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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Linear motifs confer functional diversity onto splice variants
TL;DR: It is demonstrated that short linear motifs are key components for establishing protein diversity between splice variants, suggesting that protein isoform diversity is tightly coupled to the modulation of IDRs.
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KH domains within the FMR1 sequence suggest that fragile X syndrome stems from a defect in RNA metabolism
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The identification of short linear motif-mediated interfaces within the human interactome
TL;DR: iELM is introduced, a method to identify interactions mediated by SLiMs and add molecular details of the interaction interfaces to both interacting proteins, and was applied to the human interactome to identify a set of high-confidence putative SLiM-mediated PPIs.
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Dimerization and Protein Binding Specificity of the U2AF Homology Motif of the Splicing Factor Puf60
Lorenzo Corsini,Michael Hothorn,Gunter Stier,Vladimir Rybin,Klaus Scheffzek,Toby J. Gibson,Michael Sattler +6 more
TL;DR: It is shown that the Puf 60 UHM is mainly monomeric in physiological buffer, whereas its dimerization is induced upon the addition of SDS, and the data suggest that the functional cooperativity between U2AF65 and Puf60 may involve simultaneous interactions of the two proteins with SF3b155.
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The solution structure of a leucine-zipper motif peptide.
Vladimir Saudek,A. Pastore,M. A. Castiglione Morelli,Rainer Frank,H. Gausepohl,Toby J. Gibson +5 more
TL;DR: The complete structure determination of a 34 residue synthetic peptide with the amino acid sequence of the dimerization domain (leucine zipper) of GCN4 shows the structural independence of the leucine-zipper domain from the contiguous DNA binding region.