Brian M. Austen
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Brian M. Austen has a total of 5 co-authors. Here are the top co-authors by number of shared publications:
Balpreet Matharu
Dept of Basic Medical Sciences, St George's University of London, Cranmer Terrace, London SW17 ORE, United Kingdom
1 shared publication- Eleonora Cerasoli
Biotechnology Department, National Physical Laboratory Teddington, UK
1 shared publication - Franklyn Arron Howe
Neuroscience & Cell Biology Research Institute, School of Health and Medical Sciences, City St George's, University of London, SW17 ORE, UK
1 shared publication - Maxim G. Ryadnov
National Physical Laboratory, Teddington, UK
1 shared publication Nick Spencer
Dept of Basic Medical Sciences, St George's University of London, Cranmer Terrace, London SW17 ORE, United Kingdom
1 shared publication
Latest Publications
- 1 October 2015
- Published by Elsevier in Neuropeptides
- Vol. 53, 63-70
Gadolinium-complexed Aβ-binding contrast agents for MRI diagnosis of Alzheimer's Disease
- 1 October 2015
- Published by Elsevier in Neuropeptides
- Vol. 53, 63-70
Gadolinium-complexed Aβ-binding contrast agents for MRI diagnosis of Alzheimer's Disease
- Open Access
- 19 March 2015
- Published by Frontiers Media SA in Frontiers in Chemistry
- Vol. 3, 17
The elusive nature and diagnostics of misfolded Aβ oligomers
Amyloid-beta (Aβ) peptide oligomers are believed to be the causative agents of Alzheimer’s disease (AD). Though post-mortem examination shows that insoluble fibrils are deposited in the brains of AD patients in the form of intracellular (tangles) and extracellular (plaques) deposits, it has been observed that cognitive impairment is linked to synaptic dysfunction in the stages of the illness well before the appearance of these mature deposits. Increasing evidence suggests that the most toxic forms of Aβ are soluble low-oligomer ligands whose amounts better correlate with the extent of cognitive loss in patients than those of fibrillar insoluble forms. Therefore, these ligands hold the key to a better understanding of AD prompting the search for clearer correlations between their structure and toxicity. The importance of such correlations and their diagnostic value for the early diagnosis of AD is discussed here with a particular emphasis on the transient nature and structural plasticity of misfolded Aβ oligomers.
- 19 March 2015
- Published by Frontiers Media SA in Frontiers in Chemistry
- Vol. 3, 17
Open AccessThe elusive nature and diagnostics of misfolded Aβ oligomers
Amyloid-beta (Aβ) peptide oligomers are believed to be the causative agents of Alzheimer’s disease (AD). Though post-mortem examination shows that insoluble fibrils are deposited in the brains of AD patients in the form of intracellular (tangles) and extracellular (plaques) deposits, it has been observed that cognitive impairment is linked to synaptic dysfunction in the stages of the illness well before the appearance of these mature deposits. Increasing evidence suggests that the most toxic forms of Aβ are soluble low-oligomer ligands whose amounts better correlate with the extent of cognitive loss in patients than those of fibrillar insoluble forms. Therefore, these ligands hold the key to a better understanding of AD prompting the search for clearer correlations between their structure and toxicity. The importance of such correlations and their diagnostic value for the early diagnosis of AD is discussed here with a particular emphasis on the transient nature and structural plasticity of misfolded Aβ oligomers.