Publications on Therapeutic Strategies for Neurodegenerative Diseases
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.
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.
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.
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.
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.
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.
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.
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.