Zobrazeno 1 - 10
of 1 010
pro vyhledávání: '"Christopher M. Dobson"'
Autor:
Matthias M. Schneider, Saurabh Gautam, Therese W. Herling, Ewa Andrzejewska, Georg Krainer, Alyssa M. Miller, Victoria A. Trinkaus, Quentin A. E. Peter, Francesco Simone Ruggeri, Michele Vendruscolo, Andreas Bracher, Christopher M. Dobson, F. Ulrich Hartl, Tuomas P. J. Knowles
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-11 (2021)
Molecular chaperones from the Hsp70 family can break up protein aggregates, including amyloids. Here, the authors utilize microfluidic diffusional sizing to assess the mechanism of α-synuclein (αS) disaggregation by the Hsc70–DnaJB1–Apg2 system
Externí odkaz:
https://doaj.org/article/9d156d4ff127467f8d1a03fe03aed8f5
Publikováno v:
Frontiers in Molecular Biosciences, Vol 9 (2022)
Proteins from hyperthermophilic organisms are evolutionary optimised to adopt functional structures and dynamics under conditions in which their mesophilic homologues are generally inactive or unfolded. Understanding the nature of such adaptation is
Externí odkaz:
https://doaj.org/article/b162aa5a46d046caa6e02caa4425ea8d
Autor:
Michele Perni, Benedetta Mannini, Catherine K. Xu, Janet R. Kumita, Christopher M. Dobson, Fabrizio Chiti, Michele Vendruscolo
Publikováno v:
Scientific Reports, Vol 11, Iss 1, Pp 1-12 (2021)
Abstract Misfolded protein oligomers are increasingly recognized as highly cytotoxic agents in a wide range of human disorders associated with protein aggregation. In this study, we assessed the possible uptake and resulting toxic effects of model pr
Externí odkaz:
https://doaj.org/article/a5a3433026d44b8ebabead4cd9d9b713
Autor:
Priyanka Joshi, Michele Perni, Ryan Limbocker, Benedetta Mannini, Sam Casford, Sean Chia, Johnny Habchi, Johnathan Labbadia, Christopher M. Dobson, Michele Vendruscolo
Publikováno v:
Communications Biology, Vol 4, Iss 1, Pp 1-14 (2021)
Joshi et al. identify two human metabolites, carnosine and kynurenic acid, that rescue a C. elegans model of Alzheimer’s disease by inhibiting the aggregation of the amyloid beta peptide in vivo. They find that these metabolites trigger a cytosolic
Externí odkaz:
https://doaj.org/article/b28a52b5717142fcbc1079229aedf157
Autor:
Roberta Cascella, Serene W. Chen, Alessandra Bigi, José D. Camino, Catherine K. Xu, Christopher M. Dobson, Fabrizio Chiti, Nunilo Cremades, Cristina Cecchi
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-16 (2021)
The self-assembly of α-synuclein (αS) is a pathological feature of Parkinson’s disease. The αS species responsible for neuronal damage are not well characterized. Here, the authors show that αS fibrils release soluble prefibrillar oligomeric sp
Externí odkaz:
https://doaj.org/article/c2f2c92ceab748c787667121d9608d0b
Autor:
Rodrigo Cataldi, Sean Chia, Katarina Pisani, Francesco S. Ruggeri, Catherine K. Xu, Tomas Šneideris, Michele Perni, Sunehera Sarwat, Priyanka Joshi, Janet R. Kumita, Sara Linse, Johnny Habchi, Tuomas P. J. Knowles, Benedetta Mannini, Christopher M. Dobson, Michele Vendruscolo
Publikováno v:
Communications Biology, Vol 4, Iss 1, Pp 1-10 (2021)
Cataldi et al. investigates the impact of the dopamine derivative DOPAL on the Aβ peptide oligomer formation. They report that DOPAL promotes the formation of stable Aβ oligomers that exert toxicity on neuroblastoma cells by increasing cytosolic ca
Externí odkaz:
https://doaj.org/article/4d14647112154fb9bb2c49c0fb14d6b7
Autor:
Roxine Staats, Thomas C. T. Michaels, Patrick Flagmeier, Sean Chia, Robert I. Horne, Johnny Habchi, Sara Linse, Tuomas P. J. Knowles, Christopher M. Dobson, Michele Vendruscolo
Publikováno v:
Communications Chemistry, Vol 3, Iss 1, Pp 1-9 (2020)
Promising treatments for neurogenerative disorders may involve targeting kinetic intermediates, including α-synuclein oligomers. Here a kinetic method for quantifying oligomer populations is used to screen small molecule inhibitors of oligomerisatio
Externí odkaz:
https://doaj.org/article/25cc20ef6fa54796a866e8e34065ca87
Autor:
Prajwal Ciryam, Matthew Antalek, Fernando Cid, Gian Gaetano Tartaglia, Christopher M. Dobson, Anne-Katrin Guettsches, Britta Eggers, Matthias Vorgerd, Katrin Marcus, Rudolf A. Kley, Richard I. Morimoto, Michele Vendruscolo, Conrad C. Weihl
Publikováno v:
Acta Neuropathologica Communications, Vol 7, Iss 1, Pp 1-14 (2019)
Abstract Protein aggregation is a pathological feature of neurodegenerative disorders. We previously demonstrated that protein inclusions in the brain are composed of supersaturated proteins, which are abundant and aggregation-prone, and form a metas
Externí odkaz:
https://doaj.org/article/98b5bb1d9beb43de9d33f052fb29e0d6
Autor:
Urszula Nowicka, Piotr Chroscicki, Karen Stroobants, Maria Sladowska, Michal Turek, Barbara Uszczynska-Ratajczak, Rishika Kundra, Tomasz Goral, Michele Perni, Christopher M Dobson, Michele Vendruscolo, Agnieszka Chacinska
Publikováno v:
eLife, Vol 10 (2021)
Mitochondria are organelles with their own genomes, but they rely on the import of nuclear-encoded proteins that are translated by cytosolic ribosomes. Therefore, it is important to understand whether failures in the mitochondrial uptake of these nuc
Externí odkaz:
https://doaj.org/article/bde42a68f5f14029a3273e815c975f47
Autor:
Ryan Limbocker, Roxine Staats, Sean Chia, Francesco S. Ruggeri, Benedetta Mannini, Catherine K. Xu, Michele Perni, Roberta Cascella, Alessandra Bigi, Liam R. Sasser, Natalie R. Block, Aidan K. Wright, Ryan P. Kreiser, Edward T. Custy, Georg Meisl, Silvia Errico, Johnny Habchi, Patrick Flagmeier, Tadas Kartanas, Jared E. Hollows, Lam T. Nguyen, Kathleen LeForte, Denise Barbut, Janet R. Kumita, Cristina Cecchi, Michael Zasloff, Tuomas P. J. Knowles, Christopher M. Dobson, Fabrizio Chiti, Michele Vendruscolo
Publikováno v:
Frontiers in Neuroscience, Vol 15 (2021)
The aberrant aggregation of proteins is a key molecular event in the development and progression of a wide range of neurodegenerative disorders. We have shown previously that squalamine and trodusquemine, two natural products in the aminosterol class
Externí odkaz:
https://doaj.org/article/dd03b8d056964d40bab6c08d74df6acb