Zobrazeno 1 - 10
of 53
pro vyhledávání: '"Eric W, Hewitt"'
Autor:
Chalmers C. Chau, Christopher M. Maffeo, Aleksei Aksimentiev, Sheena E. Radford, Eric W. Hewitt, Paolo Actis
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-11 (2024)
Abstract Controlled manipulation of cultured cells by delivery of exogenous macromolecules is a cornerstone of experimental biology. Here we describe a platform that uses nanopipettes to deliver defined numbers of macromolecules into cultured cell li
Externí odkaz:
https://doaj.org/article/3608c7ce0c4946648711d04cca233e42
Publikováno v:
Frontiers in Molecular Neuroscience, Vol 13 (2020)
Amyloid plaques are a pathological hallmark of Alzheimer’s disease. The major component of these plaques are highly ordered amyloid fibrils formed by amyloid-β (Aβ) peptides. However, whilst Aβ amyloid fibril assembly has been subjected to detai
Externí odkaz:
https://doaj.org/article/e1bc87a90acc4b29b1f5d1e38c23ca07
Autor:
Theodoros K Karamanos, Matthew P Jackson, Antonio N Calabrese, Sophia C Goodchild, Emma E Cawood, Gary S Thompson, Arnout P Kalverda, Eric W Hewitt, Sheena E Radford
Publikováno v:
eLife, Vol 8 (2019)
Transient oligomers are commonly formed in the early stages of amyloid assembly. Determining the structure(s) of these species and defining their role(s) in assembly is key to devising new routes to control disease. Here, using a combination of chemi
Externí odkaz:
https://doaj.org/article/ae5e6a17dff3440081ba46090b9199cc
Autor:
Fabio Marcuccio, Dimitrios Soulias, Chalmers C. Chau, Sheena E. Radford, Eric W. Hewitt, Paolo Actis, Martin A. Edwards
Solid-state nanopores have been widely employed in the detection of biomolecules, but low signal-to-noise ratios still represent a major obstacle to enable the discrimination of short nucleic acid and protein sequences. The addition of 50% polyethyle
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7784ab8772986340e21159f5d9b67a97
https://doi.org/10.1101/2022.08.17.503612
https://doi.org/10.1101/2022.08.17.503612
Autor:
Fabio Marcuccio, Martin A. Edwards, Chalmers C. Chau, Dimitrios Soulias, Sheena E. Radford, Eric W. Hewitt, Paolo Actis
Nanopore systems have emerged as a leading platform for the analysis of biomolecular complexes with single molecule resolution. However, the analysis of several analytes like short nucleic acids or proteins with nanopores represents a sensitivity cha
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5ca6bd3990017b3711eb805f5f744ae6
https://doi.org/10.1101/2021.11.01.466478
https://doi.org/10.1101/2021.11.01.466478
Autor:
Matthew P. Jackson, Eric W. Hewitt
Publikováno v:
Biomolecules, Vol 7, Iss 4, p 71 (2017)
Amyloids were first identified in association with amyloidoses, human diseases in which proteins and peptides misfold into amyloid fibrils. Subsequent studies have identified an array of functional amyloid fibrils that perform physiological roles in
Externí odkaz:
https://doaj.org/article/491b8be457ec47988646a0b30c8d88b9
Publikováno v:
PLoS ONE, Vol 9, Iss 6, p e98900 (2014)
Natural killer (NK) cell secretory lysosome exocytosis and cytotoxicity are impaired in familial hemophagocytic lymphohistiocytosis type 4 (FHL-4), a disorder caused by mutations in the gene encoding the SNARE protein syntaxin 11. We show that syntax
Externí odkaz:
https://doaj.org/article/d84c2a0f3340464e836f669a068d5f60
Autor:
Sophia C Goodchild, Tania Sheynis, Rebecca Thompson, Kevin W Tipping, Wei-Feng Xue, Neil A Ranson, Paul A Beales, Eric W Hewitt, Sheena E Radford
Publikováno v:
PLoS ONE, Vol 9, Iss 8, p e104492 (2014)
Although the molecular mechanisms underlying the pathology of amyloidoses are not well understood, the interaction between amyloid proteins and cell membranes is thought to play a role in several amyloid diseases. Amyloid fibrils of β2-microglobulin
Externí odkaz:
https://doaj.org/article/e6224361295e4cceb75dc41f1888baa1
Publikováno v:
Frontiers in Molecular Neuroscience
Frontiers in Molecular Neuroscience, Vol 13 (2020)
Frontiers in Molecular Neuroscience, Vol 13 (2020)
Amyloid plaques are a pathological hallmark of Alzheimer’s disease. The major component of these plaques are highly ordered amyloid fibrils formed by amyloid-β (Aβ) peptides. However, whilst Aβ amyloid fibril assembly has been subjected to detai
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::72df7dec583ed3dff2b1c46b206d2a2a
https://doi.org/10.3389/fnmol.2020.609073
https://doi.org/10.3389/fnmol.2020.609073
Publikováno v:
PLoS ONE, Vol 6, Iss 11, p e27353 (2011)
The formation of insoluble amyloid fibrils is associated with an array of devastating human diseases. Dialysis-related amyloidosis (DRA) is a severe complication of hemodialysis that results in the progressive destruction of the bones and joints. Ele
Externí odkaz:
https://doaj.org/article/20b7cc135f9547f29f11979bb39ba3f7