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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Lorist6, a cosmid vector with BamHI, NotI, ScaI and HindIII cloning sites and altered neomycin phosphotransferase gene expression
TL;DR: Four new features have been included in a phage-lambda-replicon-based cosmid vector, Lorist6, increasing expression of the resistance gene product and preventing transcription into insert DNAs.
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Evidence for a protein domain superfamily shared by the cyclins, TFIIB and RB/p107.
TL;DR: The results suggest the presence of a domain superfamily, which the authors term the TR domain, in nuclear regulatory proteins belonging to the TFIIB, cyclin and RB families, that has been duplicated many times during eukaryotic evolution.
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DNA-binding domain ancestry.
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Formin defines a large family of morphoregulatory genes and functions in establishment of the polarising region
Rolf Zeller,Anna G. Haramis,Aimée Zuniga,Caroline McGuigan,Rosanna Dono,Gary Davidson,Sophie Chabanis,Toby J. Gibson +7 more
TL;DR: Disruption of the epithelial-mesenchymal interactions controlling induction of metanephric kidneys in ld mutant embryos indicates that formin might function more generally in transduction of morphogenetic signals during embryonic pattern formation.
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Solution structure of the DNA-binding domain of the yeast transcriptional activator protein GCN4
Vladimir Saudek,Annalisa Pastore,M. A. Castiglione Morelli,Rainer Frank,H. Gausepohl,Toby J. Gibson,F. Weih,Paul Roesch +7 more
TL;DR: The solution structure of an active synthetic peptide containing both the leucine zipper and the adjacent basic domain of the yeast transcription factor GCN4 (residues 220-280) was determined by NMR, showing structurally distinct behaviours.