citations; IF 7.014; JR 31/299; Q1).
79. Mattoo(S) RUH, Farina Henriquez Cuendet(T) A, Sujatha(S), Finka(PD) A, Priya(PD) S, Sharma(PD) SK and Goloubinoff(PI), 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. 1:7 (4 citations (GS); IF 3.565; JR 113/299; Q2).
80. Finka(PD) A, Sood (PD) V, Quadroni M, De Los Rios(PI) P and Goloubinoff(PI), 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 20(4):605-620 (23 citations; IF 2.903; JR 122/193; Q3).
81. Finka(PD) A, Sharma(PD) SK and Goloubinoff(PI), P. (2015). Multi-layered Molecular Mechanisms of polypeptide Holding, Unfolding and Disaggregation by HSP70/HSP110 chaperones. Frontiers in Molecular Biosciences 2, 29. (74 citations (GS); IF 3.565; JR 113/299; Q2).
82. Goloubinoff(PI), P. (2016). Mechanisms of protein homeostasis in health aging and disease. Swiss Med Wkly. 146:w14306 (15 citations; IF 1.821; JR711/160; Q2).
83. Finka(PD) A., Mattoo(S) RUH and Goloubinoff(PI), P (2016). Experimental milestones in the discovery of molecular chaperones as polypeptide unfolding enzymes. Annual Reviews of Biochemistry 85:715-742.  (35 citations; IF 26.922; JR 3/299; Q1).
84. Gat-Yablonski(PI) G, Finka(PD) A, Pinto(S) G, Quadroni(T) M, Shtaif(T) B, Goloubinoff(PI), P (2016). Quantitative proteomics of rat livers shows that unrestricted feeding is stressful for proteostasis with implications on life span. Aging 8(8): 1735-1758. (7 citations; IF 5.515; JR 5/53; Q1).
85. De Los Rios(PI) P, Goloubinoff(PI), P. (2016). Hsp70 chaperones use ATP to remodel native protein oligomers and stable aggregates by entropic pulling. Nat Struct Mol Biol. 6;23(9):766-9 (11 citations; IF 12.109; JR 9/299; Q1).
86. Carra(PI) S., Alberti(PI) S., Arrigo(PI) P., Benesch(PI) J., Benjamin(PI) I., Boelen(PI)s W. , Bartelt-Kirbach(PI) B., Bianca(PI) J., Brundel(PI) B.,  Buchner(PI) J., Bukau(PI) B., Carver(PI) J., Ecroyd(PI) H., Emanuelsson(PI) C., Finet(PI) S., Golenhofen(PI) N., Goloubinoff(PI), P., Gusev(PI) N., Haslbec(PI)k M., Hightower(PI) H., Kampinga(PI) H., Klevit(PI) R., Liberek(PI) K., Hassane(PI) S., Mchaourab(PI) H. Kathryn(PI) A. McMenimen(PI) K., Poletti(PI) A., Quinlan(PI) R., Strelkov(PI) S., Melinda(PI) E., Toth(PI) M., Vierling(PI) E., Tanguay(PI) R. (2017). The growing world of small heat shock proteins: from structure to functions. Cell Stress and Chaperones 22(4):601-611. (46 citations; IF 2.903; JR 122/193; Q3).
87. Jacobson(S) T., Priya(PD) S., Sharma(PD) SK., Andersson(S) S., Jakobsson(S) S., Tanghe(S) R., Ashouri(S) A., Rauch(S) S., Goloubinoff(PI), P., Christen(PI) P. and Tamás(PI) MJ. Cadmium causes misfolding and aggregation of cytosolic proteins in yeast. Mol Cell Biol. 11;37(17) e00490-16. (4 citations; IF 3.735; JR 104/299; Q2).
88. Tamás(PI) MJ, Fauvet(PD) B, Christen(PI)  P, Goloubinoff(PI), P. Misfolding and aggregation of nascent proteins: a novel mode of toxic cadmium action in vivo. Curr Genet. 2018 Feb;64(1):177-181 (5 citations; IF 3.464; JR 59/174; Q2).
89. Doron(S) L., Goloubinoff(PI), P. and Shapira(PI), M. (2018) 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. (0 citations; IF 3.565; JR 113/299; Q2).
90. Goloubinoff(PI) P., Sassi(PD) A., Fauvet(PD) B., Barducci(PD), A. and De Los Rios(PI) P. Chaperones convert the energy from ATP into the nonequilibrium stabilisation of native proteins (2018). Natl. Chem. Biol. 14, 388–395.  (14 citations; IF 12.154; JR 8/299; Q1).
91. Kampinga(PI) H.H., Andreasson(PI) C., Barducci(PI) A., Cheetham(PI) M.E., Cyr(PI) D., Emanuelsson(PI) C., Genevaux(PI) P., Gestwicki(PI) J.E., Goloubinoff(PI), P., Huerta-Cepas(PI) J., Kirstein(PI) J., Liberek(PI) K., Mayer(PI) M.P., Nagata(PI) K., Nillegoda(PI) N.B., Pulido(PI) P., Ramos(PI) C., De Los Rios(PI) P., Rospert(PI) S., Rosenzweig(PI) R., Sahi(PI) C., Taipale(PI) M., Tomiczek(PI) B., Ushioda(PI) R., Young(PI) J.C., Zimmermann(PI) R., Zylicz(PI) A., Zylicz(PI) M., Craig(PI) E.A., and Marszalek(PI) J. (2019) Function, evolution, and structure of J-domain proteins. Cell Stress and Chaperones 24(1):7-15. (6 citations; IF 2.903; JR 122/193; Q3).
92. Mazal(S) H, Iljina(PD) M, Barak(T) Y, Elad(S) N, Rosenzweig(PI) R, Goloubinoff(PI), P, Riven(T) I, Haran(PI), G. Tunable microsecond dynamics of an allosteric switch regulate the activity of a AAA+ disaggregation machine. Nat Commun. 10(1):1438. (1 citation; IF 11.878; JR 5/69; Q1).
93. Kumar(S) V, Peter(S) JJ, Sagar(S) A, Ray(S) A, Jha(S) MP, Rebeaud(S) ME, Tiwari(PD) S, Goloubinoff(PI), P, Ashish(S), Mapa(PI), K. Inter-domain communication suppressing high intrinsic ATPase activity of Sse1 is essential for its co-dissaggregase activity with Ssa1. FEBS J. doi: 10.1111/febs.15045 (0 citations; IF 4.739; JR 55/299; Q1).
94. Mathangasinghe(PD), Y., Fauvet(PD), B., Jane(S) SM, Goloubinoff(PI) P., and Nillegoda(PI), NB. (2019) The central role of Hsp70s and co-chaperones in erythropoiesis and RBC survival. Haematologica. 2021 Jun 1; 106(6): 1519–1534. doi: 10.3324/haematol.2019.233056
95. Anthony Guihur(PD), Mathieu Marius Jean Edouard Rebeaud, Bruno Fauvet(PD), Satyam Tiwari(PD), Yoram George Weiss(PI) and Pierre Goloubinoff(PI) (2020) Moderate fever cycles as a mechanism to protect the respiratory system in COVID-19 patients Frontiers in Medicine Published on 11 Sep 2020.
96. A. Guihur, B. Fauvet, A. Finka, M. Quadroni, P. Goloubinoff, Quantitative proteomic analysis to capture the role of heat-accumulated proteins in moss plant acquired thermotolerance. Plant Cell Environ 10.1111/pce.13975 (2020).
97. Fauvet(PD) B., Finka(PI) A., Castanié-Cornet(T) MP, Cirinesi(S) AM, Genevaux(C) P., Quadroni(T) M., and Goloubinoff(PI) P. (2021) Bacterial Hsp90 mediates the degradation of aggregation-prone Hsp70-Hsp40 substrates. Frontiers in Molecular biosciences. Front. Mol. Biosci., 15 April 2021 | https://doi.org/10.3389/fmolb.2021.653073
98. Marija Iljina (PD), Hisham Mazal (PD), Pierre Goloubinoff(PI), Inbal Riven(T), and Gilad Haran(PI) Entropic Inhibition: How the Activity of a AAA+ Machine Is Modulated by Its Substrate-Binding Domain (2021) doi.org/10.1021/acschembio.1c00156
99. M. E. Rebeaud (PD), S. Mallik(PD), P. Goloubinoff (PI), D. S. Tawfik (PI), On the evolution of chaperones and cochaperones and the expansion of proteomes across the Tree of Life (2021) PNAS May 25, 2021 118 (21) e2020885118; https://doi.org/10.1073/pnas.2020885118

100. A. Guihur (PD), B. Fauvet(PD), A Finka (PD), M. Quadroni (T), P. Goloubinoff (PI) Quantitative proteomic analysis to capture the role of heat‐accumulated proteins in moss plant acquired thermotolerance. Plant, Cell & Environment 44 (7), 2117-2133. doi: 10.1111/pce.13975.

101. Y Mathangasinghe (PD), B Fauvet (PD), SM Jane (PD), P Goloubinoff (PI), NB Nillegoda (PI) Haematologica 106 (6), 1519. doi: 10.3324/haematol.2019.233056.

102. B. Fauvet (PD), M. E. Rebeaud (PD), S. Tiwari (PD), P. De Los Rios (PI), and P. Goloubinoff (PI) Repair or Degrade: The Thermodynamic Dilemma of Cellular Protein Quality-Control. Frontiers in Molecular Biosciences | www.frontiersin.org October 2021, Volume 8, doi: 10.3389/fmolb.2021.768888.

103. A. Guihur (PD), M. J. E. Rebeaud (PD), Baptiste Bourgine (PD) and P. Goloubinoff (PI), (2022). How do humans and plants feel the heat? Trends in Plant Sci. 7 March 2022 doi:10.1016/j.tibs.2022.05.004 (1 citations; IF 12.35). doi.org/10.1016/j.tplants.2022.03.006

104. A. Guihur (PD), M. J. E. Rebeaud (PD) and P. Goloubinoff (PI), (2022). How do plants feel the heat and survive? Trends in Biochemical Sci. June 01, 2022. doi:10.1016/j.tibs.2022.05.004 (1 citations; IF 16.889).

105. O. Melanker (PD), P. Goloubinoff (PI), G. Schreiber (PI) In vitro Evolution of Uracil Glycosylase Towards DnaKJ and GroEL Binding Evolves Different Misfolded States. Journal of Molecular Biology. Volume 434, Issue 13, 15 July 2022, 167627.

 

 

(e)        Published scientific reports and technical papers

 

(f)        Unrefereed professional articles and publications

1. Goloubinoff(PI), P., Gatenby. A.A, and Lorimer(PI), G. (1991). The role of chaperonins in the folding of proteins. Aids Research and Human Retroviruses 7, 193.
2. Balogi(S) Z., Glatz(PD) A., Balogh(S), G., Nagy(S), E., Liberek (PI) K., Debreczeny(S), M., Goloubinoff(PI), P., Horvath(C) I., and Vigh(PI) L. (2005). The emerging role for small heat-shock proteins in the regulation of lipid composition and dynamics of cell membranes. FEBS J., 272, 358 (0 citations; IF 4.739; JR 55/299; Q1).
3. Horvath(C), I., Balogi(S), Z., Giese(S), K., Chergy(S), O., Glatz(PD), A., Vass(S), I., Goloubinoff(PI), P., Vierling (PI), E. and Vigh(PI), L. (2006) Small heat shock proteins interact with membranes and affect membrane physical state and function. FEBS J. 273, 81 (0 citations; IF 4.739; JR 55/299; Q1).
4. Bromberg(S), Z., Goloubinoff(PI), P., and Weiss(PI) YG. (2009). Activation of the heat shock response by membrane dependent calcium channel receptors - effects in inflammation and cancer. Shock, 31: 39 (0 citations; IF 3.083; JR 11/33; Q2).
5. Weiss(PI) YG. Bromberg(S), Z., and Goloubinoff(PI), P., (2009). Activation of the heat shock response by membrane dependent calcium channel receptors effects in inflammation and cancer. Intensive Care Medicine, 35: 38 (0 citations; IF 18.967; JR 2/33; Q1).
6. Gat-Yablonski(PI) G, Finka(PD) A, Pinto(S), G, Quadroni(T) M, Shtaif(S), B., Goloubinoff(PI), P (2016). Quantitative proteomics of rat livers shows that unrestricted feeding is stressful for proteostasis with implications on life span. Hormone Research in Pediatrics 86: 60. (0 citations; IF 2.324; JR 102/145; Q3).
7. Mileo(PI), E., Ilbert(PI), M., Barducci(PI), A., Bordes(PI), P., Castanié-Cornet(PI), M., Garnier(PI), C., Genevaux(PI), P., Gillet(PI), R., Goloubinoff(PI), P., Ochsenbein(PI), F., Richarme(PI), G., Iobbi-Nivol(PI), C., Giudici-Orticoni(PI), M., Gontero(PI), B., and Genest(PI) O. (2018) Emerging fields in chaperone proteins: A French workshop. Biochimie 151, 159-165 (0 citations; IF 3.362; JR 123/299; Q2).
8. Goloubinoff(PI), P. (2014). Recent and future grand challenges in protein folding, misfolding, and degradation. Front. Mol. Biosci. 1:1. (5 citations (GS); IF 3.565; JR 113/299; Q2).
9. Goloubinoff(PI), P. (2017). Editorial: The HSP70 molecular chaperone machines. Frontiers in Molecular Biosciences, 24 January 2017. Front. Mol. Biosci. doi: 10.3389/fmolb.2017.00001 (6 citations; IF 3.565; JR 113/299; Q2).

 

Non-scientific Books and novels:

 

Tawil, H., Miodownik, S. and Goloubinoff, P. (1998) “Operation Esther: Opening the Door for the Last Jews of Yemen” Belkis Press, New York. ISBN 0966757505

 

In French under the pen name Dawoud Hamami.

Dawoud Hamami (1994). Les exilés du Yémen heureux. L’Harmattan, Paris. ISBN : 2-7384-2923-8
 

Dawoud Hamami (2004). Banei Al-Yaman; Les fils du Sud. Le Publieur, Paris. ISBN 10 : 2754900020 / 2-7549-0002-0 ISBN 13 : 9782754900027

 

Dawoud Hamami (2008) Rencontre en Arabie heureuse. Le Publieur, Paris. ISBN-10: 2754900764 ISBN-13: 978-2754900768

 

 

•        Lectures and Presentations at Meetings and Invited Seminars

 

(a)        Invited lectures at conferences/meetings

1993    Invited speaker at the Keystone meeting on Plant genome variation February 3-10, 1993. Taos. NM. USA

1995    Invited speaker at the Annual Congress of the Israeli Association of Microbiology, March 1995, The Technion, Haifa. Israel

1995    Invited speaker at the 2nd International Conference of the Hungarian Biochemical Society. August 21-23, 1995, Szeged, Hungary.

1996    Invited speaker at the 10th G.I.F meeting on Cell Biology of Protein Interaction 10-15 March 1996, Dead Sea, Israel

1996    Invited speaker and session chair at the EMBO conference on Molecular Chaperones, April 1-5, 1996, Coventry, UK.

1996    Invited speaker at the 8th International congress of Bacteriology and Applied Microbiology, August 18-23, 1996 Jerusalem, Israel.

1996    Invited speaker and session chair at the Second Mini symposium on Intracellular Trafficking, The Weizmann Institute of Science, Oct. 16, 1996, Rehovot, Israel.

1997    Invited speaker at the Biology of Molecular Chaperones meeting by the European Science Foundation. May 22-27, 1997. Obernai, France.

1997    Invited speaker at the International Congress Stress of Life, July 1-4 1997, Budapest, Hungary.

1997    Invited speaker at the Annual meeting of the Italian Society for Biochemistry. September 1997, Ancona, Italy.

1998.   Invited speaker at the Interdisciplinary Stockholm-Jerusalem Workshop on The Biology of Stress. March 1-3, 1998, Jerusalem, Israel.

1998    Invited speaker at the IX International Congress on plant tissue and cell culture. June 14-19, 1998, Jerusalem, Israel.

1999    Invited speaker at the 1999 Gordon conference on Temperature Stress in Plants, Jan. 31-Feb. 5, 1999. Ventura CA, USA.

1999    Invited speaker at the Biology of Molecular Chaperones meeting by the European Science Foundation. May 22-27, 1999. Marratea, Italy.

1999    Invited speaker and member of the Scientific Committee of The Bat-Sheva de Rothschild Seminar on Gene Regulation During Stress. June 13-17, 1999, Beer Sheva, Israel.

1999    Invited speaker at the FEBS meeting, June 19-24, 1999, Nice, France.

1999    Session Chair at the "Protein folding translocation" meeting, July 22-24 1999, Freiburg, Germany.

1999    Invited speaker at the International Meeting "Integration of Signaling pathways: The role of Multi-protein Complexes" November 2-5, 1999, Kibbutz Ma'agan, Sea of Galilee, Israel.

2000    Invited speaker "Enzymillennium: from enzyme evolution to industrial biocatalysis", a Binational UK-Israeli Symposium on Biotransformations and Biosynthesis. February 14-17, 2000, Tel Aviv, Israel.

2000    Invited speaker at the FASEB meeting on Protein folding and assembly in the Cell, July 22-27, 2000, Vermont, USA.

2001    Invited speaker at the "chaperonins: structure and function" meeting, November 6-8, 2000, Madrid, Spain. Invited speaker at the French-Israeli cooperation meeting (AFIRST) Paris, January 2001

2001    Invited speaker at the Euro-conference and EMBO workshop on "Mechanisms and Cellular Functions of Molecular Chaperones", May 26-May 31, 2001. San Feliu de Guixols, Spain.

2002    Invited speaker at the Conférences 3ieme cycle Romand, Plant Molecular Biology, Neuchatel September 21, 2002.

2002    Invited speaker at the Swiss Plant Molecular and Cell biology Meeting 27/2-1/3/2002 Adelboden, Switzerland.

2002    Invited speaker Biological Stress minisymposium, May 20-23, 2002 Jerusalem, Israel

2002    Invited speaker Annual Meeting of the Istituto Nazionale Fisica della Materia (INFM) June 24-28, 2002 Bari, Italy.

2002    Invited speaker, Session organizer and chair, FEBS 2002 meeting, 20-25 October 2002 Istanbul, Turkey.

2003    Invited speaker. Conférences 3ieme cycle Romand on “Living Matter: a new challenge to physicists” 2-8 March 2003, Les Diablerets, Switzerland.

2003    Invited speaker. ESF/FEBS meeting on protein folding and molecular chaperones. Aug. 30-Sept 4 2003, Tomar, Portugal

2003    Invited speaker. At the Swiss-Japanese workshop on "Biogenesis, Function and Acclimation of the Photosynthetic Apparatus" Kurashiki, Japan, Sept 29-Oct 2, 2003.

2004    Invited speaker. At (organized by FGF, WHO, COST281 and STUK Finland on “the Influence of RF Fields on the Expression of Stress Proteins" April 28 -29, 2004, STUK Helsinki, Finland.

2004    Co-Organizer and Invited Speaker "Protein Folding, Aggregation and Disassembly
in Cell Biology and Disease ", Villars-sur-Ollon, Switzerland, September 18-22, 2004.

2004    Invited speaker. EMBO workshop on “Hsp90” Gwatt, Switzerland Sept. 25-29, 2004.

2005    Invited Speaker and poster presenter : “The 14th Swiss Plant Molecular and Cell Biology Conference” Les Diablerets March 9-11, 2005.

2005    Invited Speaker: First Scientific Workshop and Management Meeting COST Action 859 on “Phytotechnologies to promote sustainable land use and improve food safety” 14-16 June 2005 Pisa, Italy.

2005    Invited Speaker and session chair at the "Moss 2005" meeting, Brno, Check republic, July 23-26, 2005.

2006    Invited Speaker at COST Action 859 Swiss meeting, Lausanne, Switzerland, January 12, 2006.

2007    Organizer and Speaker at the “The 16th Swiss Plant Molecular and Cell Biology Conference” Les Diablerets, March, 2007.

2007    Invited "raporteur" at the COST Action 859 "Fate of Pollutants in the Plant/Rhizosphere System Vilnus Mai 29-june 2 2007.

2007    Invited Speaker at the 8th International Conference on Alzheimer's Drug Discovery - New York, USA - October 15-16, 2007.

2007    Invited facilitator at the 2008 Drug Discovery for Neurodegeneration Conference Washington, DC - February 4-5, 2008

2008    Invited Speaker Second International conference "Towards a mechanism-based framework in EMF research". Zurich, Switzerland May 5-6 2008.

2009    Organizer et Speaker Joint UNIL-EPFL mini-Symposium on “The Hsp70 chaperone machinery, physics, structural chemistry, biochemistry and biology” January 14, 2009

2009    Invited speaker at The 18th Swiss Plant Molecular and Cell Biology Conference” Les Diablerets, January 21-23, 2009.

2009    Invited speaker at the symposium on Non-ionising Radiation: Health and Environment, Satelite of BioEM 2009 Congress in Davos, Switzerland, June 13 and 14, 2009.

2010    Invited speaker at the international meeting on: Thermodynamically unstable proteins: chance or necessity? December 14-16 2009 Trieste, Italy.

2010    Invited speaker at the 2nd International BIOmics Weizmann Institute, Israel November 15-18 2010.

2011    Invited speaker at the 5Th International Congress on Stress Responses in Biology and Medicine, Québec, Canada, August 21-25 2011.

2011    Invited speaker at the CSCH worshop on molecular chaperones and aging Chateau Bonaventure Québec, Canada, August 26 2011.

2011    Invited speaker at the Industrial Biotechnology PhD Meeting from the Università degli Studi di Milano-Bicocca Verbania Pallanza, October 23-25, 2011

2012    Invited speaker at the 2nd International Conference on"Perspetives of Cell Signalling and Molecular Medicine" January 8-11, 2012 at Bose institute, Kolkata, India.

2012    Invited speaker at the research workshop of the Israel Science Foundation on Protein Folding: Moving beyond simple model systems. May 14-17, 2012. The Weizmann Institute of Science, Rehovot, Israel.

2012    Invited speaker at "the 6th International Conference on theHsp90 chaperone machine" in les Diablerets, Switzerland September 19 to 23 2012.

2012    Invited speaker at The 6th International Symposium on Heat Shock Proteins in Biology and Medicine”. Washington DC November 3-6, 2012.

2013    Invited speaker at the FEBS Congress on Biochemistry of Stress Response in St Petersburg, July, 6-11, 2013.

2013    Invited speaker at the 9th Parnas conference of the Polish, Ukrainian and Israeli (ISBMB) Biochemical Societies. Jerusalem, September 29-October 2, 2013.

2014    Invited speaker at the 10th International Conference on Protein Stabilization 7-9 May 2014, Stresa (Lake Maggiore, Italy).

2014    Invited speaker at the European Summer School on Industrial Biotechnology: Stability, Folding, and Misfolding of Recombinant Proteins Milano, Oct 6-10, 2014

2014    Invited speaker at The 1st international conference on "Molecular mechanisms of cellular surveillance and damage responses", Heidelberg, Germany November 9-11, 2014.\

2014    Invited speaker at EMBO workshop on “The regulation of aging and proteostasis 15 – 20 February 2015, Maale Hachamisha, Israel.

2015    Invited speaker at the EMBO workshop on Macromolecular assemblies at the crossroads of stress and function.  May 31-June 4 2015. Jerusalem, Israel.

2016    Invited speaker at the Second International Workshop on The small HSP World October 12-15, 2016. CEUB, Residenziale Centro Residenziale Universitario di Bertinoro, Italy

2016    Invited speaker at the 3rd PROTEOSTASIS Action Meeting covering topics in “Proteostasis and its Biological Implications” on 2nd-5th of November 2016 in Lisbon, Portugal.

2016    Invited speaker at the mini symposium on “Mechanisms of unfolding chaperones” Nov 28, 2016 Ben Gurion University, Israel.

2017    Invited speaker at the 3rd International Conference on perspective of cell signaling and molecular medicine. 8-10 January, 2017 Bose Institute, Kolkata, India.

2018    Invited speaker at the SwissPlant 2018 Symposium, Meiringen Jan 31-Feb2 2018.

2018    Invited speaker at the “Function, Evolution, Structure of Co-chaperones Having a J-domain” International Workshop of Cell Stress Society International (CSSI) 4-7 April 2018- Gdansk, Poland.

2018    Invited Speaker at the Ninth International Conference on the Hsp90 Chaperone Machine October 2018, in Leysin, Switzerland.

2019    Chair, invited speaker at the “Protein quality control: From mechanisms to disease” 28 April – 03 May 2019 | Costa de la Calma (Mallorca), Spain

2019    Invited Speaker Plant responses to a changing environment. Weizmann Institute of Science, Israel, September 8 2019.

 

(b)       Presentation of papers at conferences

1993    Poster presenter at the meeting of the European Science Foundation on The Biology of Molecular Chaperones, September 13-17 1993, Canterbury, UK.

1994    Poster presenter at the FASEB meeting on Protein folding and assembly in the Cell, June 4-9, 1994, Vermont, USA.

1995    Poster presenter and selected speaker at the Keystone meeting on Molecular Chaperones in Medicine, February 25-March 5, 1995, Santa-Fe, NM, USA

1995    Poster presenter and selected speaker at the meeting of European Science Foundation on The Biology of Molecular Chaperones, September 14-19 1995, Crete, Greece.

1995    Poster presenter and selected speaker at the First Conference of the Israeli Associations of Biology, October 17-20, 1995, Eilat, Israel.

1996    Poster presenter at the FASEB meeting on Protein folding and assembly in the Cell, July 29, 1996, Vermont, USA.

1998    Poster presenter and selected speaker at the EMBO Workshop on Protein Folding & Misfolding inside and outside the Cell March 25-28 1998, University of Oxford, UK.

2002    Poster Presenter at the EMBO lecture course “The Biology of heat shock proteins and molecular chaperones” September 25-29, 2002 Warsaw, Poland

2004    Poster presenter Cold Spring Harbor “Molecular Chaperones and the Heat Shock Response“, May 5-9 2004. Cold Spring Harbor, NY

2005    Poster presenter. Protein aggregation and amyloid formation in systemic and neurodegenerative disease: Physical, molecular and biological approaches. 16-19 July 2005, EPFL-Lausanne, Switzerland.

2006    Poster presenter. “The 15th Swiss Plant Molecular and Cell Biology Conference” Bad Raggaz, March 16-18, 2006.

2007    Invited participant First International Workshop: "Dosimetry meets epidemiology" Zurich, Switzerland 11 January 2008.

2008    Poster presenter Cold Spring Harbor “Molecular Chaperones and the Heat Shock Response“, March 30-May 4 2008. Cold Spring Harbor, NY

2008    Session chair and poster presenter: "Euroem2008" Lausanne EPFL. July 20-25.

2009    Participant session Chair at the FEMS and NoE EPG Bacterial Pathogenomics Conference. Ein Gedi, Israel, February 22-25, 2009

2009    Invited participant at the 99th International Titisee Conference on cellular safeguards and quality control. March 25 to 29, 2009 in Titisee, Germany

2009    Speaker at the Biology of Molecular Chaperones. Dubrovnik, Crotia, 27 May 1 June, 2009.

2010    Poster presenter at the Gordon Research conference on "Protein Folding Dynamics" January 10-15, 2010 Ventura CA, USA.

2010    Speaker at the First ALPS meeting, the meeting of the arc lémanique plant science. October 8, 2010 in Pully, Switzerland.

2010    Speaker at the EMBO Conference Series “The Biology of molecular chaperones: From Basic Mechanisms to Intervention Strategies in Disease and Aging” 19 - 24 May 2011 Grundlsee, Austria

2010    Speaker at the Gordon Conference Stress Proteins in Growth, Development & Disease. July 17-22, 2011. Il Ciocco Hotel and Resort Lucca (Barga), Italy

2014    Speaker at the symposium “25 years of chaperone research: Protein Folding, in and out of Anfinsen's closet”. January 13-15 2014, Arolla, Switzerland.

2014    Poster presenter at the Cold Spring Harbor “Molecular Chaperones and Stress Response“, April 29-May 3 2014. Cold Spring Harbor, NY

2015    Session chair at the EMBO conference Molecular chaperones: From molecules to cells and misfolding diseases. 8 – 13 May 2015 | Heraklion, Greece

 

(c)        Presentations at informal international seminars and workshops (partial, since 2017)

2017    Wizo Woman Center Rehovot, Israel. Subject: The last wave of Jewish emigration from Yemen.

2019    EMBO workshop Mallorca, Spain: Introduction to molecular chaperones.

 

(d)       Seminar presentations at universities and institutions (partial, since 2017)

2017    RKMVC College Rahara, Kolkata. Subject: mechanisms of molecular chaperones in degenerative diseases.

2017    University of Neuchatel. Subject: molecular mechanisms of chaperones.

,2017   CRAG Barcelona, Spain. Subject: mechanisms of heat-shock signalling and HSPs in plants.

2017    Weizmann Institute of Sciences (Maya Schuldiner’s Group). Subject: Quantitative proteomics of the HSPome.

2017    Weizmann Institute of Sciences. Subject: Mechanism of unfolding chaperones.

2017    IGIB, New Delhi, India. Subject: The mechanism of Hsp110 chaperones

2017    Shiv Nagar University, India. Subject: mechanisms of heat-shock signalling and HSPs.

2017    CNRS, Marseilles, France. The non-equilibrium mechanism of ATP-fuelled molecular chaperones

2017    University of Stockholm. Subject: The origin and function of HSP110 co-chaperones

2018    BGU, Israel. Subject: HSP70-40 chaperones use a start-stop mechanism to optimize coupling between ATP hydrolysis and protein disaggregation

2019    BGU, Israel. Subject: The evolutionary history of the protein quality control network.

2019    Weizmann Institute of Sciences. Subject: a start-stop in J-domain cochaperones

2019    Weizmann Institute of Sciences. Subject:  The evolutionary history of the Chaperone network

2019    Weizmann Institute of Sciences. Plant Science. Subject:  the role of HSPs in Plant heat sensing and signaling

2019    IGIB New Delhi. India. Subject: The non-equilibrium mechanism of ATP-fuelled molecular chaperones

2019    CSIR Lucknow, India. Subject: Heat-shock biology and mechanisms of molecular chaperones

2019    CSIR Lucknow, India. Subject: The evolutionary history of the protein quality control network.

 

 (e)       Conference and meeting tasks

2004    Co-organizer of the "Protein Folding, Aggregation and Disassembly in Cell Biology and Disease", Villars-sur-Ollon, Switzerland, September 18-22, 2004.

2007    Co-organizer of the “The 16th Swiss Plant Molecular and Cell Biology Conference” Les Diablerets, March, 2007.

2014    Organizer of the symposium “25 years of chaperone research: Protein Folding, in and out of Anfinsen's closet”. January 13-15 2014, Arolla, Switzerland.

2020    Co-organizer of the "Cellular and Protein Homeostasis Webinars"

 

•           Patents

April 2000       European patent no 00109270.9-1212 "Methods for regulating protein conformation using molecular chaperones". Co-inventor with Prof. Bernd Bukau from the University of Freiburg, Germany.

May 2008        Joined patent application between Lausanne University and Hadassah medical school, Jerusalem: On the Use of specific inhibitors of the cellular heat-shock response in chemotherapies of cancers

 

•           Research Grants

1992-1995       Grant No. 00015/1 from the United States-Israel Binational Science Foundation. "Structure-function analysis of the GroE chaperonin protein: a mutagenesis approach". US collaborator Dr. G. Lorimer. E.I. DuPont de Nemours and Company. 95,000 US $

1992-1995       Grant 1180 from the Joint German Israeli Research Program (BMFT). "Analysis of the chaperonin protein by mutagenesis and Physicochemical approach". German collaborators: Professor Dr. Rainer Jaenicke, Dr. J. Buchner. Universität Regensburg. 105,000 DM

1993-1996       Co-Investigator with Boaz Shaanan (Principal investigator) on Grant 158-93 from the Israel Science Foundation. "Analysis of the GroESL chaperonin by X-ray crystallography and chemical crosslinking (about 25,000 US $ for my part)

1996-1999       Grant from the German Israeli Foundation (GIF). "Elucidation of The Mechanism of GroE-Mediated Protein-Folding using Electron Microscopy, Chemical Modification and Mutagenesis". Collaborators: Dr. Johannes Buchner, Dr. Reinhard Rachel, Universität Regensburg. 80,000 DM total

1999-2001       Grant Israel-Hungary scientific cooperation: Analysis of the molecular mechanism that controls stress-damage in proteins and biological membranes by a small heat-shock protein from Synechocystis PCC 6803. Collaborator: Dr. L. Vigh, Szeged. 10,000 US $ Total

1999-2001       Grant from the Israeli Ministry of Sciences. Franco-Israeli Scientific Cooperation (AFIRST) "Genetic and molecular analysis of the chaperone and ubiquitin networks involved in the stress response in Arabidopsis thaliana.". In collaboration with Dr. P. Genschick from the CNRS, Strasbourg. 40,000 US $ Total

2000-2003       Grant from the United States-Israel Binational Science Foundation. "The role of molecular chaperones in prion propagation and curing". US collaborator Dr. Yuri Chernoff, Georgia Inst. Technology, Atlanta, GA. (75,000 US $ for my part)

1. 2004. Grant with Dr. Ron Mittler (co-investigator) from the Israel National Academy of Science. Response of plants to extreme environmental conditions: characterization of the acclimation mechanisms of Retama raetam to the desert ecosystem. (About 52,000 US $ Total for my part).

1. 2005. Grant from the Swiss National Fund “Molecular analysis of the chaperone network in Arbidopsis plants, in mosses and in vitro.” 340,000 CHF

2002                Grant from the Herbette Foundation to finance in part the Sabbatical visit of Dr. Sophia Diamant from the Hebrew University of Jerusalem. 12’000 CHF

2002                Grant from the Herbette Foundation to finance in part a phytotron. 30’000 CHF

1. 2006. Internal Grant from the Faculty of Biology and Medicine from the Zwahlen fund for “Biochemical analysis of native and aggregated a-synuclein and of the mechanism by which the Hsp70 chaperone can solubilized a-synuclein fibres involved in Parkinson’s disease”. 50’000 CHF

2005-2006      Grant from the Herbette Foundation to finance the sabbatical stay of Prof David Macherel 12’000 CHF

2005-2008      Grant from the Swiss Ministry of Sciences for COST Action 859, "Development of multipurpose plant biosensor arrays for chemical and environmental stresses"180'000 CHF

2005-2008      Grant 3100A0-109290 from the Swiss National Fund: Mechanisms of ATPase disaggregating molecular chaperones: emphasis on hsp70-mediated forceful unfolding of stable protein aggregates 340,000 CHF Total

2005                Grant from the Herbette Foundation to finance the Student's expenses to the 16th Swiss Plant Molecular and Cell Biology Conference 2’400 CHF

2007-2009      Grant from the Swiss National fund NRP57 "Characterization of effects of non-ionising radiations on the nematode Caenorhabditis elegans as a model organism" 300'000 CHF

2008-2011      Grant from the Swiss Ministry of Sciences for COST Action BM0603. "Plant-based primary screen and animal-based chaperone inducing screens for drugs against protein misfolding diseases 120'000 CHF

2008-2011      Grant from the Alzheimer Drug discovery foundation, NY ""Plant-based primary screen for chaperone inducing screens for drugs against Alzheimer's disease: 80'000 US $

2009-2011      Grant 31003A-125502/1 from the Swiss National Fund: “Mechanisms of Hsp70/40 chaperones: substrate recognition and disaggregation studies” 375’000 CHF

2010-2011       Travel and housing grant Visiting Scientists of the Weizmann Institute of Science.

2012-2015      Grant 31003A-140512/1 from the Swiss National Fund: “Biochemical and biophysical analysis of the polypeptide-unfolding mechanism of human and bacterial Hsp70s and their Hsp40/Hsp110/Hsp100NEF co-chaperones” 440,359 CHF

2015-2018      Grant 31003A_156948 from the Swiss National Fund: Analysis of the disaggregation mechanism by the human cytoplasmic HSP70-HSP110 bi-chaperone machinery.” 550,000 CHF

2016-2018      Grant C15.0042 from the Swiss State Secretariat for Education Research and Innovation (SEFRI) for COST Action BM13014. “Directed molecular evolution to generate specific disaggregating chaperones to solubilize toxic PolyQ aggregates” 180'000 CHF

2018-2022       Grant 31003A_175453 from the Swiss National Fund: “Synthetic design and directed evolution of disaggregating chaperones to detoxify disease-causing aggregates” 572’000 CHF

2020-2021      Grant from the Herbette Foundation to finance the sabbatical stay of Prof Paolo Casio 12’000 CHF

2021-2024      Grant 90 3150/2 from the Israel Science Foundation. Analysis of heat-sensing and heat-signaling mechanisms in higher plants. 270’000 IS per year.

 

 

•                       Present Academic Activities

 

Main scientific Collaborations in the last decade:

Research in progress

What is the molecular mechanism by which HSP110s potentiates HSP70s in their ability to solubilize stable protein aggregates? October, 2022.

 

Is Hsp70 recruited to re-potentiate heat-depolarized calcium channels in the plasma membranes of plants? October, 2022.

 

Books and articles to be published

 

In preparation:

 

Rebeaud(S) M., Tiwari(PD) S., Fauvet(PD), B., De Los Rios(PI) P. and Goloubinoff(PI) P. (2022) HSP40s contain an inbuilt stop-start mechanism to prevent futile ATP hydrolysis by HSP70          

 

•   Synopsis of research, including reference to publications and grants in above lists

 

Perception of stress and the mechanisms of molecular chaperones

Molecular chaperones are proteins that assist the (un)folding of other proteins in the cell. Chaperones assist the initial proper folding of newly synthesized proteins and serve as active components in the translocation of proteins between cellular compartments, as well as in the signal transduction. Many molecular chaperones are stress-induced proteins (HSPs). During and following stress, such as heat-shock, they are involved in the prevention of protein misfolding and aggregation in the cell. Some chaperones can also actively unfold and solubilize protein aggregates and assist in their proper refolding or in their degradation by proteases. Hence, the chaperone network provides central mechanisms for the protection and the recovery from stress-induced damaged proteins, in simple prokaryotes, as well as in complex eukaryotes. We are also interested in the mechanism for perception of heat-stress by organisms as diverse as bacteria and higher plants.

Our long-term goal is to understand the chaperone network in bacteria, plant and human, in order to better prevent protein misfolding and promote the active curing of toxic protein aggregates in bacteria, plants, and especially in the case of protein misfolding diseases in mammals. As model organisms we use enterobacteria, cyanobacteria, the moss Physcomitrella patens and the higher plant Arabidopsis thaliana. Our experimental approaches combine genetics, biochemistry and biophysics.

 

1. What is the molecular mechanism by which HSP110s potentiates HSP70s in their ability to solubilize stable protein aggregates?

Background:  In aging mammals, various protein aggregates can cause tissue degeneration, as in Huntington and Parkinson diseases. To maintain protein homeostasis, all organisms house a network of chaperones and co-chaperones that can effectively maintain, at least in youth, low levels of harmful protein conformers below toxicity thresholds. The HSP70s, serve as the core of the network. In Mammals, it constitutes 1% of the total cellular proteome. Hsp70 can use ATP to forcefully unfold potentially toxic aggregates and revert them into harmless functional proteins. In bacteria, HSP70 forms together with a member of the AAA+ protein family, HSP100 (ClpB), a disaggregating machinery, whose mechanism is rather well-characterized. In contrast, animal cells don’t express bona fide HSP100s. Rather, a completely different type of disaggregating co-chaperone, named HSP110, which stemmed out of the HSP70s tree in the first eukaryotes, forms together with HSP70, a completely different disaggregating machinery that too can solubilize protein aggregates, albeit by mechanism that is currently unknown. Despite clear sequence and structure homologies with HSP70, HSP110 is generally thought to lack chaperone activity of its own, and serve as a nucleotide exchange factor (NEF), merely accelerating ADP release from HSP70. How, assisted by DNAJ, may the HSP70s and HSP110s precisely identify, bind and use ATP to unfold and solubilize stable aggregated substrates? This remains unclear and is a matter of great scientific interest. Both bacterial ClpB-based and HSP110-based disaggregating machineries co-exist in the cytosol of plants and fungi, implying that the two machines unlikely process the same types of aggregates, and complement each other by processing the resistant species of the other. We have expressed and purified the major components of the yeast cytosolic chaperone network: HSP100 (HSP104), HSP70s (SSA1, SSA2), DNAJ co-chaperones (SIS1, YDJ1) and the NEFs HSP110s (SSE1, SSE2, FES1), as well as HSP90 and HSP26. We have set effective in vitro assays for ATP ase and chaperone-mediated disaggregation and reactivation of stable protein aggregates and are currently using various biophysical and biochemical methods to decipher the role of each component in the chaperone network of the yeast cytosol.

 

Objectives: We are currently focusing on deciphering the molecular mechanism by which the HSP110 (yeast SSE1), acts upon HSP70 and how both can, effectively target, unfold and solubilize stable protein aggregates, leading to the native refolding of toxic aggregated species. Our objective is to use methods of molecular biology, biochemistry, directed molecular evolution and synthetic biology, to revert, stepwise, HSP110 to its earliest evolutionary stage, when in the first eukaryote about 2 billion years ago, it just became an effective disaggregating co-chaperone of HSP70s, while still keeping some of its original bona fide unfolding activity from its HSP70 ancestors. Our long-term objective is to understand the spectrum of action, the potential, as well as the limitations, of the HSP110-HSP70 disaggregation machineries, in order to better understand how metazoans that lost the other bacterial disaggregating machinery, may specially suffer from degenerative conditions, such as aging and age-related neurodegenerative diseases. I plan to apply for a grant from the Israel Science Foundation on this subject.

 

2. Is Hsp70 recruited to re-potentiate heat-depolarized calcium channels in the plasma membranes of plants?

 

Background:  Specific cyclic nucleotide gated channels (CNGCs) in the plasma membrane of higher plants act as plant thermo-sensors (Finka et al., 2012). The land plant CNGC2 contains a C-terminal cytosolic domain that can bind calmodulins and cyclic nucleotides. Upon an abrupt temperature increase, the closed channel readily opens to allow transient entry of extracellular Ca2+ ions into the cytosol, in turn activating the bound calmodulin(s) and initiating a specific signal cascade to overproduce heat-shock proteins (HSPs). Many HSPs act as molecular chaperones that can protect and repair structurally heat-damaged proteins. Yet, within minutes, the heat-depolarized channels become hermetically closed again, stopping heat-signals for more HSP production, despite an ongoing heat-stress. Up to five hours back at low temperatures are needed for plants to fully re-potentiate their heat-depolarized CNGCs and effectively produce more heat-shock proteins. Using the C-terminal cytosolic domain of CNGC2 as bait, we have recently identified in a yeast-two-hybrid screen a unique plant DNAJC protein. DNAJ co-chaperones generally target the HSP70 chaperone onto protein complexes that need to become converted into structurally different complexes. Like HSP60s, HSP70s can inject energy from ATP hydrolysis to convey, even under non-equilibrium conditions, stable misfolded proteins up a free energy landscape, and transiently convert them into a less stable native state (De Los Rios and Goloubinoff, 2016). We thus hypothesize that at non-heat-shock temperatures, this specific DNAJC is recruiting HSP70 onto the relaxed heat-depolarized, closed CNGC2, to use the energy of ATP hydrolysis to re-potentiate them into a different “tensed” closed state with a higher free energy, poised to readily respond to the next upcoming heat-shock.

Objectives: The long-term objective of this project is to decipher the mechanism by which the plant heat-sensory CNGCs, once depolarised by heat, may become tensed again after heat stress by the combined action of DNAJC and HSP70. We are using targeted CRISPR-mediated mutagenesis to knockout, as well as to cause the over expression of the DNAJC gene, in the model land plant Arabidopsis thaliana. We are also undertaking a Bioluminescence Resonance Energy Transfer (BRET) approach in an attempt to visualize in vivo the recruitment of HSP70 to the CNGCs after the heat-stress and the conditional interaction of DNAJC with the CNGC and with the recruited HSP70 molecules. We are also applying various biochemical and biophysical methods and we purified the DNAJC, aiming to determine its structure by X-ray crystallography and to decipher in vitro the precise molecular mechanism by which the DNAJC-recruited HSP70s onto the CNGCs can effectively use the energy of ATP hydrolysis for the transient stabilization of the tensed conformation of the channel, rendering it poised to readily respond to a next upcoming heat-shock. Because it is not known how related calcium channels in animals, such as the TRPVs, which similarly respond to heat-stress and signal for HSP accumulation, become re-polarized after the stress, this research may have important long-term biomedical implications.

 

Awards, Citations, Honors, Fellowships

(a) Honors, Citation Awards

1991-1994     Ygal Allon fellowship for young Israeli Scientist

1992              Recipient of the 1992 Gablinger Prize for Outstanding Researcher (Swiss-Israel).

1992              Recipient of the 1992 Bergman award (Israel, National) from the United States-Israel Binational Science Foundation

1995              Holder of the Lectureship Chair of Botany named after L. Cohen.

1996              Recipient of the 1996 M. Landau prize (Israel, National) for Young Scientists, from the Israeli lottery

1997-1998     Best lecturer of the year in Biochemistry department

 

 

(b) Fellowships

1982-1987     Scholarship from the Feinberg Graduate school of the Weizmann Institute of Science

1990-1991     Postdoctoral Grant from the Swiss National Fund

1998-1999     Long-Term Research Fellowship from the A. von Humboldt foundation (Germany)