Search Results - "Mossuto, Maria F."

A pH-Regulated Quality Control Cycle for Surveillance of Secretory Protein Assembly by Vavassori, Stefano, Cortini, Margherita, Masui, Shoji, Sannino, Sara, Anelli, Tiziana, Caserta, Imma R., Fagioli, Claudio, Mossuto, Maria F., Fornili, Arianna, van Anken, Eelco, Degano, Massimo, Inaba, Kenji, Sitia, Roberto

“…To warrant the quality of the secretory proteome, stringent control systems operate at the endoplasmic reticulum (ER)-Golgi interface, preventing the release…”
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Metastability of Native Proteins and the Phenomenon of Amyloid Formation by Baldwin, Andrew J, Knowles, Tuomas P. J, Tartaglia, Gian Gaetano, Fitzpatrick, Anthony W, Devlin, Glyn L, Shammas, Sarah Lucy, Waudby, Christopher A, Mossuto, Maria F, Meehan, Sarah, Gras, Sally L, Christodoulou, John, Anthony-Cahill, Spencer J, Barker, Paul D, Vendruscolo, Michele, Dobson, Christopher M

“…An experimental determination of the thermodynamic stabilities of a series of amyloid fibrils reveals that this structural form is likely to be the most stable…”
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The Non-Core Regions of Human Lysozyme Amyloid Fibrils Influence Cytotoxicity by Mossuto, Maria F., Dhulesia, Anne, Devlin, Glyn, Frare, Erica, Kumita, Janet R., de Laureto, Patrizia Polverino, Dumoulin, Mireille, Fontana, Angelo, Dobson, Christopher M., Salvatella, Xavier

“…Identifying the cause of the cytotoxicity of species populated during amyloid formation is crucial to understand the molecular basis of protein deposition…”
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Population of Nonnative States of Lysozyme Variants Drives Amyloid Fibril Formation by Buell, Alexander K, Dhulesia, Anne, Mossuto, Maria F, Cremades, Nunilo, Kumita, Janet R, Dumoulin, Mireille, Welland, Mark E, Knowles, Tuomas P. J, Salvatella, Xavier, Dobson, Christopher M

“…The propensity of protein molecules to self-assemble into highly ordered, fibrillar aggregates lies at the heart of understanding many disorders ranging from…”
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Characterization of Oligomeric Species on the Aggregation Pathway of Human Lysozyme by Frare, Erica, Mossuto, Maria F., de Laureto, Patrizia Polverino, Tolin, Serena, Menzer, Linda, Dumoulin, Mireille, Dobson, Christopher M., Fontana, Angelo

“…The aggregation process of wild-type human lysozyme at pH 3.0 and 60 °C has been analyzed by characterizing a series of distinct species formed on the…”
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Identification of the Core Structure of Lysozyme Amyloid Fibrils by Proteolysis by Frare, Erica, Mossuto, Maria F., Polverino de Laureto, Patrizia, Dumoulin, Mireille, Dobson, Christopher M., Fontana, Angelo

“…Human lysozyme variants form amyloid fibrils in individuals suffering from a familial non-neuropathic systemic amyloidosis. In vitro, wild-type human and hen…”
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Disulfide Bonds Reduce the Toxicity of the Amyloid Fibrils Formed by an Extracellular Protein by Mossuto, Maria F., Bolognesi, Benedetta, Guixer, Bernat, Dhulesia, Anne, Agostini, Federico, Kumita, Janet R., Tartaglia, Gian G., Dumoulin, Mireille, Dobson, Christopher M., Salvatella, Xavier

“…In a stable condition: Disulfide bonds stabilize folded proteins primarily by decreasing the entropic cost of folding. Such cross‐links also reduce toxic…”
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Local Cooperativity in an Amyloidogenic State of Human Lysozyme Observed at Atomic Resolution by Dhulesia, Anne, Cremades, Nunilo, Kumita, Janet R, Hsu, Shang-Te Danny, Mossuto, Maria F, Dumoulin, Mireille, Nietlispach, Daniel, Akke, Mikael, Salvatella, Xavier, Dobson, Christopher M

“…The partial unfolding of human lysozyme underlies its conversion from the soluble state into amyloid fibrils observed in a fatal hereditary form of systemic…”
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Single Point Mutations Induce a Switch in the Molecular Mechanism of the Aggregation of the Alzheimer’s Disease Associated Aβ42 Peptide by Bolognesi, Benedetta, Cohen, Samuel I. A, Aran Terol, Pablo, Esbjörner, Elin K, Giorgetti, Sofia, Mossuto, Maria F, Natalello, Antonino, Brorsson, Ann-Christin, Knowles, Tuomas P. J, Dobson, Christopher M, Luheshi, Leila M

“…Single point mutations in the Alzheimer’s disease associated Aβ42 peptide are found to alter significantly its neurotoxic properties in vivo and have been…”
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Conformational properties of the aggregation precursor state of HypF-N by Campioni, Silvia, Mossuto, Maria F., Torrassa, Silvia, Calloni, Giulia, de Laureto, Patrizia Polverino, Relini, Annalisa, Fontana, Angelo, Chiti, Fabrizio

“…The conversion of specific proteins or protein fragments into insoluble, ordered fibrillar aggregates is a fundamental process in protein chemistry, biology,…”
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Protein dissection enhances the amyloidogenic properties of α‐lactalbumin by Polverino de Laureto, Patrizia, Frare, Erica, Battaglia, Francesca, Mossuto, Maria F., Uversky, Vladimir N., Fontana, Angelo

“…α‐lactalbumin (LA) in its molten globule (MG) state at low pH forms amyloid fibrils. Here, we have studied the aggregation propensities of LA derivatives…”
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Disulfide Bonds Reduce the Toxicity of the Amyloid Fibrils Formed by an Extracellular Protein by Mossuto, Maria F., Bolognesi, Benedetta, Guixer, Bernat, Dhulesia, Anne, Agostini, Federico, Kumita, Janet R., Tartaglia, Gian G., Dumoulin, Mireille, Dobson, Christopher M., Salvatella, Xavier

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Population of non-native states of lysozyme variants drives amyloid fibril formation by Buell, Alexander K., Dhulesia, Anne, Mossuto, Maria F., Cremades, Nunilo, Kumita, Janet R., Dumoulin, Mireille, Welland, Mark E., Knowles, Tuomas P.J., Salvatella, Xavier, Dobson, Christopher M.

“…The propensity of protein molecules to self-assemble into highly ordered, fibrillar aggregates lies at the heart of the understanding of many disorders such as…”
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Single Point Mutations Induce a Switch in the Molecular Mechanism of the Aggregation of the Alzheimer’s Disease Associated Aβ 42 Peptide by Bolognesi, Benedetta, Cohen, Samuel I. A., Aran Terol, Pablo, Esbjörner, Elin K., Giorgetti, Sofia, Mossuto, Maria F., Natalello, Antonino, Brorsson, Ann-Christin, Knowles, Tuomas P. J., Dobson, Christopher M., Luheshi, Leila M.

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Journal of Molecular Biology by Mossuto, Maria F, Dhulesia, Anne, Devlin, Glyn, Frare, Erica, Kumita, Janet R, Polverino de Laureto, Patrizia, Dumoulin, Mireille, Fontana, Angelo, Dobson, Christopher M, Salvatella, Xavier

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Journal of Molecular Biology by Frare, Erica, Mossuto, Maria F, Polverino de Laureto, Patrizia, Tolin, Serena, Menzer, Linda, Dumoulin, Mireille, Dobson, Christopher M, Fontana, Angelo

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Journal of the American Chemical Society by Zervosen, Astrid, Herman, Raphaël, Kerff, Frédéric, Herman, A, Bouillez, André, Prati, F, Pratt, R. F, Frère, Jean-Marie, Joris, Bernard, Luxen, André, Charlier, Paulette, Sauvage, Eric

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Journal of Molecular Biology by Jacquin, Olivier, Balbeur, Dorothée, Damblon, Christian, Marchot, Pierre, De Pauw, Edwin, Roberts, Gordon C K, Frère, Jean-Marie, Matagne, André

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Journal of Molecular Biology by Frare, Erica, Mossuto, Maria F, Polverino de Laureto, Patrizia, Dumoulin, Mireille, Dobson, Christopher M, Fontana, Angelo

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Disulfide Bonds Reduce the Toxicity of the Amyloid Fibrils Formed by an Extracellular Protein by Mossuto, Maria F., Bolognesi, Benedetta, Guixer, Bernat, Dhulesia, Anne, Agostini, Federico, Kumita, Janet R., Tartaglia, Gian G., Dumoulin, Mireille, Dobson, Christopher M., Salvatella, Xavier

“…In stabilem Zustand: Disulfidbindungen stabilisieren gefaltete Proteine primär dadurch, dass sie die Entropiekosten der Faltung minimieren. Solche Vernetzungen…”
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