http://www.cnr.it/ontology/cnr/individuo/prodotto/ID202404
Modulation of alpha-synuclein aggregation by dopamine analogs (Contributo in atti di convegno)
- Type
- Label
- Modulation of alpha-synuclein aggregation by dopamine analogs (Contributo in atti di convegno) (literal)
- Anno
- 2009-01-01T00:00:00+01:00 (literal)
- Alternative label
Giuseppe Legname1,2,#, Diane Latawiec1,2, Fernando Herrera2,3, Alpan Bek4, Michela
Candotti2,3, Federico Benetti1,2, Vincenzo Grillo5, Elvio Carlino5, Marco Lazzarino4,5, Stefano
Gustincich1,2 and Paolo Carloni2,3, (2009)
Modulation of alpha-synuclein aggregation by dopamine analogs
in Microscopy Conference 2009, Graz (A), 30 Aug. Sept 4 2009
(literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Giuseppe Legname1,2,#, Diane Latawiec1,2, Fernando Herrera2,3, Alpan Bek4, Michela
Candotti2,3, Federico Benetti1,2, Vincenzo Grillo5, Elvio Carlino5, Marco Lazzarino4,5, Stefano
Gustincich1,2 and Paolo Carloni2,3, (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#titoloVolume
- Microscopy Conference 2009 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#volumeInCollana
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- 1Department of Neurobiology, 2Italian Institute of Technology (IIT)-SISSA Unit, Via Beirut
2-4, 34014 Trieste, Italy.3Department of Statistical and Biological Physics, Scuola
Internazionale Superiore di Studi Avanzati-International School for Advanced Studies
(SISSA-ISAS), I-34014 Trieste, Italy. 4LANA3DA Scanning Probe BioNanoAnalysis, CBM,
I-34012 Trieste-Italy; 5TASC-INFM-CNR National Laboratory, I-34012 Trieste, Italy. (literal)
- Titolo
- Modulation of alpha-synuclein aggregation by dopamine analogs (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#curatoriVolume
- Abstract
- Parkinson's disease is a fatal neurodegenerative movement disorder, which affects an
estimated four million people worldwide [1]. However, no known cure exists. The action of
dopamine on the aggregation of ?-synuclein (?-syn) is associated with the onset of the
pathogenesis of the disease and recent studies have revealed that dopamine and its analogs
can inhibit aggregation of ?-syn [2-6]. Here, we have used a combined computational and
experimental/microscopical approach to investigate the effect of dopamine mimickers on the
aggregation of ?-syn.
Using computational methods, small molecules were found in the ligand.info database
[7], which are structurally and electrostatically similar to dopamine. Molecular dynamics
simulations showed that binding to ?-syn is much weaker than that of dopamine, which
inhibits fibrillation [8]. Five of the identified molecules were tested in an in vitro fibrillization
assay and analyzed by high-resolution atomic force microscopy (AFM) and
transmission electron microscopy (TEM) (literal)
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