D
David A. Pearce
Researcher at Northumbria University
Publications - 405
Citations - 20297
David A. Pearce is an academic researcher from Northumbria University. The author has contributed to research in topics: Batten disease & CLN3. The author has an hindex of 72, co-authored 396 publications receiving 18416 citations. Previous affiliations of David A. Pearce include University of Zurich & University of York.
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Distinct patterns of serum immunoreactivity as evidence for multiple brain‐directed autoantibodies in juvenile neuronal ceroid lipofuscinosis
Ming K. Lim,J. Beake,Ellen Bible,Timothy M. Curran,Denia Ramirez-Montealegre,David A. Pearce,Jonathan D. Cooper +6 more
TL;DR: Collectively, these studies provide evidence of the presence of autoreactive antibodies within multiple forms of NCL, and are not exclusively directed towards GAD65.
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Localization and processing of CLN3, the protein associated to Batten disease: where is it and what does it do?
TL;DR: The most likely conclusion is that CLN3 is a lysosomal/endosomal protein that is trafficked through the endoplasmic reticulum (ER) and Golgi and has a potential role in the recycling of synaptic vesiclesthrough the endosome/lysosome.
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Finding the most appropriate mouse model of juvenile CLN3 (Batten) disease for therapeutic studies: the importance of genetic background and gender
Attila D. Kovács,David A. Pearce +1 more
TL;DR: The results show that Cln3−/− male mice on the 129S6/SvEv genetic background are the most appropriate candidates for therapeutic studies, and males and females on the C57BL/6J background provide good outcome measures for therapeutic interventions.
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Differing preferences of Antarctic soil nematodes for microbial prey
TL;DR: It is concluded that complex trophic interactions may occur in apparently simple Antarctic soil food webs using nematodes extracted from moss at Signy Island for two microalgae, three microfungi and six heterotrophic bacteria.
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NH2 terminus of serum and glucocorticoid-regulated kinase 1 binds to phosphoinositides and is essential for isoform-specific physiological functions
Alan C. Pao,James A. McCormick,James A. McCormick,Hongyan Li,John Siu,Cédric Govaerts,Vivek Bhalla,Rama Soundararajan,David A. Pearce +8 more
TL;DR: Observations support the idea that the NH(2)-terminal domain acts downstream of PI 3-kinase-dependent activation to target the kinase to specific cellular compartments and/or substrates, possibly through its interactions with a subset of phosphoinositides.