Zobrazeno 1 - 10
of 23
pro vyhledávání: '"C. Hugh Reynolds"'
Autor:
Bilal Malik, Stuart Kellie, C. Hugh Reynolds, Cathy Fernandes, Richard Killick, Ritchie Williamson, Brian H. Anderton, Richard Wroe, Alessia Usardi
Publikováno v:
Neurochemistry International. 61:321-333
Amyloid-β peptide (Aβ) is the principal component of plaques in the brains of patients with Alzheimer's disease (AD), and the most toxic form of Aβ may be as soluble oligomers. We report here the results of a microarray study of gene expression pr
Autor:
Pascal Derkinderen, Amy M. Pooler, Ritchie Williamson, Brian H. Anderton, Alessia Usardi, Diane P. Hanger, C. Hugh Reynolds, Wendy Noble, Anjan Seereeram
Publikováno v:
FEBS Journal. 278:2927-2937
Recent reports have demonstrated that interactions between the microtubule-associated protein tau and the nonreceptor tyrosine kinase Fyn play a critical role in mediating synaptic toxicity and neuronal loss in response to β-amyloid (Aβ) in models
Autor:
Pascal Derkinderen, Wendy Noble, Charles Duyckaerts, Diane P. Hanger, C. Hugh Reynolds, Timothy M. E. Scales, Ritchie Williamson, Brian H. Anderton, Thibaud Lebouvier
Publikováno v:
Journal of Alzheimer's Disease. 18:1-9
Tau protein is the principal component of the neurofibrillary tangles found in Alzheimer's disease (AD), where it is hyperphosphorylated on serine and threonine residues. It is hypothesized that this hyperphosphorylation contributes to neurodegenerat
Autor:
Brian H. Anderton, C. Hugh Reynolds, Diane P. Hanger, Thibaud Lebouvier, Timothy M. E. Scales, Robert L. Geahlen, Bernard Lardeux, Pascal Derkinderen
Publikováno v:
Biochimica et Biophysica Acta
Aberrant phosphorylation of tau protein on serine and threonine residues has been shown to be critical in neurodegenerative disorders called tauopathies. An increasing amount of data suggest that tyrosine phosphorylation of tau might play an equally
Autor:
Selina Wray, Brian H. Anderton, Malcolm Saxton, Kit-Yi Leung, Anjan Seereeram, Diane P. Hanger, Helen Byers, Malcolm Ward, C. Hugh Reynolds
Publikováno v:
Journal of Biological Chemistry. 282:23645-23654
Tau in Alzheimer disease brain is highly phosphorylated and aggregated into paired helical filaments comprising characteristic neurofibrillary tangles. Here we have analyzed insoluble Tau (PHF-tau) extracted from Alzheimer brain by mass spectrometry
Autor:
Simon Lovestone, Claudie Hooper, C. Hugh Reynolds, Richard Killick, Brian H. Anderton, Ayodeji A. Asuni
Publikováno v:
European Journal of Neuroscience. 24:3387-3392
In the presence of a Wnt signal beta-catenin is spared from proteasomal degradation through a complex mechanism involving GSK3beta, resulting in the transcription of Wnt target genes. In this study we have explored whether GSK3alpha, a related isofor
Autor:
Alessia, Usardi, Amy M, Pooler, Anjan, Seereeram, C Hugh, Reynolds, Pascal, Derkinderen, Brian, Anderton, Diane P, Hanger, Wendy, Noble, Ritchie, Williamson
Publikováno v:
The FEBS journal. 278(16)
Recent reports have demonstrated that interactions between the microtubule-associated protein tau and the nonreceptor tyrosine kinase Fyn play a critical role in mediating synaptic toxicity and neuronal loss in response to β-amyloid (Aβ) in models
Autor:
Timothy M. E. Scales, Caroline Price, C. Hugh Reynolds, Malcolm Ward, Timothy Perera, Ritchie Williamson, Brian H. Anderton, Pascal Derkinderen, Stuart Kellie, Helen Byers, Kit-Yi Leung, Ian N. Bird
Publikováno v:
Molecular Neurodegeneration, Vol 6, Iss 1, p 12 (2011)
Molecular Neurodegeneration
Molecular Neurodegeneration
Background Tau protein is the principal component of the neurofibrillary tangles found in Alzheimer's disease, where it is hyperphosphorylated on serine and threonine residues, and recently phosphotyrosine has been demonstrated. The Src-family kinase
Autor:
C. Hugh Reynolds, Stuart Kellie, Caroline Price, Ian M. Varndell, Brian H. Anderton, Diane P. Hanger, Timothy Perera, Marketa Zvelebil, Alice Yang, Selina Wray, Claire J. Garwood, Paul W. Sheppard
Publikováno v:
The Journal of biological chemistry. 283(26)
The microtubule-associated protein tau can associate with various other proteins in addition to tubulin, including the SH3 domains of Src family tyrosine kinases. Tau is well known to aggregate to form hyperphosphorylated filamentous deposits in seve
Publikováno v:
King's College London
Oxidative stress and free radical damage have been implicated in the neurodegenerative changes characteristic of several neurodegenerative diseases, including Alzheimer's disease. There is experimental evidence that the neurotoxicity of beta-amyloid