Zobrazeno 1 - 10
of 35
pro vyhledávání: '"Amberley D Stephens"'
Autor:
Chaolie Huang, Sara Wagner-Valladolid, Amberley D Stephens, Raimund Jung, Chetan Poudel, Tessa Sinnige, Marie C Lechler, Nicole Schlörit, Meng Lu, Romain F Laine, Claire H Michel, Michele Vendruscolo, Clemens F Kaminski, Gabriele S Kaminski Schierle, Della C David
Publikováno v:
eLife, Vol 8 (2019)
Reduced protein homeostasis leading to increased protein instability is a common molecular feature of aging, but it remains unclear whether this is a cause or consequence of the aging process. In neurodegenerative diseases and other amyloidoses, spec
Externí odkaz:
https://doaj.org/article/d304ea99735c4d8ea67842213713ac7f
Autor:
Amberley D. Stephens, Ana Fernandez Villegas, Chyi Wei Chung, Oliver Vanderpoorten, Dorothea Pinotsi, Ioanna Mela, Edward Ward, Thomas M. McCoy, Robert Cubitt, Alexander F. Routh, Clemens F. Kaminski, Gabriele S. Kaminski Schierle
Publikováno v:
Communications Biology, Vol 6, Iss 1, Pp 1-13 (2023)
Abstract Monomeric alpha-synuclein (aSyn) is a well characterised protein that importantly binds to lipids. aSyn monomers assemble into amyloid fibrils which are localised to lipids and organelles in insoluble structures found in Parkinson’s diseas
Externí odkaz:
https://doaj.org/article/47a85327169c4aaf9bffa1e9000eb692
Autor:
Amberley D. Stephens, Maria Zacharopoulou, Rani Moons, Giuliana Fusco, Neeleema Seetaloo, Anass Chiki, Philippa J. Woodhams, Ioanna Mela, Hilal A. Lashuel, Jonathan J. Phillips, Alfonso De Simone, Frank Sobott, Gabriele S. Kaminski Schierle
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-15 (2020)
In Parkinson’s disease (PD) the monomeric protein alpha-synuclein (aSyn) misfolds and aggregates into insoluble fibrils. Here the authors use NMR measurements and hydrogen–deuterium exchange mass spectrometry and find that the more solvent expose
Externí odkaz:
https://doaj.org/article/06df908e29ff4c6a9479ca48a333babb
Autor:
Janin Lautenschläger, Amberley D. Stephens, Giuliana Fusco, Florian Ströhl, Nathan Curry, Maria Zacharopoulou, Claire H. Michel, Romain Laine, Nadezhda Nespovitaya, Marcus Fantham, Dorothea Pinotsi, Wagner Zago, Paul Fraser, Anurag Tandon, Peter St George-Hyslop, Eric Rees, Jonathan J. Phillips, Alfonso De Simone, Clemens F. Kaminski, Gabriele S. Kaminski Schierle
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-13 (2018)
Alpha-synuclein is associated with neuronal dysfunction in Parkinson’s disease. This study shows that alpha-synuclein interacts with neuronal synaptic vesicles in a calcium-dependent fashion, and this interaction is important for synaptic vesicle c
Externí odkaz:
https://doaj.org/article/70d12e9421354902991a3d31fd154a54
Autor:
Amberley D. Stephens, Johanna Kölbel, Rani Moons, Chyi Wei Chung, Michael T. Ruggiero, Najet Mahmoudi, Talia A. Shmool, Thomas M. McCoy, Daniel Nietlispach, Alexander F. Routh, Frank Sobott, J. Axel Zeitler, Gabriele S. Kaminski Schierle
Publikováno v:
Angewandte Chemie: international edition in English
The solvation shell is essential for the folding and function of proteins, but how it contributes to protein misfolding and aggregation has still to be elucidated. We show that the mobility of solvation shell H2O molecules influences the aggregation
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1b44cbead7c121db4099de2660cf4a4a
Autor:
Giuliana Fusco, Tillmann Pape, Amberley D. Stephens, Pierre Mahou, Ana Rita Costa, Clemens F. Kaminski, Gabriele S. Kaminski Schierle, Michele Vendruscolo, Gianluigi Veglia, Christopher M. Dobson, Alfonso De Simone
Publikováno v:
Nature Communications, Vol 7, Iss 1, Pp 1-12 (2016)
α-synuclein, a protein associated to Parkinson's disease, is involved in synaptic vesicle interaction and assembly. Here, the authors use NMR spectroscopy and super-resolution microscopy to unveil the nature and molecular mechanism of α-synuclein-m
Externí odkaz:
https://doaj.org/article/b6df8c3334454adeab13d8b8305bc6e2
Autor:
Amberley D. Stephens, Ana Fernandez Villegas, Chyi Wei Chung, Oliver Vanderpoorten, Dorothea Pinotsi, Ioanna Mela, Edward Ward, Thomas M. McCoy, Robert Cubitt, Alexander F. Routh, Clemens F. Kaminski, Gabriele S. Kaminski Schierle
Monomeric alpha-synuclein (aSyn) is a well characterised as a lipid binding protein. aSyn is known to form amyloid fibrils which are also localised with lipids and organelles in so called Lewy bodies, insoluble structures found in Parkinson’s disea
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c17e2e8cc3331fbaa56cabb3db6d5efd
https://doi.org/10.1101/2022.10.04.510646
https://doi.org/10.1101/2022.10.04.510646
Autor:
Chyi Wei Chung, Alexandra J. Zhou, Ioanna Mela, Amberley D. Stephens, Akinori Miyashita, Peter H. St George-Hyslop, Clemens F. Kaminski, Tuomas P. J. Knowles, Gabriele S. Kaminski Schierle
SummaryThe molecular mechanisms that connect the formation of aberrant cytoplasmic FUS condensates to biological malfunction are incompletely understood. Here, we develop an approach to determine the intracellular FUS viscosity in live mammalian cell
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::cc1511699333682a1213879b0b976630
https://doi.org/10.1101/2022.10.04.510756
https://doi.org/10.1101/2022.10.04.510756
Autor:
Chyi Wei Chung, Amberley D. Stephens, Tasuku Konno, Edward Ward, Edward Avezov, Clemens F. Kaminski, Ali A. Hassanali, Gabriele S. Kaminski Schierle
Funder: Cambridge Commonwealth, European and International Trust
Funder: Infinitus China Ltd.
The aggregation of Aβ42 is a hallmark of Alzheimer's disease. It is still not known what the biochemical changes are inside a cell which will eve
Funder: Infinitus China Ltd.
The aggregation of Aβ42 is a hallmark of Alzheimer's disease. It is still not known what the biochemical changes are inside a cell which will eve
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e9f2246a481563df40c9c4be1fe067da
https://www.repository.cam.ac.uk/handle/1810/338539
https://www.repository.cam.ac.uk/handle/1810/338539
Autor:
Neeleema Seetaloo, Maria Zacharopoulou, Amberley D. Stephens, Gabriele S. Kaminski Schierle, Jonathan J. Phillips
In Parkinson’s disease and other synucleinopathies, the intrinsically disordered, presynaptic protein alpha-synuclein misfolds and aggregates. We hypothesise that the exposure of alpha-synuclein to different cellular environments, with different ch
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9dec3879704754eb81c72774a2801410
https://doi.org/10.1101/2022.02.11.480045
https://doi.org/10.1101/2022.02.11.480045