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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Identification of α-fetoprotein as an autoantigen in juvenile Batten disease
TL;DR: Findings provide more evidence that autoimmunity is an active component of juvenile Batten disease, and the gender-apparent difference evidenced by patients with regard anti-AFP antibodies may underlie variation in progression and clinical manifestations in this disorder.
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Sensors for observing ecosystem status
Silke Kröger,E. R. Parker,Julian D. Metcalfe,Naomi Greenwood,Rodney M. Forster,D. B. Sivyer,David A. Pearce +6 more
TL;DR: An introduction to how and why ecosystem status is currently observed, what variables are quantified, from what platforms, using remote sensing or in-situ measurements, and gives examples of useful sensor based tools are given.
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Decreased intestinal glucose transport in the sgk3-knockout mouse
Ciprian D. Sandu,Rexhep Rexhepaj,Florian Grahammer,James A. McCormick,Guido Henke,Monica Palmada,Srinivas Nammi,Undine E. Lang,Marco Metzger,Lothar Just,Thomas Skutella,Kevin Dawson,Jian Wang,David A. Pearce,Florian Lang +14 more
TL;DR: SGK3 is required for adequate intestinal Na+ coupled glucose transport and impaired glucose absorption may contribute to delayed growth and decreased plasma glucose concentrations of SGK3 deficient mice.
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Identification of the contiguous Paracoccus denitrificans ccmF and ccmH genes : disruption of ccmF, encoding a putative transporter, results in formation of an unstable apocytochrome c and deficiency in siderophore production
TL;DR: Apocytochrome C550 was detected in the periplasm of a new mutant of Paracoccus denitrificans, HN48, that is pleiotropically lacking c-type cytochromes, produces reduced levels of siderophores and carries a Tn5 insertion in the ccmF gene for which sequence data, along with that for the contiguous ccmH, are reported.
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Scaffold protein connector enhancer of kinase suppressor of Ras isoform 3 (CNK3) coordinates assembly of a multiprotein epithelial sodium channel (ENaC)-regulatory complex
TL;DR: The results strongly suggest that CNK3 is a molecular scaffold, which coordinates the assembly of a multiprotein ENaC-regulatory complex and hence plays a central role in Na+ homeostasis.