Nigel P. Birch
University of Auckland
79 Papers
1K Citations
Nigel P. Birch is an academic researcher from University of Auckland. The author has contributed to research in topics: Neuroserpin & Serpin. The author has an hindex of 28, co-authored 77 publications. Previous affiliations of Nigel P. Birch include National Institutes of Health.
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Papers
RNA interference in the light brown apple moth, Epiphyas postvittana (Walker) induced by double-stranded RNA feeding.
C. T. Turner,Marcus Davy,Robin M. MacDiarmid,Kim M. Plummer,Nigel P. Birch,Richard D. Newcomb +5 more
TL;DR: It is demonstrated in the horticultural pest, Epiphyas postvittana, that RNAi can be triggered by oral delivery of dsRNA to larvae, and Transcript levels of a larval gut carboxylesterase gene were reduced to less than half that of controls within 2 days of being fed EposCXE1 ds RNA.
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An Optimised Human Cell Culture Model for Alveolar Epithelial Transport
TL;DR: Experimental conditions for the application of NCI-H441 cells as a model for investigating ion and water transport in the human alveolar epithelium are defined and the pathways of sodium and chloride transport are identified.
Identification of novel dietary phytochemicals inhibiting the efflux transporter breast cancer resistance protein (BCRP/ABCG2)
TL;DR: The identified inhibitory activity of dietary phytochemicals onABCG2 provides a framework for further investigation of ABCG2-modulated phytochemical bioavailability, MDR, and possible food-drug interactions.
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Isolation of Two Complementary Deoxyribonucleic Acid Clones from a Rat Insulinoma Cell Line Based on Similarities to Kex2 and Furin Sequences and the Specific Localization of Each Transcript to Endocrine and Neuroendocrine Tissues in Rats
TL;DR: Two rat insulinoma cDNAs that code for proteins homologous to the Kex2 dibasic protease of yeast and the mammalian furin gene product are identified, indicating that both enter the secretory pathway.
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Processing of synthetic pro-islet amyloid polypeptide (proIAPP) ‘amylin’ by recombinant prohormone convertase enzymes, PC2 and PC3, in vitro
Claire E Higham,Rebecca L. Hull,Laura Catherine Lawrie,Kathleen I.J. Shennan,John F. Morris,Nigel P. Birch,Kevin Docherty,Anne Clark +7 more
TL;DR: Synthetic human proIAPP was incubated with recombinant prohormone convertases and there was no evidence for substantial competition for the processing enzymes when the combined substrates proinsulin andproIAPP were incubation with both PC2 and PC3, suggesting that proteolysis of pro-IAPP and pro-insulin is coincident in secretory granules and increased Proinsulin secretion in diabetes could be accompanied by increased production of proI APP.
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