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Molecular Biology

D-Index
100
Citations
38730
World Ranking
528
National Ranking
40

Research.com Recognitions

  • 2012 - Member of Academia Europaea
  • 2010 - Fellow of the Royal Society, United Kingdom
  • 1996 - Fellow of the Royal Society of Edinburgh

Overview

Ronald T. Hay is affiliated with the University of Dundee in the United Kingdom. Their research spans the fields of Biochemistry, Genetics and Molecular Biology, with significant contributions also to Medicine. Within these fields, their work often focuses on Molecular Biology, Oncology, Epidemiology, Cell Biology, and Genetics.

The scientist's main research topics include:

  • Ubiquitin and proteasome pathways
  • Peptidase inhibition and analysis
  • Virus-based gene therapy research
  • Protein degradation and inhibitors
  • RNA modifications and cancer
  • Retinoids in leukemia and cellular processes
  • Acute myeloid leukemia research

They have published numerous peer-reviewed papers, with notable recent publications including:

  • Mechanism and function of DNA replication-independent DNA-protein crosslink repair via the SUMO-RNF4 pathway (2021) in The EMBO Journal
  • Antibody RING-Mediated Destruction of Endogenous Proteins (2020) in Molecular Cell
  • Ubiquitin transfer by a RING E3 ligase occurs from a closed E2~ubiquitin conformation (2020) in Nature Communications
  • Mechanism of degrader-targeted protein ubiquitinability (2024) in Science Advances
  • Concerted SUMO-targeted ubiquitin ligase activities of TOPORS and RNF4 are essential for stress management and cell proliferation (2024) in Nature Structural & Molecular Biology

Frequent coauthors collaborating with them include:

  • Michael H. Tatham
  • Adel F.M. Ibrahim
  • Niels Mailand
  • Barbara Mojsa
  • Alejandro Rojas-Fernández

Their work has been published repeatedly in venues such as bioRxiv (Cold Spring Harbor Laboratory), Nature Communications, The Journal of Cell Biology, Nature Structural & Molecular Biology, and Cell Reports.

Recognition of their scientific contributions includes being named a Fellow of the Royal Society of Edinburgh in 1996, a Fellow of the Royal Society, United Kingdom in 2010, and a Member of Academia Europaea in 2012.

Best Publications

  • SUMO: a history of modification

    Ronald T. Hay

  • SUMO-1 Modification of IκBα Inhibits NF-κB Activation

    Joana M.P Desterro;Manuel S Rodriguez;Ronald T Hay

  • Thioredoxin regulates the DNA binding activity of NF-kappa B by reduction of a disulphide bond involving cysteine 62.

    James R. Matthews;Naomi Wakasugi;Jean-Louis virelizier;Junji Yodoi

  • Polymeric chains of SUMO-2 and SUMO-3 are conjugated to protein substrates by SAE1/SAE2 and Ubc9

    Michael H. Tatham;Ellis Jaffray;Owen A. Vaughan;Joana M.P. Desterro

  • RNF4 is a poly-SUMO-specific E3 ubiquitin ligase required for arsenic-induced PML degradation.

    Michael H Tatham;Marie-Claude Geoffroy;Linnan Shen;Anna Plechanovova

  • SUMO-1 Conjugation in Vivo Requires Both a Consensus Modification Motif and Nuclear Targeting

    Manuel S. Rodriguez;Catherine Dargemont;Catherine Dargemont;Ronald T. Hay

  • SUMO-1 modification activates the transcriptional response of p53

    Manuel S. Rodriguez;Joana M. P. Desterro;Sonia Lain;Carol A. Midgley

  • Mdm2-Mediated NEDD8 Conjugation of p53 Inhibits Its Transcriptional Activity

    Dimitris P. Xirodimas;Mark K. Saville;Jean Christophe Bourdon;Ronald T. Hay

  • Nuclear localization of I kappa B alpha promotes active transport of NF-kappa B from the nucleus to the cytoplasm

    F. Arenzana-Seisdedos;P. Turpin;M. Rodriguez;D. Thomas

  • Inducible nuclear expression of newly synthesized I kappa B alpha negatively regulates DNA-binding and transcriptional activities of NF-kappa B

    F Arenzana-Seisdedos;J Thompson;M S Rodriguez;F Bachelerie

  • OMERO: flexible, model-driven data management for experimental biology

    Christopher Allan;Jean-Marie Burel;Josh Moore;Colin Blackburn

  • Structure of a RING E3 ligase and ubiquitin-loaded E2 primed for catalysis

    Anna Plechanovová;Ellis G. Jaffray;Michael H. Tatham;James H. Naismith

  • Inhibition of NF-κB DNA Binding by Nitric Oxide

    James R. Matthews;Catherine H. Botting;Maria Panico;Howard R. Morris

  • P300 transcriptional repression is mediated by SUMO modification.

    David Girdwood;Donna Bumpass;Owen A Vaughan;Alison Thain

  • System-wide changes to SUMO modifications in response to heat shock

    Filip Golebiowski;Ivan Matic;Michael H. Tatham;Christian Cole

  • Multiple C-Terminal Lysine Residues Target p53 for Ubiquitin-Proteasome-Mediated Degradation

    Manuel S Rodriguez;Joana M P Desterro;Sonia Lain;David P. Lane

  • Mutations in the IkBa gene in Hodgkin's disease suggest a tumour suppressor role for IkappaBalpha.

    Eric Cabannes;Gulfaraz Khan;Fabienne Aillet;Ruth F Jarrett

  • Ubch9 conjugates SUMO but not ubiquitin

    Joana M.P Desterro;Jill Thomson;Ronald T Hay

  • Family-wide analysis of poly(ADP-ribose) polymerase activity

    Sejal Vyas;Ivan Matic;Lilen Uchima;Jenny Rood

  • Identification of the Enzyme Required for Activation of the Small Ubiquitin-like Protein SUMO-1

    Joana M.P. Desterro;Manuel S. Rodriguez;Graham D. Kemp;Ronald T. Hay

Frequent Co-Authors

Manuel S. Rodriguez
Manuel S. Rodriguez Centre national de la recherche scientifique, CNRS
James H. Naismith
James H. Naismith Rosalind Franklin Institute
Angus I. Lamond
Angus I. Lamond University of Dundee
Matthias Mann
Matthias Mann Max Planck Institute of Biochemistry
David P. Lane
David P. Lane Karolinska Institute
Jean-Louis Virelizier
Jean-Louis Virelizier Institut Pasteur
Fernando Arenzana-Seisdedos
Fernando Arenzana-Seisdedos Chinese Academy of Sciences
Ian Wilmut
Ian Wilmut University of Edinburgh
Catherine Dargemont
Catherine Dargemont Université Paris Cité
John P. Iredale
John P. Iredale University of Bristol

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