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Leonard J. Foster

Researcher at University of British Columbia

Publications -  314
Citations -  18409

Leonard J. Foster is an academic researcher from University of British Columbia. The author has contributed to research in topics: Proteome & Honey bee. The author has an hindex of 60, co-authored 286 publications receiving 16070 citations. Previous affiliations of Leonard J. Foster include University of Southern Denmark & Vancouver Coastal Health.

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PSORTb 3.0

TL;DR: This work developed PSORTb version 3.0 with improved recall, higher proteome-scale prediction coverage, and new refined localization subcategories, and evaluated the most accurate SCL predictors using 5-fold cross validation plus an independent proteomics analysis.
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Unbiased quantitative proteomics of lipid rafts reveals high specificity for signaling factors

TL;DR: This work uses quantitative high-resolution MS to specifically detect proteins depleted from rafts by cholesterol-disrupting drugs, resulting in a set of 241 authentic lipid raft components, providing the first large-scale and unbiased evidence for the connection of rafts with signaling and place limits on the fraction of plasma membrane composed by rafts.
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A proteomics strategy to elucidate functional protein-protein interactions applied to EGF signaling

TL;DR: Stable isotopic amino acids in cell culture is employed to differentially label proteins in EGF-stimulated versus unstimulated cells and SILAC combined with modification-based affinity purification is a useful approach to detect specific and functional protein-protein interactions.
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A Mammalian Organelle Map by Protein Correlation Profiling

TL;DR: This analysis ties biochemistry, cell biology, and genomics into a common framework for organelle analysis and identifies networks of coexpressed genes, cis-regulatory motifs, and putative transcriptional regulators involved in organelle biogenesis.
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Isotopic labeling of terminal amines in complex samples identifies protein N-termini and protease cleavage products

TL;DR: The approach, named terminal amine isotopic labeling of substrates (TAILS), addresses this challenge by using dendritic polyglycerol aldehyde polymers that remove tryptic and C-terminal peptides to discriminate between the substrates of the protease of interest and the products of background proteolysis.