Search Results - "Francesco Ruggeri"

Different soluble aggregates of Aβ42 can give rise to cellular toxicity through different mechanisms by De, Suman, Wirthensohn, David C., Flagmeier, Patrick, Hughes, Craig, Aprile, Francesco A., Ruggeri, Francesco S., Whiten, Daniel R., Emin, Derya, Xia, Zengjie, Varela, Juan A., Sormanni, Pietro, Kundel, Franziska, Knowles, Tuomas P. J., Dobson, Christopher M., Bryant, Clare, Vendruscolo, Michele, Klenerman, David

“…Protein aggregation is a complex process resulting in the formation of heterogeneous mixtures of aggregate populations that are closely linked to…”
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AFM-Based Single Molecule Techniques: Unraveling the Amyloid Pathogenic Species by Ruggeri, Francesco Simone, Habchi, Johnny, Cerreta, Andrea, Dietler, Giovanni

“…A wide class of human diseases and neurodegenerative disorders, such as Alzheimer's disease, is due to the failure of a specific peptide or protein to keep its…”
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Small soluble α-synuclein aggregates are the toxic species in Parkinson’s disease by Emin, Derya, Zhang, Yu P., Lobanova, Evgeniia, Miller, Alyssa, Li, Xuecong, Xia, Zengjie, Dakin, Helen, Sideris, Dimitrios I., Lam, Jeff Y. L., Ranasinghe, Rohan T., Kouli, Antonina, Zhao, Yanyan, De, Suman, Knowles, Tuomas P. J., Vendruscolo, Michele, Ruggeri, Francesco S., Aigbirhio, Franklin I., Williams-Gray, Caroline H., Klenerman, David

“…Soluble α-synuclein aggregates varying in size, structure, and morphology have been closely linked to neuronal death in Parkinson’s disease. However, the…”
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Identification of Oxidative Stress in Red Blood Cells with Nanoscale Chemical Resolution by Infrared Nanospectroscopy by Ruggeri, Francesco S, Marcott, Curtis, Dinarelli, Simone, Longo, Giovanni, Girasole, Marco, Dietler, Giovanni, Knowles, Tuomas P J

“…During their lifespan, Red blood cells (RBC), due to their inability to self-replicate, undergo an ageing degradation phenomenon. This pathway, both in vitro…”
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Silk micrococoons for protein stabilisation and molecular encapsulation by Shimanovich, Ulyana, Ruggeri, Francesco S., De Genst, Erwin, Adamcik, Jozef, Barros, Teresa P., Porter, David, Müller, Thomas, Mezzenga, Raffaele, Dobson, Christopher M., Vollrath, Fritz, Holland, Chris, Knowles, Tuomas P. J.

“…Naturally spun silks generate fibres with unique properties, including strength, elasticity and biocompatibility. Here we describe a microfluidics-based…”
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N-terminal Huntingtin (Htt) phosphorylation is a molecular switch regulating Htt aggregation, helical conformation, internalization, and nuclear targeting by DeGuire, Sean M., Ruggeri, Francesco S., Fares, Mohamed-Bilal, Chiki, Anass, Cendrowska, Urszula, Dietler, Giovanni, Lashuel, Hilal A.

“…Huntington’s disease is a fatal neurodegenerative disorder resulting from a CAG repeat expansion in the first exon of the gene encoding the Huntingtin protein…”
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Nanoplasmonic mid-infrared biosensor for in vitro protein secondary structure detection by Etezadi, Dordaneh, Warner IV, John B, Ruggeri, Francesco S, Dietler, Giovanni, Lashuel, Hilal A, Altug, Hatice

“…Plasmonic nanoantennas offer new applications in mid-infrared (mid-IR) absorption spectroscopy with ultrasensitive detection of structural signatures of…”
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Trodusquemine enhances Aβ 42 aggregation but suppresses its toxicity by displacing oligomers from cell membranes by Limbocker, Ryan, Chia, Sean, Ruggeri, Francesco S, Perni, Michele, Cascella, Roberta, Heller, Gabriella T, Meisl, Georg, Mannini, Benedetta, Habchi, Johnny, Michaels, Thomas C T, Challa, Pavan K, Ahn, Minkoo, Casford, Samuel T, Fernando, Nilumi, Xu, Catherine K, Kloss, Nina D, Cohen, Samuel I A, Kumita, Janet R, Cecchi, Cristina, Zasloff, Michael, Linse, Sara, Knowles, Tuomas P J, Chiti, Fabrizio, Vendruscolo, Michele, Dobson, Christopher M

“…Transient oligomeric species formed during the aggregation process of the 42-residue form of the amyloid-β peptide (Aβ ) are key pathogenic agents in…”
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Measurement of intrinsic properties of amyloid fibrils by the peak force QNM method by Adamcik, Jozef, Lara, Cecile, Usov, Ivan, Jeong, Jae Sun, Ruggeri, Francesco S, Dietler, Giovanni, Lashuel, Hilal A, Hamley, Ian W, Mezzenga, Raffaele

“…We report the investigation of the mechanical properties of different types of amyloid fibrils by the peak force quantitative nanomechanical (PF-QNM)…”
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Rational design of a conformation-specific antibody for the quantification of Aβ oligomers by Aprile, Francesco A., Sormanni, Pietro, Podpolny, Marina, Chhangur, Shianne, Needham, Lisa-Maria, Ruggeri, Francesco S., Perni, Michele, Limbocker, Ryan, Heller, Gabriella T., Sneideris, Tomas, Scheidt, Tom, Mannini, Benedetta, Habchi, Johnny, Lee, Steven F., Salinas, Patricia C., Knowles, Tuomas P. J., Dobson, Christopher M., Vendruscolo, Michele

“…Protein misfolding and aggregation is the hallmark of numerous human disorders, including Alzheimer’s disease. This process involves the formation of transient…”
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Imaging protein aggregates in the serum and cerebrospinal fluid in Parkinson's disease by Lobanova, Evgeniia, Whiten, Daniel, Ruggeri, Francesco S, Taylor, Christopher G, Kouli, Antonina, Xia, Zengjie, Emin, Derya, Zhang, Yu P, Lam, Jeff Y L, Williams-Gray, Caroline H, Klenerman, David

“…Aggregation of α-synuclein plays a key role in the development of Parkinson's disease. Soluble aggregates are present not only within human brain but also the…”
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Ultrathin Polydopamine Films with Phospholipid Nanodiscs Containing a Glycophorin A Domain by Marchesi D'Alvise, Tommaso, Harvey, Sean, Hueske, Lisa, Szelwicka, Jolanta, Veith, Lothar, Knowles, Tuomas P. J., Kubiczek, Dennis, Flaig, Carolin, Port, Fabian, Gottschalk, Kay‐E., Rosenau, Frank, Graczykowski, Bartlomiej, Fytas, George, Ruggeri, Francesco S., Wunderlich, Katrin, Weil, Tanja

“…Cellular membranes have long served as an inspiration for nanomaterial research. The preparation of ultrathin polydopamine (PDA) films with integrated protein…”
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The Nt17 Domain and its Helical Conformation Regulate the Aggregation, Cellular Properties and Neurotoxicity of Mutant Huntingtin Exon 1 by Vieweg, Sophie, Mahul-Mellier, Anne-Laure, Ruggeri, Francesco S., Riguet, Nathan, DeGuire, Sean M., Chiki, Anass, Cendrowska, Urszula, Dietler, Giovanni, Lashuel, Hilal A.

“…[Display omitted] •The Nt17 and polyQ domains synergistically promote Httex1 aggregation.•The Nt17 domain is a key determinant of the lateral association and…”
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Molecular determinants of the interaction of EGCG with ordered and disordered proteins by Fusco, Giuliana, Sanz‐Hernandez, Maximo, Ruggeri, Francesco S., Vendruscolo, Michele, Dobson, Christopher M., De Simone, Alfonso

“…The aggregation process of peptides and proteins is of great relevance as it is associated with a wide range of highly debilitating disorders, including…”
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Effects of sedimentation, microgravity, hydrodynamic mixing and air-water interface on α-synuclein amyloid formation by Zhou, Jiangtao, Ruggeri, Francesco S, Zimmermann, Manuela R, Meisl, Georg, Longo, Giovanni, Sekatskii, Sergey K, Knowles, Tuomas P. J, Dietler, Giovanni

“…The formation of amyloid fibrils is a characterizing feature of a range of protein misfolding diseases, including Parkinson's disease. The propensity of native…”
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Mutant Exon1 Huntingtin Aggregation is Regulated by T3 Phosphorylation‐Induced Structural Changes and Crosstalk between T3 Phosphorylation and Acetylation at K6 by Chiki, Anass, DeGuire, Sean M., Ruggeri, Francesco S., Sanfelice, Domenico, Ansaloni, Annalisa, Wang, Zhe‐Ming, Cendrowska, Urszula, Burai, Ritwik, Vieweg, Sophie, Pastore, Annalisa, Dietler, Giovanni, Lashuel, Hilal A.

“…Herein, we used protein semisynthesis to investigate, for the first time, the effect of lysine acetylation and phosphorylation, as well as the crosstalk…”
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Supramolecular Peptide Nanofibrils with Optimized Sequences and Molecular Structures for Efficient Retroviral Transduction by Sieste, Stefanie, Mack, Thomas, Lump, Edina, Hayn, Manuel, Schütz, Desiree, Röcker, Annika, Meier, Christoph, Kaygisiz, Kübra, Kirchhoff, Frank, Knowles, Tuomas P. J., Ruggeri, Francesco S., Synatschke, Christopher V., Münch, Jan, Weil, Tanja

“…Amyloid‐like peptide nanofibrils (PNFs) are abundant in nature providing rich bioactivities and playing both functional and pathological roles. The structural…”
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Environmental Control of Amyloid Polymorphism by Modulation of Hydrodynamic Stress by Zhou, Jiangtao, Venturelli, Leonardo, Keiser, Ludovic, Sekatskii, Sergey K, Gallaire, François, Kasas, Sandor, Longo, Giovanni, Knowles, Tuomas P. J, Ruggeri, Francesco S, Dietler, Giovanni

“…The phenomenon of amyloid polymorphism is a key feature of protein aggregation. Unravelling this phenomenon is of great significance for understanding the…”
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Soluble aggregates present in cerebrospinal fluid change in size and mechanism of toxicity during Alzheimer's disease progression by De, Suman, Whiten, Daniel R, Ruggeri, Francesco S, Hughes, Craig, Rodrigues, Margarida, Sideris, Dimitrios I, Taylor, Christopher G, Aprile, Francesco A, Muyldermans, Serge, Knowles, Tuomas P J, Vendruscolo, Michele, Bryant, Clare, Blennow, Kaj, Skoog, Ingmar, Kern, Silke, Zetterberg, Henrik, Klenerman, David

“…Soluble aggregates of amyloid-β (Aβ) have been associated with neuronal and synaptic loss in Alzheimer's disease (AD). However, despite significant recent…”
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Sequence‐Optimized Peptide Nanofibers as Growth Stimulators for Regeneration of Peripheral Neurons by Schilling, Corinna, Mack, Thomas, Lickfett, Selene, Sieste, Stefanie, Ruggeri, Francesco S., Sneideris, Tomas, Dutta, Arghya, Bereau, Tristan, Naraghi, Ramin, Sinske, Daniela, Knowles, Tuomas P. J., Synatschke, Christopher V., Weil, Tanja, Knöll, Bernd

“…There is an urgent need for biomaterials that support tissue healing, particularly neuronal regeneration. In a medium throughput screen novel self‐assembling…”
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