Search Results - "De Franceschi, Giorgia"

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  1. 1

    Global analysis of protein structural changes in complex proteomes by Feng, Yuehan, De Franceschi, Giorgia, Kahraman, Abdullah, Soste, Martin, Melnik, Andre, Boersema, Paul J, de Laureto, Patrizia Polverino, Nikolaev, Yaroslav, Oliveira, Ana Paula, Picotti, Paola

    Published in Nature biotechnology (01-10-2014)
    “…Coupling limited proteolysis and a proteomics workflow enables measurement of both subtle and wholesale protein conformational changes in a eukaryotic…”
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    Journal Article
  2. 2

    α-Synuclein oligomers induced by docosahexaenoic acid affect membrane integrity by Fecchio, Chiara, De Franceschi, Giorgia, Relini, Annalisa, Greggio, Elisa, Dalla Serra, Mauro, Bubacco, Luigi, Polverino de Laureto, Patrizia

    Published in PloS one (29-11-2013)
    “…A key feature of Parkinson disease is the aggregation of α-synuclein and its intracellular deposition in fibrillar form. Increasing evidence suggests that the…”
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    Journal Article
  3. 3

    Covalent α-synuclein dimers: chemico-physical and aggregation properties by Pivato, Micaela, De Franceschi, Giorgia, Tosatto, Laura, Frare, Erica, Kumar, Dhruv, Aioanei, Daniel, Brucale, Marco, Tessari, Isabella, Bisaglia, Marco, Samori, Bruno, de Laureto, Patrizia Polverino, Bubacco, Luigi

    Published in PloS one (13-12-2012)
    “…The aggregation of α-synuclein into amyloid fibrils constitutes a key step in the onset of Parkinson's disease. Amyloid fibrils of α-synuclein are the major…”
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    Journal Article
  4. 4
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    α-Synuclein structural features inhibit harmful polyunsaturated fatty acid oxidation, suggesting roles in neuroprotection by De Franceschi, Giorgia, Fecchio, Chiara, Sharon, Ronit, Schapira, Anthony H.V., Proukakis, Christos, Bellotti, Vittorio, de Laureto, Patrizia Polverino

    Published in The Journal of biological chemistry (28-04-2017)
    “…α-Synuclein (aS) is a protein abundant in presynaptic nerve terminals in Parkinson disease (PD) and is a major component of intracellular Lewy bodies, the…”
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  7. 7

    Structural and Morphological Characterization of Aggregated Species of α-Synuclein Induced by Docosahexaenoic Acid by De Franceschi, Giorgia, Frare, Erica, Pivato, Micaela, Relini, Annalisa, Penco, Amanda, Greggio, Elisa, Bubacco, Luigi, Fontana, Angelo, de Laureto, Patrizia Polverino

    Published in The Journal of biological chemistry (24-06-2011)
    “…The interaction of brain lipids with α-synuclein may play an important role in the pathogenesis of Parkinson disease (PD). Docosahexaenoic acid (DHA) is an…”
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    Journal Article
  8. 8

    The oleic acid complexes of proteolytic fragments of α‐lactalbumin display apoptotic activity by Tolin, Serena, De Franceschi, Giorgia, Spolaore, Barbara, Frare, Erica, Canton, Marcella, Polverino de Laureto, Patrizia, Fontana, Angelo

    Published in The FEBS journal (01-01-2010)
    “…The complexes formed by partially folded human and bovine α‐lactalbumin with oleic acid (OA) have been reported to display selective apoptotic activity against…”
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  9. 9
  10. 10

    Molecular Insights into the Interaction between α-Synuclein and Docosahexaenoic Acid by De Franceschi, Giorgia, Frare, Erica, Bubacco, Luigi, Mammi, Stefano, Fontana, Angelo, de Laureto, Patrizia Polverino

    Published in Journal of molecular biology (20-11-2009)
    “…α-Synuclein (α-syn) is a 140-residue protein of unknown function, involved in several neurodegenerative disorders, such as Parkinson's disease. Recently, the…”
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    Journal Article
  11. 11

    Amyloid Fibril Formation and Disaggregation of Fragment 1-29 of Apomyoglobin: Insights into the Effect of pH on Protein Fibrillogenesis by Picotti, Paola, De Franceschi, Giorgia, Frare, Erica, Spolaore, Barbara, Zambonin, Marcello, Chiti, Fabrizio, de Laureto, Patrizia Polverino, Fontana, Angelo

    Published in Journal of molecular biology (13-04-2007)
    “…The N-terminal fragment 1–29 of horse heart apomyoglobin (apoMb 1–29) is highly prone to form amyloid-like fibrils at low pH. Fibrillogenesis at pH 2.0 occurs…”
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    Journal Article
  12. 12

    Covalent [alpha]-Synuclein Dimers: Chemico-Physical and Aggregation Properties by Pivato, Micaela, De Franceschi, Giorgia, Tosatto, Laura, Frare, Erica, Kumar, Dhruv, Aioanei, Daniel, Brucale, Marco, Tessari, Isabella, Bisaglia, Marco, Samori, Bruno, de Laureto, Patrizia Polverino, Bubacco, Luigi

    Published in PloS one (13-12-2012)
    “…The aggregation of [alpha]-synuclein into amyloid fibrils constitutes a key step in the onset of Parkinson's disease. Amyloid fibrils of [alpha]-synuclein are…”
    Get full text
    Journal Article
  13. 13

    The role of tryptophan in protein fibrillogenesis: relevance of Trp7 and Trp14 to the amyloidogenic properties of myoglobin by Cecchini, Paola, De Franceschi, Giorgia, Frare, Erica, Fontana, Angelo, Polverino de Laureto, Patrizia

    Published in Protein engineering, design and selection (01-04-2012)
    “…In order to understand the role of tryptophan in the mechanisms of fibrils formation, the ability of a series of analogs of the residue 7–18 span of myoglobin…”
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    Journal Article
  14. 14

    The oleic acid complexes of proteolytic fragments of [alpha]-lactalbumin display apoptotic activity by Tolin, Serena, De Franceschi, Giorgia, Spolaore, Barbara, Frare, Erica, Canton, Marcella, Polverino de Laureto, Patrizia, Fontana, Angelo

    Published in The FEBS journal (01-01-2010)
    “…The complexes formed by partially folded human and bovine [alpha]-lactalbumin with oleic acid (OA) have been reported to display selective apoptotic activity…”
    Get full text
    Journal Article
  15. 15

    alpha -Synuclein Oligomers Induced by Docosahexaenoic Acid Affect Membrane Integrity: e82732 by Fecchio, Chiara, Franceschi, Giorgia De, Relini, Annalisa, Greggio, Elisa, Serra, Mauro Dalla, Bubacco, Luigi, Laureto, Patrizia Polverinode

    Published in PloS one (01-11-2013)
    “…A key feature of Parkinson disease is the aggregation of alpha -synuclein and its intracellular deposition in fibrillar form. Increasing evidence suggests that…”
    Get full text
    Journal Article