E
Edel M. Hyland
Researcher at Queen's University Belfast
Publications - 16
Citations - 745
Edel M. Hyland is an academic researcher from Queen's University Belfast. The author has contributed to research in topics: Nucleosome & Histone code. The author has an hindex of 10, co-authored 16 publications receiving 668 citations. Previous affiliations of Edel M. Hyland include Dublin City University & Johns Hopkins University.
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Journal ArticleDOI
Insights into the role of histone H3 and histone H4 core modifiable residues in Saccharomyces cerevisiae.
Edel M. Hyland,Michael S. Cosgrove,Michael S. Cosgrove,Henrik Molina,Dongxia Wang,Dongxia Wang,Akhilesh Pandey,Robert J. Cottee,Jef D. Boeke +8 more
TL;DR: It is shown that substitutions at hist one H4 K91, K59, S47, and R92 and histone H3 K56 and K115 lead to hypersensitivity to DNA-damaging agents, linking the significance of the chemical identity of these modifiable residues to DNA metabolism.
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Probing Nucleosome Function: A Highly Versatile Library of Synthetic Histone H3 and H4 Mutants
Junbiao Dai,Edel M. Hyland,Daniel S. Yuan,Hailiang Huang,Hailiang Huang,Joel S. Bader,Joel S. Bader,Jef D. Boeke +7 more
TL;DR: A versatile library of 486 systematic histone H3 and H4 substitution and deletion mutants that probes the contribution of each residue to nucleosome function was generated in Saccharomyces cerevisiae, revealing new functions for distinct histone residues and new interdependencies among nucleosomes components and their modifiers.
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HistoneHits: A database for histone mutations and their phenotypes
Hailiang Huang,Alexandra Maertens,Edel M. Hyland,Junbiao Dai,Anne Norris,Jef D. Boeke,Joel S. Bader +6 more
TL;DR: HistoneHits, a database of phenotypes for systematic collections of histone mutants, combines assay results (phenotypes) with information about sequences, structures, post-translational modifications, and evolutionary conservation.
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Histone H3 exerts a key function in mitotic checkpoint control
TL;DR: It is shown that histone H3 plays a crucial role in activating the spindle assembly checkpoint in response to a defect in mitosis, and is thus a key factor transmitting the tension status to the spindles emanating from the opposite spindle pole bodies.
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The DNA Binding Domain of the Gene 2.5 Single-stranded DNA-binding Protein of Bacteriophage T7
TL;DR: Gene 2.5 of bacteriophage T7 encodes a single-stranded DNA-binding protein that is essential for viral survival and its crystal structure reveals a conserved oligosaccharide/oligonucleotide binding fold predicted to interact with single-Stranded DNA, but there is no experimental evidence to support this hypothesis.