Ronald T. Hay

30.3k total citations · 7 hit papers
247 papers, 24.3k citations indexed

About

Ronald T. Hay is a scholar working on Molecular Biology, Oncology and Genetics. According to data from OpenAlex, Ronald T. Hay has authored 247 papers receiving a total of 24.3k indexed citations (citations by other indexed papers that have themselves been cited), including 205 papers in Molecular Biology, 66 papers in Oncology and 52 papers in Genetics. Recurrent topics in Ronald T. Hay's work include Ubiquitin and proteasome pathways (128 papers), Virus-based gene therapy research (44 papers) and NF-κB Signaling Pathways (37 papers). Ronald T. Hay is often cited by papers focused on Ubiquitin and proteasome pathways (128 papers), Virus-based gene therapy research (44 papers) and NF-κB Signaling Pathways (37 papers). Ronald T. Hay collaborates with scholars based in United Kingdom, United States and France. Ronald T. Hay's co-authors include Manuel S. Rodríguez, Joana Desterro, Ellis Jaffray, Michael H. Tatham, Catherine Dargemont, James R. Matthews, James H. Naismith, David P. Lane, Marie‐Claude Geoffroy and Anna Plechanovová and has published in prestigious journals such as Nature, Cell and Proceedings of the National Academy of Sciences.

In The Last Decade

Ronald T. Hay

247 papers receiving 24.0k citations

Hit Papers

SUMO 1992 2026 2003 2014 2005 1998 1992 2001 2008 400 800 1.2k
What are hit papers?

Hit papers significantly outperform the citation benchmark for their cohort. A paper qualifies if it has ≥500 total citations, achieves ≥1.5× the top-1% citation threshold for papers in the same subfield and year (this is the minimum needed to enter the top 1%, not the average within it), or reaches the top citation threshold in at least one of its specific research topics.

  1. SUMO
    2005 1.4k citations Ronald T. Hay profile →
  2. SUMO-1 Modification of IκBα Inhibits NF-κB Activation
    1998 899 citations Joana Desterro, Manuel S. Rodríguez et al. profile →
  3. Thiordoxin regulates the DNA binding activity of NF-χB by reduction of a disulphid bond involving cysteine 62
    1992 696 citations James R. Matthews, Ronald T. Hay et al. Nucleic Acids Research profile →
  4. Polymeric Chains of SUMO-2 and SUMO-3 Are Conjugated to Protein Substrates by SAE1/SAE2 and Ubc9
    2001 689 citations Michael H. Tatham, Ellis Jaffray et al. Journal of Biological Chemistry profile →
  5. RNF4 is a poly-SUMO-specific E3 ubiquitin ligase required for arsenic-induced PML degradation
    2008 678 citations Michael H. Tatham, Anna Plechanovová et al. profile →
  6. SUMO-1 Conjugation in Vivo Requires Both a Consensus Modification Motif and Nuclear Targeting
    2001 626 citations Manuel S. Rodríguez, Ronald T. Hay et al. Journal of Biological Chemistry profile →
  7. SUMO-1 modification activates the transcriptional response of p53
    1999 541 citations Manuel S. Rodríguez, Joana Desterro et al. The EMBO Journal profile →

Peers — A (Enhanced Table)

Peers by citation overlap · career bar shows stage (early→late) cites · hero ref

Name h Career Trend Papers Cites
Ronald T. Hay United Kingdom 83 19.5k 6.6k 4.4k 4.1k 3.3k 247 24.3k
David Komander United Kingdom 70 19.2k 1.0× 5.4k 0.8× 4.0k 0.9× 3.1k 0.8× 1.6k 0.5× 124 23.0k
David C.S. Huang Australia 82 20.4k 1.0× 6.2k 0.9× 6.7k 1.5× 2.5k 0.6× 1.1k 0.3× 236 28.2k
John L. Cleveland United States 78 14.8k 0.8× 6.8k 1.0× 4.7k 1.1× 3.3k 0.8× 1.2k 0.3× 224 22.7k
Cecile M. Pickart United States 59 16.6k 0.9× 5.0k 0.8× 2.8k 0.6× 2.5k 0.6× 1.8k 0.5× 90 19.4k
Yoshihide Tsujimoto Japan 85 18.8k 1.0× 4.3k 0.6× 4.0k 0.9× 2.4k 0.6× 1.4k 0.4× 184 28.6k
Suzanne Cory Australia 76 23.2k 1.2× 8.0k 1.2× 8.4k 1.9× 3.7k 0.9× 2.6k 0.8× 183 34.3k
Aaron Ciechanover Israel 91 35.5k 1.8× 10.3k 1.6× 4.3k 1.0× 3.7k 0.9× 3.6k 1.1× 294 43.8k
Kunihiro Matsumoto Japan 87 20.1k 1.0× 3.4k 0.5× 6.0k 1.4× 5.4k 1.3× 1.5k 0.4× 233 29.2k
Yue Xiong United States 91 24.3k 1.2× 11.3k 1.7× 2.2k 0.5× 5.4k 1.3× 2.2k 0.7× 254 34.2k
Ulrich Siebenlist United States 73 10.6k 0.5× 4.3k 0.7× 10.5k 2.4× 7.5k 1.8× 1.8k 0.6× 176 22.4k

Countries citing papers authored by Ronald T. Hay

Since Specialization
Citations

This map shows the geographic impact of Ronald T. Hay's research. It shows the number of citations coming from papers published by authors working in each country. You can also color the map by specialization and compare the number of citations received by Ronald T. Hay with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Ronald T. Hay more than expected).

Fields of papers citing papers by Ronald T. Hay

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Ronald T. Hay. Nodes represent research fields, and links connect fields that are likely to share authors. Colored nodes show fields that tend to cite the papers produced by Ronald T. Hay. The network helps show where Ronald T. Hay may publish in the future.

Co-authorship network of co-authors of Ronald T. Hay

This figure shows the co-authorship network connecting the top 25 collaborators of Ronald T. Hay. A scholar is included among the top collaborators of Ronald T. Hay based on the total number of citations received by their joint publications. Widths of edges represent the number of papers authors have co-authored together. Node borders signify the number of papers an author published with Ronald T. Hay. Ronald T. Hay is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

20 of 20 papers shown
1.
Jaffray, Ellis, Michael H. Tatham, Barbara Mojsa, et al.. (2025). PML mutants from arsenic-resistant patients reveal SUMO1-TOPORS and SUMO2/3-RNF4 degradation pathways. The Journal of Cell Biology. 224(6). 1 indexed citations
2.
Nakasone, Mark A., Conner Craigon, Gajanan Sathe, et al.. (2024). Mechanism of degrader-targeted protein ubiquitinability. Science Advances. 10(41). eado6492–eado6492. 25 indexed citations
3.
Ackermann, Leena, Saskia Hoffmann, Ivo A. Hendriks, et al.. (2024). Concerted SUMO-targeted ubiquitin ligase activities of TOPORS and RNF4 are essential for stress management and cell proliferation. Nature Structural & Molecular Biology. 31(9). 1355–1367. 15 indexed citations
4.
Hertz, Emil Peter Thrane, Thomas Kruse, Ivo A. Hendriks, et al.. (2023). The SUMO–NIP45 pathway processes toxic DNA catenanes to prevent mitotic failure. Nature Structural & Molecular Biology. 30(9). 1303–1313. 9 indexed citations
5.
Su, Xue Bessie, Menglu Wang, Olga O. Nerusheva, et al.. (2021). SUMOylation stabilizes sister kinetochore biorientation to allow timely anaphase. The Journal of Cell Biology. 220(7). 11 indexed citations
6.
Larsen, Nicolai Balle, Dimitriya H. Garvanska, Ivo A. Hendriks, et al.. (2021). Mechanism and function of DNA replication‐independent DNA‐protein crosslink repair via the SUMO‐RNF4 pathway. The EMBO Journal. 40(18). e107413–e107413. 45 indexed citations
7.
Branigan, Emma, J. Carlos Penedo, & Ronald T. Hay. (2020). Ubiquitin transfer by a RING E3 ligase occurs from a closed E2~ubiquitin conformation. Nature Communications. 11(1). 2846–2846. 38 indexed citations
8.
Paulus, Christina, Hans Stubbe, Maryam Karimi, et al.. (2020). Viral DNA Binding Protein SUMOylation Promotes PML Nuclear Body Localization Next to Viral Replication Centers. mBio. 11(2). 24 indexed citations
9.
Pelisch, Federico, et al.. (2019). Sumoylation regulates protein dynamics during meiotic chromosome segregation in C. elegans oocytes. Journal of Cell Science. 132(14). 19 indexed citations
10.
MacKay, Craig, et al.. (2014). E3 Ubiquitin Ligase HOIP Attenuates Apoptotic Cell Death Induced by Cisplatin. Cancer Research. 74(8). 2246–2257. 58 indexed citations
11.
Xu, Yingqi, Anna Plechanovová, P. J. Simpson, et al.. (2014). Structural insight into SUMO chain recognition and manipulation by the ubiquitin ligase RNF4. Nature Communications. 5(1). 4217–4217. 38 indexed citations
12.
Lake, Annette, Lesley Shield, Pablo Cordano, et al.. (2009). Mutations of NFKBIA, encoding IκBα, are a recurrent finding in classical Hodgkin lymphoma but are not a unifying feature of non‐EBV‐associated cases. International Journal of Cancer. 125(6). 1334–1342. 60 indexed citations
13.
Frade, Raquel F. M., Tomáš Lébl, Ellis Jaffray, et al.. (2009). Iso‐seco‐tanapartholides: Isolation, Synthesis and Biological Evaluation. European Journal of Organic Chemistry. 2009(33). 5711–5715. 24 indexed citations
14.
Santos, Vera Lúcia Pereira dos, Fernando Ferreira, Rafael M. Costa, et al.. (2008). Conjugation of Human Topoisomerase 2α with Small Ubiquitin-like Modifiers 2/3 in Response to Topoisomerase Inhibitors: Cell Cycle Stage and Chromosome Domain Specificity. Cancer Research. 68(7). 2409–2418. 49 indexed citations
15.
Meinecke, Ingmar, Anja Baier, Marvin Peters, et al.. (2007). Modification of nuclear PML protein by SUMO-1 regulates Fas-induced apoptosis in rheumatoid arthritis synovial fibroblasts. Proceedings of the National Academy of Sciences. 104(12). 5073–5078. 110 indexed citations
16.
Bouras, Toula, Maofu Fu, Anthony A. Sauve, et al.. (2005). SIRT1 Deacetylation and Repression of p300 Involves Lysine Residues 1020/1024 within the Cell Cycle Regulatory Domain 1. Journal of Biological Chemistry. 280(11). 10264–10276. 283 indexed citations
17.
Rodríguez, Manuel S., Joana Desterro, Sonia Laı́n, et al.. (1999). SUMO-1 modification activates the transcriptional response of p53. The EMBO Journal. 18(22). 6455–6461. 541 indexed citations breakdown →
18.
Stark, Lesley A. & Ronald T. Hay. (1998). Human immunodeficiency virus type 1 (HIV-1) viral protein R (Vpr) interacts with Lys-tRNA synthetase. Journal of Virology. 72(4). 1 indexed citations
19.
Matthews, James R., Catherine H. Botting, Maria Panico, Howard R. Morris, & Ronald T. Hay. (1996). Inhibition of NF- B DNA Binding by Nitric Oxide. Nucleic Acids Research. 24(12). 2236–2242. 428 indexed citations
20.
Hay, Ronald T., et al.. (1996). Pyridoxal 5′-Phosphate Inhibition of Adenovirus DNA Polymerase. Journal of Biological Chemistry. 271(39). 24242–24248. 11 indexed citations

Rankless uses publication and citation data sourced from OpenAlex, an open and comprehensive bibliographic database. While OpenAlex provides broad and valuable coverage of the global research landscape, it—like all bibliographic datasets—has inherent limitations. These include incomplete records, variations in author disambiguation, differences in journal indexing, and delays in data updates. As a result, some metrics and network relationships displayed in Rankless may not fully capture the entirety of a scholar's output or impact.

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