Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Claire H. Michel"'
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:
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:
Gabriele S. Kaminski Schierle, Ajay Kumar Mishra, Alan Tunnacliffe, Neil R. Williamson, Claire H. Michel, Meng Lu, Clemens F. Kaminski
Publikováno v:
The Journal of Biological Chemistry
The 42-amino-acid β-amyloid (Aβ42) is a critical causative agent in the pathology of Alzheimer's disease. The hereditary Arctic mutation of Aβ42 (E22G) leads to increased intracellular accumulation of β-amyloid in early-onset Alzheimer's disease.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::831a4dcdfc1c5284009603c5bf32db5c
https://www.repository.cam.ac.uk/handle/1810/292817
https://www.repository.cam.ac.uk/handle/1810/292817
Publikováno v:
Microscopy Research and Technique. 79:677-683
Alzheimer's disease (AD) is the main cause of dementia in the elderly population. Over 30 million people worldwide are living with dementia and AD prevalence is projected to increase dramatically in the next two decades. In terms of neuropathology, A
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::963f1c22ff782fa445030e7738638d52
https://doi.org/10.1002/jemt.22698
https://doi.org/10.1002/jemt.22698
Autor:
Pierre Mahou, Claire H. Michel, Gabriele S. Kaminski Schierle, Alexander K. Buell, Clemens F. Kaminski, Dorothea Pinotsi, Christopher M. Dobson, Romain F. Laine
Publikováno v:
Proceedings of the National Academy of Sciences. 113:3815-3819
New strategies for visualizing self-assembly processes at the nanoscale give deep insights into the molecular origins of disease. An example is the self-assembly of misfolded proteins into amyloid fibrils, which is related to a range of neurodegenera
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b643d1d4cc0ed9b95baa57572f105345
https://doi.org/10.1073/pnas.1516546113
https://doi.org/10.1073/pnas.1516546113
Autor:
Marie C. Lechler, Claire H. Michel, G. S. Kaminski Schierle, Chaolie Huang, Raimund Jung, Chetan Poudel, Clemens F. Kaminski, Della C. David, N. Schlörit, A.D. Stephens, Michele Vendruscolo, Romain F. Laine, Tessa Sinnige, Sara Wagner-Valladolid
Reduced protein homeostasis and increased protein instability is a common feature of aging. Yet it remains unclear whether protein instability is a cause of aging. In neurodegenerative diseases and amyloidoses, specific proteins self-assemble into am
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dd3f0aaba92d0d8b1562dd9e98d11e31
Autor:
Sean Tenant, Evangelia K. Ttofi, Claire H. Michel, David C. Rubinsztein, Matthieu Y. Pasco, Cahir J. O'Kane, Zdenek Berger
Publikováno v:
Human Molecular Genetics. 14:3003-3011
We have previously shown that lithium can protect against the polyglutamine toxicity of the Huntington's disease mutation in cell models. Here, we demonstrate for the first time in vivo that lithium can protect against the toxicity caused by aggregat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1ce5c4310bfff772fd7e2ded53f22984
https://doi.org/10.1093/hmg/ddi331
https://doi.org/10.1093/hmg/ddi331
Publikováno v:
SPIE Proceedings.
The misfolding and self-assembly of intrinsically disordered proteins into insoluble amyloid structures is central to many neurodegenerative diseases such as Alzheimer’s and Parkinson’s Diseases. Optical imaging of this self-assembly process in v
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::01accfda1ca23281b345d2446e2d8fce
https://doi.org/10.1117/12.2062721
https://doi.org/10.1117/12.2062721
Publikováno v:
Alzheimer's & Dementia. 10
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9473fdcb8cd5205aa2abf81c15465377
https://doi.org/10.1016/j.jalz.2014.05.1137
https://doi.org/10.1016/j.jalz.2014.05.1137
Autor:
Carol V. Robinson, David A. Lomas, Didier Belorgey, Elena Miranda, James A. Irving, Joanna Freeke, Benoit D. Roussel, Juan Pérez, Stefan J. Marciniak, Damian C. Crowther, Ugo I. Ekeowa, Claire H. Michel
Neuroserpin is a member of the serine protease inhibitor or serpin superfamily of proteins. It is secreted by neurones and plays an important role in the regulation of tissue plasminogen activator at the synapse. Point mutations in the neuroserpin ge
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e32581922aa3e9fa5f040f80768289bd
http://hdl.handle.net/11573/142281
http://hdl.handle.net/11573/142281