ORCID Profile
0000-0002-4330-0818
Current Organisation
The University of Edinburgh
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Publisher: Wiley
Date: 28-02-2023
Abstract: Protein misfolding and aggregation into oligomeric and fibrillar structures is a common feature of many neurogenerative disorders. Single‐molecule techniques have enabled characterization of these lowly abundant, highly heterogeneous protein aggregates, previously inaccessible using ensemble averaging techniques. However, they usually rely on the use of recombinantly‐expressed labeled protein, or on the addition of amyloid stains that are not protein‐specific. To circumvent these challenges, we have made use of a high affinity antibody labeled with orthogonal fluorophores combined with fast‐flow microfluidics and single‐molecule confocal microscopy to specifically detect α‐synuclein, the protein associated with Parkinson's disease. We used this approach to determine the number and size of α‐synuclein aggregates down to picomolar concentrations in biologically relevant s les.
Publisher: Cambridge University Press (CUP)
Date: 28-12-2021
DOI: 10.1017/AEE.2021.31
Abstract: They thought they felt something , perhaps. The wisp of an outline not distinct enough to trace. Good. They circled it, at times, and at other times found themselves within. As they walked (a sort of walking. Figurative but real. Digital, but here. Over months of events), it curled open and headed in several directions. Foldings in the backcloth that furrowed them along until, as they walked and talked, they felt that perhaps a territory was becoming simultaneously clearer and more obscure, that they might find a way to enquire, even as it meant becoming the folds themselves. As they coalesce, Scott, Jamie, and Dave each come to this project differently (of course). From their own situations, with their own problems and with different voices and ways of writing. We (for the first shift in voice) take post-qualitative inquiry to be infused with a question mark, wary of attempts to make it a ‘thing’. Yet here we are, drawn to potentials, to the opening of conditions, to the possibility of something still to come. We hope to make a shift, to realise (as in make manifest) ontology and its everyday performance as synonymous with environmental education. Environmental education as a life .
Publisher: Wiley
Date: 28-02-2023
Abstract: Protein misfolding and aggregation into oligomeric and fibrillar structures is a common feature of many neurogenerative disorders. Single‐molecule techniques have enabled characterization of these lowly abundant, highly heterogeneous protein aggregates, previously inaccessible using ensemble averaging techniques. However, they usually rely on the use of recombinantly‐expressed labeled protein, or on the addition of amyloid stains that are not protein‐specific. To circumvent these challenges, we have made use of a high affinity antibody labeled with orthogonal fluorophores combined with fast‐flow microfluidics and single‐molecule confocal microscopy to specifically detect α‐synuclein, the protein associated with Parkinson's disease. We used this approach to determine the number and size of α‐synuclein aggregates down to picomolar concentrations in biologically relevant s les.
Location: United Kingdom of Great Britain and Northern Ireland
Location: United Kingdom of Great Britain and Northern Ireland
Location: United Kingdom of Great Britain and Northern Ireland
No related grants have been discovered for David Clarke.