Schechter M, Atias M, Abd Elhadi S, Davidi D, Gitler D and
Sharon R. (2020) α-Synuclein facilitates endocytosis by elevating the steady-state levels of phosphatidylinositol 4,5-bisphosphate. 2020 Dec 25;295(52):18076-18090.
Davidi D, Schechter M, Matatov A, Nathanson L and
Sharon R (2020). α-Synuclein normally translocate to the nucleus to activate retinoic acid- dependent gene transcription. IScience. 6(12):2426-2436.
Schechter M, Grigoletto J, Glickstein H, and
Sharon R (2020). Axonal damage coexists with axonal branching in cortico straiatal neurons of α-Synuclein transgenic mouse brains. Molecular Neurodegeneration. 15(1):24.
Trudler D, Levy-Barazany H, Nash Y, Samuel L,
Sharon R and Frenkel D. (2019). Alpha synuclein deficiency increases CD4+ T-cells pro-inflammatory profile in a Nurr1-dependent manner. J Neurochem. 152(1):61-71.
Abd-ElHadi S, Grigoletto J., Poli M, Arosio P, Arkadir D. and
Sharon R (2019). Blood cells-expressed α-Synuclein differentiates Parkinson's disease and healthy controls. Annals of Clinical Translational Neurology. Dec;6(12):2426-2436
Abd-Elhadi S, Basora M, Vilas D, Tolosa E and
Sharon R (2016). Total α-Synuclein levels in human blood cells, CSF and saliva determined by A Lipid-ELISA. Analytical and Bioanalytical Chemistry. 408(27):7669-7677.
Grigoletto G, Pukaß K, Gamliel A, Komisarov D, Katz-Brull R, Richter-Landsberg C and
Sharon R. Higher levels of myelin phospholipids in brains of neuronal α-Synuclein transgenic mice precede myelin loss. Acta Neuropathol. C. 2017, 5(1):37
De Franceschi G, Fecchio C,
Sharon R, Schapira AH, Proukakis C, Bellotti V and Polverino de Laureto P. Alpha-Synuclein Structural Features Inhibit Harmful Polyunsaturated Fatty Acids Oxidation, Suggesting Roles in Neuroprotection. J Biol Chem. 2017 Apr 28;292(17):6927-6937.
Lasser-Katz E, Simchovitz A, Chiu W-H1, Oertel WH,
Sharon R, Soreq H, Roeper J, and Goldberg JA. Mutant alpha-Synuclein overexpression induces stressless pacemaking in vagal motoneurons at risk in Parkinson's disease. J. Neuroscience. 2016, 37(1):47-57.
Cooper G, Lasser-Katz E, Simchovitz A,
Sharon R, Soreq H, Surmeier DJ, Goldberg JA. Functional segregation of voltage-activated calcium channels in motoneurons of the dorsal motor nucleus of the vagus. J Neurophysiol. 2015, 114(3):1513-20
Abd-Elhadi S, Honig A, Simhi-Haham D, Schechter M, Linetsky E, Ben-Hur T and
Sharon R (2015). Total and proteinase K-resistant α-Synuclein levels in erythrocytes, determined by their ability to bind phospholipids, associate with Parkinson's disease. Sci. Rep. 5:11120.
Zarbiv Y, Simhi-Haham D, Israeli E, Grigoletto J,
Sharon R (2014). Mutations at the first and second KTKEGV repeats of α-Synuclein affect binding to membrane phospholipids and link soluble oligomers with endocytosis, Neurobiol. Dis. 70:90-98.
Yakunin E, Kisos H, Grigoletto J, Kulik WC Wanders RJA, and
Sharon R (2014). α-Synuclein expression inhibits catalase activity in brains of mice modeling Parkinson's disease. Annals of Clinical and Translational Neurology, 1(3):145-59.
Kisos H, Ben-Gedalya T,
Sharon R (2013). The clathrin-dependent localization of dopamine transporter to surface membranes is affected by α-Synuclein. J Mol Neurosci 2013, 2.35; 173/289/9
Kisos H, Pukass K, Ben-Hur T, Richter-Landsberg C, and
Sharon R (2012). Enhanced neuronal α-Synuclein pathology associates with its accumulation in oligodendrocytes in mice modeling α-Synucleinopathies. PLoSOne, 7(10):e46817. 3.53; 11/63/21
Yakunin Y, Loeb V, Kisos H, Biala Y, Yehuda S, Yaari Y, Selkoe DJ, and
Sharon R (2012). α-Synuclein neuropathology is controlled by nuclear hormone receptors and enhanced by docosahexaenoic acid in a mouse model for Parkinson's disease. Brain Pathol. 22(3): 280-94.
Israeli E, Yakunin E, Zarbiv Y, Hacohen-Solovich A, Kisos H, Loeb V, Lichtenstein M, Sabag O, Pikarsky E, Lorberboum-Galski H, and
Sharon R (2011). α-Synuclein expression selectively affects tumorigenesis in mice modeling Parkinson's disease. PLoSOne, 6(5):e19622
Loeb V, Yakunin Y, Saada A,
Sharon R (2010). α-Synuclein expression but not pathology is associated with inhibited complex I activity. J. Biol Chem. 285 (10), pp. 7334–7343.
Yakunin E, Moser A, Loeb V , Saada A, Faust P, Crane DI, Baes M and
Sharon R (2009). α-Synuclein abnormalities in mouse models of Peroxisome Biogenesis Disorders: implications for the involvement of Peroxisomes in Parkinson's disease. J. Neurosci. Res, 88: 866-876.
Israeli E, and
Sharon R (2008). α-Synuclein occurs in vivo in lipid associated oligomers and forms hetero-oligomers with α-Synuclein. J. Neurochem. 108 (2), 465-474.
Ben Gedalya T, Loeb V, Israeli E, Altschuler Y, Selkoe DJ, and
Sharon, R (2009). α-Synuclein promotes clathrin-mediated endocytosis and synaptic vesicle recycling through its interactions with polyunsaturated fatty acids. Traffic, 10(2):218-34.
Haviv Y, Avrahami D, Ovadia H, Ben-Hur T, Gabizon R, and
Sharon R (2008). Induced neuroprotection independently from PrPSc accumulation in a mouse model for prion disease treated with simvastatin. Arch Neurol 65, 762-775.
Assayag K, Yakunin E, Loeb V, Selkoe D J, and
Sharon R (2007). Polyunsaturated fatty acids induce α-Synuclein-Related Pathogenic Changes in Neuronal Cells. Am J Pathol 171, 2000-2011.
Sharon R, Bar-Joseph I, Mirick GE, Serhan CN and Selkoe DJ (2003). Altered fatty acid composition of dopaminergic neurons expressing alpha -synuclein and human brains with α-synucleinopathies. J Biol Chem. 278 (50): 49874-49881.
Sharon R, Bar-Joseph I, Frosch MP, Walsh DM, Hamilton JA and Selkoe DJ (2003). The formation of highly soluble oligomers of α-synuclein is regulated by fatty acids and enhanced in Parkinson's disease. Neuron 37(4): 583-595.
Schlossmacher MG, Frosch MP, Gai WP, Medina M, Shimura H, Ochiishi T,
Sharon R, Hattori NC, Mizono Y, Selkoe DJ and Kosik KS. 2002, Parkin and α-Synuclein interact in normal brain and colocalize in Lewy bodies of Parkinson's disease. Am J Pathol. 160(5): 1655-1667. 5.697;2/68;136.
Sharon R, Goldberg MS, Bar-Josef I, Betensky RA, Shen J and Selkoe DJ (2001). α-Synuclein occurs in lipid-rich high molecular weight complexes, binds fatty acids and shows homology to the fatty acid binding proteins. PNAS 98(16): 9110-911.
