Our Publications

The technologies and innovative tools and discovery platforms employed by ND-Biosciences are based on 17 years of innovation and pioneering work that was carried out at the laboratory of its co-founder, Prof. Hilal A. Lashuel, and are well-documented in many high-impact peer-reviewed publications. 

Below is a list of key publications related to ND-Biosciences technologies and R&D platforms. Please check Prof. Lashuel’s PubMed page for a complete list of publications.

Preclinical Models of Parkinson’s and Alzheimer’s Disease
  1. Fares MB, Jagannath S, Lashuel HA. Reverse engineering Lewy bodies: how far have we come and how far can we go? Nat Rev Neurosci. 2021 Feb;22(2):111-131. doi: 10.1038/s41583-020-00416-6. Epub 2021 Jan 11.
  2. Mahul-Mellier AL, Burtscher J, Maharjan N, Weerens L, Croisier M, Kuttler F, Leleu M, Knott GW, Lashuel HA. The process of Lewy body formation, rather than simply α-synuclein fibrillization, is one of the major drivers of neurodegeneration. Proc Natl Acad Sci U S A. 2020 Mar 3;117(9):4971-4982. doi: 10.1073/pnas.1913904117. Epub 2020 Feb 19. PMID: 32075919; PMCID: PMC7060668.
  3. Fares MB, Maco B, Oueslati A, Rockenstein  E, Ninkina N, Buchman V, Masliah E, Lashuel HA*. Induction of de novo α-Synuclein fibrillization in a novel neuronal model for Parkinson’s disease. Proceedings of the National Academy of Sciences. 2016, 16;113(7): E912-21.
  4. Mahul-Mellier A, Vercruysse F, Maco B, Ait-Bouziad N, De Roo M, Muller D and Lashuel HA*. Fibril growth and seeding capacity play key roles in α-synuclein-mediated apoptotic cell death. Cell Death and Differentiation. 2015, (12):2107-22.
  5. Jan A, Adolfsson O, Allaman I, Buccarello AL, Magistretti PJ, Pfeifer A, Muhs A, Lashuel HA*. Aβ42 neurotoxicity is mediated by ongoing nucleated polymerization process rather than by discrete Aβ42 species. Journal of Biological Chemistry. 2011, 286(10):8585-96.
Therapeutic Strategies for Alzheimer’s, Parkinson’s and Huntington’s Disease
  1. DeGuire SM, Ruggeri SM,Fares MF,Cendrowska U,Dietler G,and Lashuel HA*. Phosphorylation at S13 and/or S16 strongly inhibits the aggregation of mutant Httex1, regulates its helical conformation and prompts the internalization and nuclear targeting of preformed Httex1aggregates. Journal of Biological Chemistry. 2018, 293(48):18540-18558.
  2. Eleuteri S, Di Giovanni S, Rockenstein E, Mante M, Adame A, Trejo M, Wrasidlo W, Wu F, Fraering PC, Masliah E, Lashuel HA*. Novel therapeutic strategy for neurodegeneration by blocking Aβ seeding mediated aggregation in models of Alzheimer’s disease. Neurobiology of Disease. 2015, 74:144-57.
  3. Mahul-Mellier AL, Fauvet B, Gysbers A, Dikiy I, Oueslati A, Georgeon S, Lamontanara AJ, Bisquertt A, Eliezer D, Masliah E, Halliday G, Hantschel O, Lashuel HA*. c-Abl phosphorylates a-synuclein and regulates its degradation: implications for a-syn clearance and contribution to the pathogenesis of Parkinson’s disease. Human Molecular Genetics. 2014, 23(11): 2858-79.
  4. Oueslati A, Schneider BL, Aebischer P, and Lashuel HA*. PLK2 regulates selective autophagic clearance of a-synuclein and suppresses its toxicity. Proceedings of the National Academy of Sciences. 2013, 110(41):E3945-54.
  5. Oueslati A, Paleologou KE, Schneider BL, Aebischer P, Lashuel HA*. Mimicking phosphorylation at Serin87 inhibits the aggregation of human alpha-synuclein and protects against its toxicity in a rat model of Parkinson’s disease. Journal of Neuroscience. 2012, 1;32(5):1536-44.
  6. Di Giovanni S, Eleuteri SC, Paeologou KE, Zweckstetter M, Carrupt PA, Lashuel HA*. Entacapone and Tolcapone, two catechol‑O‑methyltransferase inhibitors, block fibril formation of a-syn and Aβ and protect against amyloid induced toxicity. Journal of Biological Chemistry. 2010, 285(20):14941-54.
  7. Paleologou KE, Oueslati A, Kim HY, Lamberto GR, Rospigliosi CC, Schmid A, Chiappe D, Moniatte M, Eliezer D, Zweckstetter M, Masliah E, Lashuel HA*. Phosphorylation at S87 is enhanced in synucleinopathies, inhibits alpha-synuclein oligomerization, and influences synuclein-membrane interactions. Journal of Neuroscience. 2010, 3;30(9):3184-98.
  8. Arimon M., Grimminger V., Sanz F, Lashuel HA*. Hsp104 targets multiple intermediates on the amyloid pathway and suppresses the seeding capacity of fibrils and protofibrils of Aβ. Journal [MA1] of Molecular Biology. 2008, 384(5):1157-1173.
Protein Engineering Technologies Related to Parkinson’s Disease
  1. Dikiy I, Fauvet B, Jovičić A, Mahul-Mellier A, Desorby C, El-Turk F, Gitler AD, Lashuel HA*, Eliezer D*. Semisynthetic and in vitro phosphorylation of alpha-synuclein at Y39 promotes functional partly-helical membrane-bound states resembling those induced by PD mutations. ACS Chem Biol. 2016, 11(9):2428-37.
  2. Fauvet B and Lashuel HA*. Semisynthesis and enzymatic preparation of post-translationally modified α-Synuclein. Methods in Molecular Biology. 2016, 1345:3-20.
  3. Fauvet B, Butterfield SM, Fuks J, Brik A, and Lashuel HA*. One-pot total chemical synthesis of alpha-synulein. Chem Commu. 2013, 49 (81), 9254 – 9256.
  4. Haj-Yahia M, Fauvet B, Herman-Badhinsky Y, Hejjaoui M, Bavikar SN, Vedhanarayanan K, Ciechanover A*, Lashuel HA* and Brik A*. Synthetic polyubiquitin alpha-synuclein reveals important insights into the roles of the ubiquitin chain in regulating its pathophysiology., Proceedings of the National Academy of Sciences. 2013, 110(44):17726-31
  5. Hejjaoui M, Butterfield S, Fauvet B, Vercryusse F, Cun J, Dikiy I, Prudent M, Olschewski D, Zhang Y, Eliezer D, Lashuel HA*.  Chemical Biology of α-synuclein: Elucidating the role of C-terminal post-translational modifications using protein semisynthetic strategies: Phosphorylation at Tyrosine 125. Journal of the American Chemical Society. 2012. 21;134(11):5196-210.
  6. Fauvet B, Fares BM, Samuel F, Kikiy I, Tandon A, Eliezer D, Lashuel HA*. Characterization of semisynthetic and natural N-terminal acetylated α-synuclein in vitro and in intact cells: Iimplications for a-synuclein aggregation and cellular properties. Journal of Biological Chemistry. 2012, 17;287(34):28243-62.
  7. Hejjaoui H, Haj-Yahya M, Kumar KS, Brik A*, Lashuel HA*. Towards elucidating the role of ubiquitination in the pathogenesis of Parkinson’s disease using semisynthetic ubquitinated α-synuclein. Angewandte Chem Int Ed. 2011, 10;50(2):405-9.
Protein Engineering Technologies Related to Alzheimer’s Disease
  1. Haj-Yahya M and Lashuel HA*. Protein semisynthesis provides access to Tau disease-associated post-translational modifications (PTMs) and paves the way to deciphering the Tau PTM code in health and disease states. Journal of the American Chemical Society (JACS). 2018, I Apr 23. doi: 10.1021/jacs.8b02668.
  2. Ait-Bouziad N, Lv G, Mahul-Mellier AL, Xiao S, Zorludemir G, Eliezer D, Walz Tand Lashuel HA*. Discovery and Characterization of Novel Stable Tau Oligomeric Complexes: Implications for the Role of Tau/Phospholipid Interactions in Regulating its Functions in Health and Disease. Nature Communications. 2017, 8, 1, 1678, 2017.
  3. Adamcik J, Sánchez-Ferrer A, Ait-Bouziad N, Reynolds NP, Lashuel HA*, Mezzenga R*. Microtubule-Binding R3 Fragment from Tau Self-Assembles into Giant Multistranded Amyloid Ribbons. Angewandte Chem. Int. Ed. 2016, 11;55(2):618-22.
  4. Jan A, Hartley DM and Lashuel HA*. Preparation and characterization of toxic Aβ intermediates for structural and functional studies in Alzheimer’s disease research. Nature Protocols. 2010;5(6):1186-209.  
  5. Lashuel HA*, Hartley D, Petre B, Wall, Simon M, Walz T, Lansbury PT. Mixtures of wild-type and a pathogenic (E22G) form of ABeta40 in vitro accumulate protofibrils, including amyloid pores. Journal of Molecular Biology. 2003, 332, 795-808.
  6. Lashuel HA*, Petre B, Wall, Simon M, Nowak RJ, Walz T, Lansbury PT. -Synuclein, Especially the Parkinson’s Disease-Associated Mutants, Form Pore-like Annular and Tubular Protofibrils.  J. Mol. Biol. 2002. 322, 5, 1089-1102
Protein Engineering Technologies Related to Huntington’s Disease
  1. Reif A, Chiki A, Ricci J, and Lashuel HA*. Generation of native, untagged Huntingtin Exon1 monomers and fibrils using a SUMO fusion strategy. Journal of Visualized Experiments. 2018, 136, doi: 10.3791/5706.
  2. DeGuire SM, Ruggeri SM,Fares MF,Cendrowska U,Dietler G,and Lashuel HA*. Phosphorylation at S13 and/or S16 strongly inhibits the aggregation of mutant Httex1, regulates its helical conformation and prompts the internalization and nuclear targeting of preformed Httex1aggregates. Journal of Biological Chemistry. 2018, 293(48):18540-18558.
  3. Warner J, Ruff K, Tan P, Lemke E, Pappu R* and Lashuel HA*. Monomeric huntingtin exon 1 has similar overall structural features for wild type and pathological polyglutamine lengths. Journal of the American Chemical Society, 2017, 139(41):14456-14469.
  4. Chiki A.,DeGuire SM., Ruggeri SF.,Cendrowska U.,Ansaloni A.,Wang Z.,  Sanfelice D.,Burai R.,Vieweg S.,Pastore A.,Dietler G., and Lashuel HA*. Mutant Exon1 huntingtin aggregation is regulated by T3 phosphorylation-induced structural changes and cross-talk between T3 phosphorylation and acetylation at K6. Angewandte Chem. Int. Ed. 2017, 56(19): 5202-5207.
  5. Ansaloni A, Wang ZM, Jeong JS, Ruggeri FS, Dietler G, Lashuel HA*. One-pot semisynthesis of Exon1 of the Huntingtin protein: new tools for elucidating the role of post-translational modifications in the pathogenesis of Huntington’s disease. Angewandte Chem Int. Ed. Engl. 2014, 10;53(7):1928-33.
Biomarker Discovery for Parkinson’s and Huntingtin’s Disease
  1. Cariulo C, Azzollini L, Verani M, Martufi P, Chiki A, Deguire SM, Cherubini M, Gines S, Marsh LJ, Lavery D, Doherty E, Conforti P, Cattaneo E, Santimone J, Squitieri F, Lashuel HA*, Petricca L*, and Caricasole A*. Phosphorylation of huntingtin at residue T3 is decreased in Huntington’s disease and modulates mutant huntingtin protein conformation, Proceedings of the National Academy of Sciences. 2017, 114(50): E10809-E10818.
  2. Mollenhauer B, Batrla B, El-Agnaf O, Galasko DR, Lashuel HA, Merchant KM, Shaw LM, Selkoe DJ, Umek R, Vanderstichele H, Zetterberg H, Zhang J, Caspell-Garcia C, Coffey C, Hutten SJ, Frasier M, Taylor P for the Investigating Synuclein Consortium of the Michael J. Fox Foundation for Parkinson’s Research. A user’s guide for α-synuclein biomarker studies in biological fluids: Peri-analytical considerations. Journal of Movement Disorder. 2017, 32(8):1117-1130.
  3. Schmid A, Fauvet B, Moniatte M, and Lashuel HA*. Alpha-synuclein post-translational modifications as potential biomarkers for Parkinson’s disease and other synucleinopathies., Molecular and Cellular Proteomics. 2013, 12(12):3543-58.
  4. Schmid A, Fauvet B, Moniatte M, and Lashuel HA*. Alpha-synuclein post-translational modifications as potential biomarkers for Parkinson’s disease and other synucleinopathies., Molecular and Cellular Proteomics. 2013, 12(12):3543-58.
Elucidating Mechanisms Underlying Alzheimer’s, Parkinson’s and Huntington’s Disease
  1. El Turk F, De Genst E, Guilliams T, Fauvet B, Hejjaoui M, Vendruscolo M*, Lashuel HA*, Dobson CM*. “Exploring the role of post-translational modifications in regulating α-synuclein interactions by studying the effects of phosphorylation on nanobody binding”. Protein Science. 2018, (7):1262-1274.
  2. Mbefo MK, Fares MB, Paleologou K, Oueslati A, Yin G, Tenreiro S, Pinto M, Outeiro T, Zweckstetter M, Masliah E, Lashuel HA*. Parkinson Disease Mutant E46K Enhances α-Synuclein Phosphorylation in Mammalian Cell Lines, in Yeast, and in Vivo. Journal of Biological Chemistry. 2015 Apr 10;290(15):9412-27.
  3. Droste P, Frenzel A, Steinwand M, Pelat T, Thullier P, Hust M, Lashuel HA*, Dübel S*. Structural differences of Amyloid-b fibrils revealed by antibodies from phage display. BMC Biotechnology. 2015;15(1):57. doi: 10.1186/s12896-015-0146-8.
  4. Fares MB, Ait-Bouziad N, Dikiy I, Mbefo MK, Jovičić A, Kiely A, Holton JL, Lee SJ, Gitler AD, Eliezer D, Lashuel HA*. The novel Parkinson’s disease linked mutation G51D attenuates in vitro aggregation and membrane binding of α-synuclein, and enhances its secretion and nuclear localization in cells. Human Molecular Genetics. 2014, 23(17):4491-509.
  5. Jeong JS, Ansaloni A, Mezzenga R, Lashuel HA*, and Dietler G*. Novel mechanistic insight into the molecular basis of amyloid polymorphism and secondary nucleation during amyloid formation. Journal of Molecular Biology. 2013, 425(10):1765-81.
  6. Wang Z and Lashuel HA*. Discovery of a novel aggregation domain in the Huntingtin Protein: Implications for the mechanisms of Htt aggregation and toxicity. 2013, Angewandte Chem. Int. Ed. 2013 Jan 7;52(2):562-7.
  7. Fauvet B., Mebfo MK, Fares BM, Desobry C, Michael S, Ardah MT, Tsika E, Coune P, Eliezer D, Moore DJ, Schneider B, Aebischer P., El-agnaf OM, Masliah E, and Lashuel HA*. Alpha-synuclein in the central nervous system, in mammalian cells, and produced by E. coli exists predominantly as a disorderd monomer. Journal of Biological Chemistry. 2012, 287, 15345-15364
  8. Jan A and Lashuel HA*. Biophysical Approaches for Establishing the Links between Aβ aggregation and toxicity. Methods in Molecular Biology. 2012, 849, 227-43
  9. Mbefo MK, Paleologou KE, Boucharaba A, Oueslati A, Olschewski D, Schell H, Fournier M, Zweckstetter M., Kahle PJ, Masliah E Hirling H, Lashuel HA*. Phosphorylation of synucleins (α, β and g) by members of the Polo Like family of Kinases, PLKs 1-4. Journal of Biological Chemistry. 2010, 285(4):2807-22.
  10. Oueslati A, Fournier M, and Lashuel HA*. Role of post-translational modifications in modulating α-synuclein structure, aggregation and toxicity: implications for Parkinson’s disease pathogenesis and therapies. Progress in Brain Research. 2010;183C:115-145.
  11. Jan A, Goekce Ol, Luthi-Carter R, and Lashuel HA*. The ratio of monomeric/ aggregatedforms of Ab (40&42) is an important determinant of Ab aggregation and fibrillogenesis in Alzheimer’s diseases. Journal of Biological Chemistry. 2008, 283(42):28176-89.