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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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Definition of Naturally Processed Peptides Reveals Convergent Presentation of Autoantigenic Topoisomerase I Epitopes in Scleroderma

TL;DR: Autoimmune responses to DNA topoisomerase I (topo I) are found in a subset of scleroderma patients who are at high risk for interstitial lung disease and mortality, and the frequency of HLA–DR–restricted topo I–specific CD4+ T cells is associated with the presence, severity, and progression of ILD.
Posted ContentDOI

Definition of naturally processed peptides reveals convergent presentation of autoantigenic topoisomerase-I epitopes in scleroderma

TL;DR: Use of a novel natural antigen processing assay reveals a mechanism for the presentation of shared CD4+ T cell epitopes of topoisomerase-I in immunogenetically diverse patients with scleroderma.
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Deleting a UBE3A substrate rescues impaired hippocampal physiology and learning in Angelman syndrome mice

TL;DR: In this article, the authors identify Ephexin5 as a key driver of hippocampal dysfunction and related behavioral deficits in Angelman syndrome (AS) mouse models, and they demonstrate the exciting potential of targeting EphexIN5, and possibly other UBE3A substrates, to improve symptoms of AS and other Ube3A-related developmental disorders.
Posted ContentDOI

Deleting a UBE3A substrate rescues impaired hippocampal physiology and learning in Angelman syndrome mice

TL;DR: It is reported that Ephexin5 is a direct substrate of UBE3A ubiquitin ligase activity and identified as a key driver of hippocampal dysfunction and related behavioral deficits in AS mouse models.
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PRINT: A Protein Bioconjugation Method with Exquisite N-terminal Specificity.

TL;DR: This work generates with high yield and purity exquisitely site specific and selective bio-conjugates of TNF-α by using amine reactive NHS ester chemistry and confirms the N terminal selectivity and specificity.