T
Toby J. Gibson
Researcher at European Bioinformatics Institute
Publications - 176
Citations - 177834
Toby J. Gibson is an academic researcher from European Bioinformatics Institute. The author has contributed to research in topics: Short linear motif & Eukaryotic Linear Motif resource. The author has an hindex of 78, co-authored 171 publications receiving 167371 citations. Previous affiliations of Toby J. Gibson include University of Rome Tor Vergata & University College Dublin.
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The phylogenetic distribution of frataxin indicates a role in iron-sulfur cluster protein assembly
TL;DR: Combining data on the co-occurrence of genes in genomes with experimental and predicted cellular localization data of their proteins supports the hypothesis that frataxin is directly involved in iron-sulfur cluster protein assembly.
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Dystrophin and utrophin: the missing links!
TL;DR: This work reviews recent findings and presents new hypotheses into the structural and functional properties of the actin‐binding domain, central coiled‐coil region and regulatory/membrane protein‐binding regions of dystrophin and utrophin.
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Friedreich's ataxia protein: phylogenetic evidence for mitochondrial dysfunction
TL;DR: Clues to the function of frataxin are provided by the mitochondrial location, a clinically similar ataxia with vitamin E deficiency, and certain neuropathies with mitochondrial DNA instability caused by mutations in nuclear genes.
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Motif switches: decision-making in cell regulation
TL;DR: Pioneering work on the nature and function of intrinsically disordered protein regions has revealed many elegant switching mechanisms that underlie cell signalling and regulation, prompting a reevaluation of their role in cooperative decision-making.
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Nucleosome Binding by the Bromodomain and PHD Finger of the Transcriptional Cofactor p300
Anja Ragvin,Håvard Valvatne,Sigrid Erdal,Vibeke Årskog,Katharina R. Tufteland,Kamilla Breen,Anne Margrete Øyan,Anton Eberharter,Toby J. Gibson,Peter B. Becker,Rein Aasland +10 more
TL;DR: The bromodomain/PHD finger region of the transcriptional cofactor p300 can bind to nucleosomes that have a high degree of histone acetylation, consistent with a model where the two domains cooperate in nucleosome binding.