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Robert N. O'Meally

Researcher at Johns Hopkins University School of Medicine

Publications -  43
Citations -  3175

Robert N. O'Meally is an academic researcher from Johns Hopkins University School of Medicine. The author has contributed to research in topics: Phosphorylation & Proteome. The author has an hindex of 22, co-authored 38 publications receiving 2587 citations. Previous affiliations of Robert N. O'Meally include Johns Hopkins University.

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The Plasma Proteome Identifies Expected and Novel Proteins Correlated with Micronutrient Status in Undernourished Nepalese Children

TL;DR: Plasma proteomics can identify and quantify protein biomarkers of micronutrient status in undernourished children, and individual proteins explained 34–77% of variation in their respective nutrient concentration by this strategy.
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Fatty acid synthase inhibits the O- GlcNAcase during oxidative stress

TL;DR: In this paper, the authors demonstrate that oxidative stress leads to elevated O-GlcNAc levels in U2OS cells but has little impact on the activity of OGT.
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Defective human MutY phosphorylation exists in colorectal cancer cell lines with wild-type MutY alleles.

TL;DR: The authors showed that the defective repair of 8-oxoguanine (8-oxoG) mispairs was due to defective phosphorylation of the MutY protein in colorectal cancer cells.
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Phosphorylation of mutant huntingtin at serine 116 modulates neuronal toxicity.

TL;DR: The results suggest that S116 is a potential therapeutic target for Huntington's Disease, and indicate that the screening method is useful for identifying candidate phosphorylation sites.
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Combined Antibody/Lectin Enrichment Identifies Extensive Changes in the O-GlcNAc Sub-proteome upon Oxidative Stress

TL;DR: Analysis of proteins with altered glycosylation suggests that stress-induced changes in O-GlcNAcylation cluster into pathways known to regulate the cell's response to injury and include protein folding, transcriptional regulation, epigenetics, and proteins involved in RNA biogenesis.