H
Helen R. Flynn
Researcher at Francis Crick Institute
Publications - 53
Citations - 3811
Helen R. Flynn is an academic researcher from Francis Crick Institute. The author has contributed to research in topics: Kinase & Plasmodium falciparum. The author has an hindex of 23, co-authored 45 publications receiving 3176 citations. Previous affiliations of Helen R. Flynn include GlaxoSmithKline & University of Cambridge.
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Journal ArticleDOI
Poly(ADP-ribose)-dependent regulation of DNA repair by the chromatin remodeling enzyme ALC1.
Dragana Ahel,Zuzana Hořejší,Nicola Wiechens,Sophie E. Polo,Elisa Garcia-Wilson,Ivan Ahel,Ivan Ahel,Helen R. Flynn,Mark Skehel,Stephen C. West,Stephen P. Jackson,Tom Owen-Hughes,Simon J. Boulton +12 more
TL;DR: A chromatin-remodeling enzyme, ALC1 (Amplified in Liver Cancer 1, also known as CHD1L), is identified that interacts with poly(ADP-ribose) and catalyzes PARP1-stimulated nucleosome sliding and provides new insights into the mechanisms by which poly(adenosine 5′-diphosphate (ADP)–riboses) regulates DNA repair.
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Eco1-Dependent Cohesin Acetylation During Establishment of Sister Chromatid Cohesion
Tom Rolef Ben-Shahar,Sebastian Heeger,Chris Lehane,Philip East,Helen R. Flynn,Mark Skehel,Frank Uhlmann +6 more
TL;DR: The results indicate that Eco1 modifies cohesin to stabilize sister chromatid cohesion in parallel with a cohesion establishment reaction that is in principle Eco1-independent.
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Identification of Holliday junction resolvases from humans and yeast
TL;DR: The human Holliday junction resolvase, GEN1, and its yeast orthologue, Yen1, were independently identified using two distinct experimental approaches: GEN1 was identified by mass spectrometry following extensive fractionation of HeLa cell-free extracts, whereas Yen1 was detected by screening a yeast gene fusion library for nucleases capable of Holliday junctions resolution.
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Discovery and Characterization of Small Molecule Inhibitors of the Bet Family Bromodomains.
Chun-wa Chung,Hervé Coste,Julia H. White,Olivier Mirguet,Jonathan I. Wilde,Romain Luc Marie Gosmini,Chris J. Delves,Sylvie M. Magny,Robert Woodward,Stephen A. Hughes,Eric Boursier,Helen R. Flynn,Anne Marie Jeanne Bouillot,Paul Bamborough,Jean-Marie Brusq,Françoise Gellibert,Emma J. Jones,Alizon M. Riou,Paul Homes,Sandrine Martin,Iain Uings,Jérôme Toum,Catherine A. Clément,Anne-Benedicte Boullay,Rachel Grimley,Florence Blandel,Rab K. Prinjha,Kevin Lee,Jorge Kirilovsky,Edwige Nicodeme +29 more
TL;DR: X-ray crystal structures of compounds bound into bromodomains of Brd2 and Brd4 elucidate the molecular interactions of binding and explain the precisely defined stereochemistry required for activity.
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CDK Substrate Phosphorylation and Ordering the Cell Cycle.
TL;DR: A phosphoproteomics-based systems analysis of CDK substrates in fission yeast is presented and it is demonstrated that the phosphorylation of different CDK substrateates can be temporally ordered during the cell cycle by a single cyclin-CDK.