Zobrazeno 1 - 10
of 27
pro vyhledávání: '"Alexander J. Dear"'
Autor:
Catherine K. Xu, Georg Meisl, Ewa A. Andrzejewska, Georg Krainer, Alexander J. Dear, Marta Castellana-Cruz, Soma Turi, Irina A. Edu, Giorgio Vivacqua, Raphaël P. B. Jacquat, William E. Arter, Maria Grazia Spillantini, Michele Vendruscolo, Sara Linse, Tuomas P. J. Knowles
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-11 (2024)
Abstract Oligomeric species arising during the aggregation of α-synuclein are implicated as a major source of toxicity in Parkinson’s disease, and thus a major potential drug target. However, both their mechanism of formation and role in aggregati
Externí odkaz:
https://doaj.org/article/a4d1104eb0184ade8af0b5e5b4fb8983
Autor:
Enrico Zurlo, Pravin Kumar, Georg Meisl, Alexander J Dear, Dipro Mondal, Mireille M A E Claessens, Tuomas P J Knowles, Martina Huber
Publikováno v:
PLoS ONE, Vol 16, Iss 1, p e0245548 (2021)
Knowledge of the mechanisms of assembly of amyloid proteins into aggregates is of central importance in building an understanding of neurodegenerative disease. Given that oligomeric intermediates formed during the aggregation reaction are believed to
Externí odkaz:
https://doaj.org/article/e806670bc9994730b928f0b2e45f01bc
Autor:
Catherine K Xu, Georg Meisl, Ewa Andrzejewska, Georg Krainer, Alexander J Dear, Marta Castellana Cruz, Soma Turi, Raphael Jacquat, William E Arter, Michele Vendruscolo, Sara Linse, Tuomas PJ Knowles
Oligomeric species arising during aggregation of α-synuclein are proposed to be a major source of toxicity in Parkinson’s disease, and thus a major potential drug target. However, their mechanism of formation and role in aggregation are largely un
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::dcc4870555b44e74731ac4a281b09956
https://doi.org/10.1101/2023.05.28.542651
https://doi.org/10.1101/2023.05.28.542651
Autor:
Patrick Flagmeier, Thomas C. T. Michaels, David Klenerman, Xiaoting Yang, Sara Linse, Alexander J. Dear, Suman De, Cecilia Emanuelsson, Christopher M. Dobson, Tuomas P. J. Knowles, Michele Vendruscolo
Publikováno v:
Nature Structural & Molecular Biology. 27:886-891
The formation of amyloid deposits in human tissues is a defining feature of more than 50 medical disorders, including Alzheimer’s disease. Strong genetic and histological evidence links these conditions to the process of protein aggregation, yet it
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5299bb93c6fd9facce1700a55ed3c60d
https://doi.org/10.1038/s41594-020-0471-z
https://doi.org/10.1038/s41594-020-0471-z
Autor:
Si Wu, David Klenerman, Tuomas P. J. Knowles, Georg Meisl, Sarah Perrett, Alexander J. Dear, Christopher M. Dobson, Thomas C. T. Michaels, Sara Linse
Publikováno v:
Proc Natl Acad Sci U S A
The spontaneous assembly of proteins into amyloid fibrils is a phenomenon central to many increasingly common and currently incurable human disorders, including Alzheimer’s and Parkinson’s diseases. Oligomeric species form transiently during this
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::21933ec7208db9d117bb6e60946ad8df
https://doi.org/10.1073/pnas.1922267117
https://doi.org/10.1073/pnas.1922267117
Publikováno v:
The Journal of chemical physics. 155(6)
The self-assembly of peptides and proteins into amyloid fibrils plays a causative role in a wide range of increasingly common and currently incurable diseases. The molecular mechanisms underlying this process have recently been discovered, prompting
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::addc9c162d2026d938e6d3d576541009
https://pubmed.ncbi.nlm.nih.gov/34391352
https://pubmed.ncbi.nlm.nih.gov/34391352
Autor:
Dipro Mondal, Georg Meisl, Tuomas P. J. Knowles, Martina Huber, Mireille Maria Anna Elisabeth Claessens, Enrico Zurlo, Pravin Kumar, Alexander J. Dear
Publikováno v:
PLoS ONE, Vol 16, Iss 1, p e0245548 (2021)
PLoS ONE
PLoS ONE, 16(1):e0245548. Public Library of Science
PLoS ONE, 16(1), e0245548
PLoS ONE
PLoS ONE, 16(1):e0245548. Public Library of Science
PLoS ONE, 16(1), e0245548
Funder: Lindemann Trust Fellowship, English-Speaking Union
Knowledge of the mechanisms of assembly of amyloid proteins into aggregates is of central importance in building an understanding of neurodegenerative disease. Given that oligomeric inte
Knowledge of the mechanisms of assembly of amyloid proteins into aggregates is of central importance in building an understanding of neurodegenerative disease. Given that oligomeric inte
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::93faa4661c9ee3a4948e8d4acd83d473
Autor:
Thomas C. T. Michaels, Alexander J. Dear, Samuel I. A. Cohen, Michele Vendruscolo, Tuomas P. J. Knowles
Publikováno v:
The Journal of Chemical Physics. 156:164904
Protein self-assembly into amyloid fibrils underlies several neurodegenerative conditions, including Alzheimer’s and Parkinson’s diseases. It has become apparent that the small oligomers formed during this process constitute neurotoxic molecular
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a9e2a3d45fc9e38cda72859ff694e0cf
https://doi.org/10.1063/5.0077609
https://doi.org/10.1063/5.0077609
Autor:
Thomas C. T. Michaels, Manuela R Zimmermann, Alexander J. Dear, Sara Linse, Georg Meisl, Tuomas P. J. Knowles
Publikováno v:
The Journal of Chemical Physics
The formation of amyloid fibrils from soluble peptide is a hallmark of many neurodegenerative diseases such as Alzheimer's and Parkinson's diseases. Characterization of the microscopic reaction processes that underlie these phenomena have yielded ins
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9335805af326bdd373199565395fb641
https://pubmed.ncbi.nlm.nih.gov/32007046
https://pubmed.ncbi.nlm.nih.gov/32007046
Autor:
Christopher M. Dobson, Paolo Arosio, Sara Linse, Georg Meisl, Michele Vendruscolo, Katja Bernfur, Andela Saric, Thomas C. T. Michaels, Samo Curk, Alexander J. Dear, Samuel I. A. Cohen, Tuomas P. J. Knowles
Oligomeric aggregates populated during the aggregation of the Aβ42 peptide have been identified as potent cytotoxins linked to Alzheimer’s disease, but the fundamental molecular pathways that control their dynamics have yet to be elucidated. By de
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1737f7f9eceed0d3b7502ccebe355762