Thomas Dever

16.8k total citations · 5 hit papers
129 papers, 13.1k citations indexed

About

Thomas Dever is a scholar working on Molecular Biology, Cell Biology and Immunology. According to data from OpenAlex, Thomas Dever has authored 129 papers receiving a total of 13.1k indexed citations (citations by other indexed papers that have themselves been cited), including 122 papers in Molecular Biology, 12 papers in Cell Biology and 11 papers in Immunology. Recurrent topics in Thomas Dever's work include RNA and protein synthesis mechanisms (94 papers), RNA Research and Splicing (52 papers) and RNA regulation and disease (43 papers). Thomas Dever is often cited by papers focused on RNA and protein synthesis mechanisms (94 papers), RNA Research and Splicing (52 papers) and RNA regulation and disease (43 papers). Thomas Dever collaborates with scholars based in United States, Canada and Cameroon. Thomas Dever's co-authors include William C. Merrick, Nahum Sonenberg, Alan G. Hinnebusch, Chune Cao, Frank Sicheri, Rachel Green, Byung‐Sik Shin, Manuel J. Glynias, Eric Klann and Arvin C. Dar and has published in prestigious journals such as Nature, Science and Cell.

In The Last Decade

Thomas Dever

127 papers receiving 12.9k citations

Hit Papers

Evidence That Hepatitis C Virus Resistance to Interferon ... 1987 2026 2000 2013 1997 1992 2002 1990 1987 200 400 600

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Thomas Dever United States 62 10.6k 1.6k 1.4k 1.4k 1.2k 129 13.1k
William C. Merrick United States 71 13.9k 1.3× 1.2k 0.7× 1.1k 0.8× 768 0.5× 1.3k 1.1× 179 16.3k
Henry D. Hunt United States 30 7.2k 0.7× 785 0.5× 1.9k 1.4× 1.9k 1.3× 2.0k 1.7× 73 12.1k
Michael R. Green United States 68 15.3k 1.4× 748 0.5× 1.8k 1.3× 1.0k 0.7× 2.4k 2.0× 177 19.2k
John W.B. Hershey United States 72 16.3k 1.5× 1.4k 0.9× 1.2k 0.8× 609 0.4× 2.2k 1.9× 215 18.6k
Jeffrey K. Pullen United States 11 6.9k 0.7× 767 0.5× 1.3k 0.9× 732 0.5× 1.9k 1.5× 14 10.4k
Jack D. Keene United States 63 11.4k 1.1× 425 0.3× 1.4k 1.0× 1.3k 0.9× 1.7k 1.4× 148 14.4k
Nicholas T. Ingolia United States 48 15.1k 1.4× 1.1k 0.7× 1.1k 0.8× 1.1k 0.8× 1.2k 1.0× 89 18.1k
Alan G. Hinnebusch United States 89 23.5k 2.2× 2.7k 1.8× 1.2k 0.9× 1.1k 0.8× 1.5k 1.3× 269 26.3k
M Kozak United States 31 9.7k 0.9× 863 0.6× 1.2k 0.8× 943 0.7× 1.9k 1.6× 35 12.8k
Enno Hartmann Germany 53 9.4k 0.9× 2.6k 1.7× 1.0k 0.7× 775 0.5× 2.3k 1.9× 104 11.4k

Countries citing papers authored by Thomas Dever

Since Specialization
Citations

This map shows the geographic impact of Thomas Dever'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 Thomas Dever with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Thomas Dever more than expected).

Fields of papers citing papers by Thomas Dever

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Thomas Dever. 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 Thomas Dever. The network helps show where Thomas Dever may publish in the future.

Co-authorship network of co-authors of Thomas Dever

This figure shows the co-authorship network connecting the top 25 collaborators of Thomas Dever. A scholar is included among the top collaborators of Thomas Dever 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 Thomas Dever. Thomas Dever 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.
Grosely, Rosslyn, Carlos Alvarado, Ivaylo P. Ivanov, et al.. (2025). eIF1 and eIF5 dynamically control translation start site fidelity. Nature Structural & Molecular Biology. 32(11). 2308–2318. 3 indexed citations
2.
Ivanov, Ivaylo P., et al.. (2025). Conserved +1 translational frameshifting in the Saccharomyces cerevisiae gene encoding YPL034W. Journal of Biological Chemistry. 301(12). 110891–110891.
3.
Shin, Byung‐Sik, et al.. (2023). eEF2 diphthamide modification restrains spurious frameshifting to maintain translational fidelity. Nucleic Acids Research. 51(13). 6899–6913. 10 indexed citations
4.
Dever, Thomas, Ivaylo P. Ivanov, & Alan G. Hinnebusch. (2023). Translational regulation by uORFs and start codon selection stringency. Genes & Development. 37(11-12). 474–489. 65 indexed citations
5.
Ivanov, Ivaylo P., James A. Saba, Chen‐Ming Fan, et al.. (2022). Evolutionarily conserved inhibitory uORFs sensitize Hox mRNA translation to start codon selection stringency. Proceedings of the National Academy of Sciences. 119(9). 30 indexed citations
6.
Lapointe, Christopher P., Rosslyn Grosely, Masaaki Sokabe, et al.. (2022). eIF5B and eIF1A reorient initiator tRNA to allow ribosomal subunit joining. Nature. 607(7917). 185–190. 38 indexed citations
7.
Kotzaeridou, Urania, Sara K. Young, Vanessa Suckow, et al.. (2020). Novel pathogenic EIF2S3 missense variants causing clinically variable MEHMO syndrome with impaired eIF2γ translational function, and literature review. Clinical Genetics. 98(5). 507–514. 10 indexed citations
8.
Wang, Jinfan, Jing Wang, Byung‐Sik Shin, et al.. (2020). Structural basis for the transition from translation initiation to elongation by an 80S-eIF5B complex. Nature Communications. 11(1). 5003–5003. 26 indexed citations
9.
Young, Sara K., et al.. (2019). Suppression of MEHMO Syndrome Mutation in eIF2 by Small Molecule ISRIB. Molecular Cell. 77(4). 875–886.e7. 31 indexed citations
10.
Melnikov, Sergey, J. Mailliot, Byung‐Sik Shin, et al.. (2016). Molecular insights into protein synthesis with proline residues. EMBO Reports. 17(12). 1776–1784. 77 indexed citations
11.
Cao, Chune, Janet M. Young, Chikako Ono, et al.. (2015). Baculovirus protein PK2 subverts eIF2α kinase function by mimicry of its kinase domain C-lobe. Proceedings of the National Academy of Sciences. 112(32). E4364–73. 15 indexed citations
12.
Rojas, Margarito, Anne‐Claude Gingras, & Thomas Dever. (2014). Protein phosphatase PP1/GLC7 interaction domain in yeast eIF2γ bypasses targeting subunit requirement for eIF2α dephosphorylation. Proceedings of the National Academy of Sciences. 111(14). E1344–53. 25 indexed citations
13.
Shin, Byung Sik, et al.. (2011). Structural integrity of α-helix H12 in translation initiation factor eIF5B is critical for 80S complex stability. RNA. 17(4). 687–696. 16 indexed citations
14.
Gárriz, Andrés, Hongfang Qiu, Madhusudan Dey, et al.. (2008). A Network of Hydrophobic Residues Impeding Helix αC Rotation Maintains Latency of Kinase Gcn2, Which Phosphorylates the α Subunit of Translation Initiation Factor 2. Molecular and Cellular Biology. 29(6). 1592–1607. 31 indexed citations
15.
Dever, Thomas, Arvin C. Dar, & Frank Sicheri. (2007). 12 The eIF2α Kinases. Cold Spring Harbor Monograph Archive. 48. 319–344. 4 indexed citations
16.
Shin, Byung‐Sik & Thomas Dever. (2007). Molecular Genetic Structure–Function Analysis of Translation Initiation Factor eIF5B. Methods in enzymology on CD-ROM/Methods in enzymology. 429. 185–201. 12 indexed citations
17.
Hinnebusch, Alan G., Thomas Dever, & Katsura Asano. (2007). 9 Mechanism of Translation Initiation in the Yeast Saccharomyces cerevisiae. Cold Spring Harbor Monograph Archive. 48. 225–268. 54 indexed citations
18.
Shin, Byung‐Sik, et al.. (2006). Intragenic Suppressor Mutations Restore GTPase and Translation Functions of a Eukaryotic Initiation Factor 5B Switch II Mutant. Molecular and Cellular Biology. 27(5). 1677–1685. 11 indexed citations
19.
Gale, Michael, Marcus J. Korth, Norina Tang, et al.. (1997). Evidence That Hepatitis C Virus Resistance to Interferon Is Mediated through Repression of the PKR Protein Kinase by the Nonstructural 5A Protein. Virology. 230(2). 217–227. 670 indexed citations breakdown →
20.
Anthony, Donald D., et al.. (1986). Affinity labeling of protein synthesis factors. Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States). 46(21). 8836–42. 1 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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