T.M. Iverson

8.0k total citations · 1 hit paper
89 papers, 6.2k citations indexed

About

T.M. Iverson is a scholar working on Molecular Biology, Materials Chemistry and Cellular and Molecular Neuroscience. According to data from OpenAlex, T.M. Iverson has authored 89 papers receiving a total of 6.2k indexed citations (citations by other indexed papers that have themselves been cited), including 78 papers in Molecular Biology, 17 papers in Materials Chemistry and 12 papers in Cellular and Molecular Neuroscience. Recurrent topics in T.M. Iverson's work include Receptor Mechanisms and Signaling (25 papers), Enzyme Structure and Function (16 papers) and Photosynthetic Processes and Mechanisms (16 papers). T.M. Iverson is often cited by papers focused on Receptor Mechanisms and Signaling (25 papers), Enzyme Structure and Function (16 papers) and Photosynthetic Processes and Mechanisms (16 papers). T.M. Iverson collaborates with scholars based in United States, United Kingdom and Egypt. T.M. Iverson's co-authors include So Iwata, James Barber, Karim Maghlaoui, Gary Cecchini, Douglas C. Rees, C. Luna-Chavez, Catherine L. Drennan, Javier Seravalli, Stephen W. Ragsdale and Tzanko Doukov and has published in prestigious journals such as Nature, Science and Proceedings of the National Academy of Sciences.

In The Last Decade

T.M. Iverson

87 papers receiving 6.2k citations

Hit Papers

Architecture of the Photosynthetic Oxygen-Evolving Center 2004 2026 2011 2018 2004 500 1000 1.5k 2.0k 2.5k

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
T.M. Iverson United States 32 4.3k 1.3k 1.1k 1.1k 1.0k 89 6.2k
Bernhard Loll Germany 32 4.1k 1.0× 1.0k 0.8× 1.1k 1.0× 950 0.9× 961 0.9× 107 5.6k
Kyoko Shinzawa‐Itoh Japan 39 6.3k 1.5× 423 0.3× 1.8k 1.7× 965 0.9× 1.0k 1.0× 110 7.6k
M. R. Gunner United States 42 5.1k 1.2× 1.1k 0.9× 1.5k 1.4× 1.4k 1.3× 356 0.3× 100 6.9k
Shinya Yoshikawa Japan 42 6.9k 1.6× 528 0.4× 2.2k 2.0× 1.1k 1.0× 1.2k 1.2× 165 8.9k
Kunio Hirata Japan 44 3.7k 0.9× 394 0.3× 1.4k 1.3× 1.1k 1.1× 360 0.3× 117 5.8k
Bernd Ludwig Germany 42 6.6k 1.5× 577 0.4× 1.8k 1.7× 804 0.8× 798 0.8× 175 7.8k
Genji Kurisu Japan 36 3.5k 0.8× 961 0.7× 469 0.4× 602 0.6× 545 0.5× 152 4.7k
Terrance E. Meyer United States 39 3.5k 0.8× 960 0.7× 1.1k 1.0× 704 0.7× 595 0.6× 135 4.9k
Edward A. Berry United States 34 4.2k 1.0× 606 0.5× 445 0.4× 575 0.5× 633 0.6× 65 5.5k
Ville R. I. Kaila Germany 41 3.3k 0.8× 439 0.3× 1.1k 1.1× 656 0.6× 413 0.4× 119 4.9k

Countries citing papers authored by T.M. Iverson

Since Specialization
Citations

This map shows the geographic impact of T.M. Iverson'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 T.M. Iverson with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites T.M. Iverson more than expected).

Fields of papers citing papers by T.M. Iverson

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by T.M. Iverson. 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 T.M. Iverson. The network helps show where T.M. Iverson may publish in the future.

Co-authorship network of co-authors of T.M. Iverson

This figure shows the co-authorship network connecting the top 25 collaborators of T.M. Iverson. A scholar is included among the top collaborators of T.M. Iverson 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 T.M. Iverson. T.M. Iverson 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.
Singh, Prashant K., Pankaj Sharma, Elena Maklashina, et al.. (2024). CryoEM structures reveal how the bacterial flagellum rotates and switches direction. Nature Microbiology. 9(5). 1271–1281. 20 indexed citations
2.
Minko, Irina G., Pankaj Sharma, Lei Li, et al.. (2023). Base excision repair of the N-(2-deoxy-d-erythro-pentofuranosyl)-urea lesion by the hNEIL1 glycosylase. Nucleic Acids Research. 51(8). 3754–3769. 9 indexed citations
3.
Bensing, Barbara A., Rupesh Agarwal, Kemal Solakyildirim, et al.. (2022). Origins of glycan selectivity in streptococcal Siglec-like adhesins suggest mechanisms of receptor adaptation. Nature Communications. 13(1). 2753–2753. 9 indexed citations
4.
Maklashina, Elena, T.M. Iverson, & Gary Cecchini. (2022). How an assembly factor enhances covalent FAD attachment to the flavoprotein subunit of complex II. Journal of Biological Chemistry. 298(10). 102472–102472. 7 indexed citations
5.
Qu, Changxiu, Ji Young Park, Qing‐tao He, et al.. (2021). Scaffolding mechanism of arrestin-2 in the cRaf/MEK1/ERK signaling cascade. Proceedings of the National Academy of Sciences. 118(37). 38 indexed citations
6.
Kaya, Ali İ., Nicole A. Perry, Vsevolod V. Gurevich, & T.M. Iverson. (2020). Phosphorylation barcode-dependent signal bias of the dopamine D1 receptor. Proceedings of the National Academy of Sciences. 117(25). 14139–14149. 45 indexed citations
7.
Chen, Qiuyan, Ya Zhuo, Pankaj Sharma, et al.. (2020). An Eight Amino Acid Segment Controls Oligomerization and Preferred Conformation of the two Non-visual Arrestins. Journal of Molecular Biology. 433(4). 166790–166790. 19 indexed citations
8.
Spraggins, Jeffrey M., et al.. (2020). Methyltransferase Contingencies in the Pathway of Everninomicin D Antibiotics and Analogues. ChemBioChem. 21(23). 3349–3358. 5 indexed citations
9.
Bensing, Barbara A., Pankaj Sharma, Hai Yu, et al.. (2020). Tandem sialoglycan-binding modules in a Streptococcus sanguinis serine-rich repeat adhesin create target dependent avidity effects. Journal of Biological Chemistry. 295(43). 14737–14749. 4 indexed citations
10.
Chen, Qiuyan, T.M. Iverson, & Vsevolod V. Gurevich. (2018). Structural Basis of Arrestin-Dependent Signal Transduction. Trends in Biochemical Sciences. 43(6). 412–423. 60 indexed citations
11.
Chen, Qiuyan, Nicole A. Perry, Sergey A. Vishnivetskiy, et al.. (2017). Structural basis of arrestin-3 activation and signaling. Nature Communications. 8(1). 1427–1427. 92 indexed citations
12.
Seo, Ho Seong, G. Minasov, Ravin Seepersaud, et al.. (2013). Characterization of Fibrinogen Binding by Glycoproteins Srr1 and Srr2 of Streptococcus agalactiae. Journal of Biological Chemistry. 288(50). 35982–35996. 81 indexed citations
13.
Iverson, T.M.. (2012). Catalytic mechanisms of complex II enzymes: A structural perspective. Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1827(5). 648–657. 63 indexed citations
14.
Kaya, Ali İ., Tarjani Thaker, Anita M. Preininger, T.M. Iverson, & Heidi E. Hamm. (2011). Coupling Efficiency of Rhodopsin and Transducin in Bicelles. Biochemistry. 50(15). 3193–3203. 24 indexed citations
15.
Tomasiak, Thomas, Tara L. Archuleta, Juni Andréll, et al.. (2010). Geometric Restraint Drives On- and Off-pathway Catalysis by the Escherichia coli Menaquinol:Fumarate Reductase. Journal of Biological Chemistry. 286(4). 3047–3056. 21 indexed citations
16.
Cogan, Joy D., John A. Phillips, Nathalie Schnetz‐Boutaud, et al.. (2008). Inherited human cPLA2α deficiency is associated with impaired eicosanoid biosynthesis, small intestinal ulceration, and platelet dysfunction. Journal of Clinical Investigation. 118(6). 2121–31. 100 indexed citations
17.
Maklashina, Elena, T.M. Iverson, Juni Andréll, et al.. (2006). Fumarate Reductase and Succinate Oxidase Activity of Escherichia coli Complex II Homologs Are Perturbed Differently by Mutation of the Flavin Binding Domain. Journal of Biological Chemistry. 281(16). 11357–11365. 49 indexed citations
18.
Iverson, T.M., et al.. (2004). Architecture of the Photosynthetic Oxygen-Evolving Center. Science. 303(5665). 1831–1838. 2704 indexed citations breakdown →
19.
Doukov, Tzanko, T.M. Iverson, Javier Seravalli, Stephen W. Ragsdale, & Catherine L. Drennan. (2002). A Ni-Fe-Cu Center in a Bifunctional Carbon Monoxide Dehydrogenase/ Acetyl-CoA Synthase. Science. 298(5593). 567–572. 434 indexed citations
20.
Iverson, T.M., David M. Arciero, Alan B. Hooper, & Douglas C. Rees. (2001). High-resolution structures of the oxidized and reduced states of cytochrome c554 from Nitrosomonas europaea. JBIC Journal of Biological Inorganic Chemistry. 6(4). 390–397. 35 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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