E
Estrella Guarino
Researcher at University of Oxford
Publications - 13
Citations - 1073
Estrella Guarino is an academic researcher from University of Oxford. The author has contributed to research in topics: Ribonucleotide reductase & DNA replication. The author has an hindex of 8, co-authored 11 publications receiving 936 citations. Previous affiliations of Estrella Guarino include University of Extremadura.
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Journal ArticleDOI
Germline mutations affecting the proofreading domains of POLE and POLD1 predispose to colorectal adenomas and carcinomas
Claire Palles,Jean-Baptiste Cazier,Kimberley Howarth,Enric Domingo,Angela M. Jones,Peter Broderick,Zoe Kemp,Sarah L. Spain,Estrella Guarino,Israel Salguero,Amy L. Sherborne,Daniel Chubb,Luis G. Carvajal-Carmona,Yusanne Ma,Kulvinder Kaur,Sara E. Dobbins,Ella Barclay,Maggie Gorman,Lynn Martin,Michal Kovac,Michal Kovac,Sean Humphray,Anneke Lucassen,Christopher Holmes,David Bentley,Peter Donnelly,Peter Donnelly,Jenny C. Taylor,Christos Petridis,Rebecca Roylance,Elinor J. Sawyer,David J. Kerr,Susan K. Clark,Jonathan M. Grimes,Stephen E. Kearsey,Huw Thomas,Gilean McVean,Richard S. Houlston,Ian Tomlinson +38 more
TL;DR: A recently described group of hypermutant, microsatellite-stable CRCs is likely to be caused by somatic POLE mutations affecting the exonuclease domain, predicted to cause a defect in the correction of mispaired bases inserted during DNA replication.
Journal ArticleDOI
Cellular regulation of ribonucleotide reductase in eukaryotes.
TL;DR: Additional mechanisms of control responsible for providing a balanced supply of dNTPs, including regulation of expression of RNR genes, proteolysis of R NR subunits, control of the cellular localization of the small RNR subunit, and regulation of Rnr activity by small protein inhibitors are focused on.
Journal ArticleDOI
Direct Role for Proliferating Cell Nuclear Antigen in Substrate Recognition by the E3 Ubiquitin Ligase CRL4Cdt2
Courtney G. Havens,Nadia Shobnam,Estrella Guarino,Richard C. Centore,Lee Zou,Stephen E. Kearsey,Johannes C. Walter +6 more
TL;DR: This work identifies an acidic residue in PCNA that is essential to support destruction of all CRL4Cdt2 substrates and illustrates a potentially general mechanism by which E3 ligases can couple ubiquitylation to the formation of protein-protein interactions.
Journal ArticleDOI
Double-Strand Break Generation under Deoxyribonucleotide Starvation in Escherichia coli
TL;DR: Stalled replication forks produced by three different ways of depleting deoxynucleoside triphosphate showed different capacities to undergo "replication fork reversal," which occurred at the stalled forks generated by hydroxyurea treatment.
Journal ArticleDOI
Cdt1 proteolysis is promoted by dual PIP degrons and is modulated by PCNA ubiquitylation
Estrella Guarino,Marianne E. A. Shepherd,Israel Salguero,Hui Hua,Rachel S. Deegan,Stephen E. Kearsey +5 more
TL;DR: It is shown that fission yeast Cdt1 interacts with PCNA in vivo and that DNA loading of PCNA is needed for Cdt2 proteolysis after DNA damage and in S phase, and that poly-ubiquitylation ofPCNA, which occurs after DNADamage, reduces Cdt 1 proteolytic activity.