Gonzalo R. Lamberto

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alpha-Synuclein (alpha-syn) phosphorylation at serine 129 is characteristic of Parkinson disease (PD) and related alpha-synulceinopathies. However, whether phosphorylation promotes or inhibits alpha-syn aggregation and neurotoxicity in vivo remains unknown. This understanding is critical for elucidating the role of alpha-syn in the pathogenesis of PD and(More)
Increasing evidence suggests that phosphorylation may play an important role in the oligomerization, fibrillogenesis, Lewy body (LB) formation, and neurotoxicity of alpha-synuclein (alpha-syn) in Parkinson disease. Herein we demonstrate that alpha-syn is phosphorylated at S87 in vivo and within LBs. The levels of S87-P are increased in brains of transgenic(More)
From the Laboratory of Molecular Neurobiology and Neuroproteomics, Brain Mind Institute, Ecole Polytechnique Federale de Lausanne, CH-1015 Lausanne, Switzerland, Department of Biochemistry and Program in Structural Biology, Weill Cornell Medical College, New York, New York 10021, Department of NMR-based Structural Biology, Max Planck Institute for(More)
The synuclein family of intrinsically unfolded proteins is composed of three highly homologous members, alpha-synuclein (alphaS), beta-synuclein (betaS) and gamma-synuclein (gammaS), which are linked to neurodegenerative disorders and cancer. alphaS has been studied intensively after its identification as the major protein component of amyloid-like deposits(More)
The aggregation of alpha-synuclein (AS) is a critical step in the etiology of Parkinson's disease (PD) and other neurodegenerative synucleinopathies. Protein-metal interactions play a critical role in AS aggregation and might represent the link between the pathological processes of protein aggregation and oxidative damage. Our previous studies established a(More)
Gonzalo R. Lamberto, Valentina Torres-Monserrat, Carlos W. Bertoncini, Xavier Salvatella, Markus Zweckstetter , Christian Griesinger, and Claudio O. Fernández From the Instituto de Biología Molecular y Celular de Rosario, Consejo Nacional de Investigaciones Científicas y Técnicas, Universidad Nacional de Rosario, Suipacha 531, S2002LRK Rosario, Argentina,(More)
Katerina E. Paleologou,1* Abid Oueslati,1* Gideon Shakked,4 Carla C. Rospigliosi,5 Hai-Young Kim,6 Gonzalo R. Lamberto,7 Claudio O. Fernandez,7 Adrian Schmid,1 Fariba Chegini,8 Wei Ping Gai,8 Diego Chiappe,2 Marc Moniatte,2 Bernard L. Schneider,3 Patrick Aebischer,3 David Eliezer,5 Markus Zweckstetter,6,9 Eliezer Masliah,4 and Hilal A. Lashuel1,2(More)
The fibrillation of amyloidogenic proteins is a critical step in the etiology of neurodegenerative disorders such as Alzheimer and Parkinson diseases. There is major interest in the therapeutic intervention on such aberrant aggregation phenomena, and the utilization of polyaromatic scaffolds has lately received considerable attention. In this regard, the(More)
0022-2836/$ see front matter © 2007 E The synuclein family of intrinsically unfolded proteins is composed of three highly homologous members, α-synuclein (αS), β-synuclein (βS) and γsynuclein (γS), which are linked to neurodegenerative disorders and cancer. αS has been studied intensively after its identification as the major protein component of(More)
The identification of aggregation inhibitors and the investigation of their mechanism of action are fundamental in the quest to mitigate the pathological consequences of amyloid formation. Here, characterization of the structural and mechanistic basis for the antiamyloidogenic effect of phthalocyanine tetrasulfonate (PcTS) on alpha-synuclein (AS) allowed us(More)
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