Thomas B. Thompson

5.2k total citations
95 papers, 3.9k citations indexed

About

Thomas B. Thompson is a scholar working on Molecular Biology, Genetics and Rheumatology. According to data from OpenAlex, Thomas B. Thompson has authored 95 papers receiving a total of 3.9k indexed citations (citations by other indexed papers that have themselves been cited), including 72 papers in Molecular Biology, 16 papers in Genetics and 13 papers in Rheumatology. Recurrent topics in Thomas B. Thompson's work include TGF-β signaling in diseases (31 papers), Muscle Physiology and Disorders (20 papers) and Genetic Syndromes and Imprinting (11 papers). Thomas B. Thompson is often cited by papers focused on TGF-β signaling in diseases (31 papers), Muscle Physiology and Disorders (20 papers) and Genetic Syndromes and Imprinting (11 papers). Thomas B. Thompson collaborates with scholars based in United States, Canada and Australia. Thomas B. Thompson's co-authors include W. Sean Davidson, Theodore S. Jardetzky, Chandramohan Kattamuri, Merlin G. Butler, Robert W. Cook, Teresa K. Woodruff, Irene D. Feurer, Ivan Rayment, Kristof Nolan and Ryan G. Walker and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and Nature Communications.

In The Last Decade

Thomas B. Thompson

92 papers receiving 3.8k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Thomas B. Thompson United States 35 2.5k 772 452 407 378 95 3.9k
Hua Pan United States 37 2.7k 1.1× 459 0.6× 226 0.5× 791 1.9× 383 1.0× 160 4.7k
Hong‐Wei Sun United States 46 3.9k 1.6× 715 0.9× 350 0.8× 237 0.6× 384 1.0× 141 9.0k
Alexandre Montpetit Canada 33 1.4k 0.6× 897 1.2× 243 0.5× 160 0.4× 219 0.6× 66 3.5k
Ruti Parvari Israel 28 1.2k 0.5× 831 1.1× 458 1.0× 177 0.4× 196 0.5× 88 2.7k
Mustafa A. Salih Saudi Arabia 37 2.8k 1.1× 1.0k 1.3× 219 0.5× 216 0.5× 338 0.9× 235 5.2k
Siu Yuen Chan Hong Kong 32 1.4k 0.6× 712 0.9× 166 0.4× 404 1.0× 292 0.8× 99 3.5k
Shinji Fushiki Japan 44 2.4k 1.0× 748 1.0× 179 0.4× 193 0.5× 357 0.9× 198 6.3k
Ian Carr United Kingdom 32 1.7k 0.7× 908 1.2× 423 0.9× 182 0.4× 138 0.4× 111 3.5k
João Bosco Pesquero Brazil 40 1.7k 0.7× 358 0.5× 276 0.6× 312 0.8× 274 0.7× 255 5.5k
Michèl A.A.P. Willemsen Netherlands 41 2.8k 1.1× 1.3k 1.7× 396 0.9× 153 0.4× 393 1.0× 199 5.7k

Countries citing papers authored by Thomas B. Thompson

Since Specialization
Citations

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

Fields of papers citing papers by Thomas B. Thompson

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Thomas B. Thompson

This figure shows the co-authorship network connecting the top 25 collaborators of Thomas B. Thompson. A scholar is included among the top collaborators of Thomas B. Thompson 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 B. Thompson. Thomas B. Thompson 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.
Howard, J. A., Richard L. Cate, Nicholas Nagykery, et al.. (2025). A divergent two-domain structure of the anti-Müllerian hormone prodomain. Proceedings of the National Academy of Sciences. 122(3). e2418088122–e2418088122.
2.
Luan, Yi, et al.. (2025). Pancreatic Damage in Ovarian Cancer–Associated Cachexia Is Driven by Activin A Signalling. Journal of Cachexia Sarcopenia and Muscle. 16(5). e70096–e70096.
3.
Walker, Ryan G., Ana Vujić, Kathleen A. Messemer, et al.. (2023). Functional substitutions of amino acids that differ between GDF11 and GDF8 impact skeletal development and skeletal muscle. Life Science Alliance. 6(3). e202201662–e202201662. 6 indexed citations
4.
Briley, Shawn M., et al.. (2021). Deletion of Gremlin-2 alters estrous cyclicity and disrupts female fertility in mice. Biology of Reproduction. 105(5). 1205–1220. 10 indexed citations
5.
Nagykery, Nicholas, Kelly L. Walton, Craig A. Harrison, et al.. (2021). Structure of AMH bound to AMHR2 provides insight into a unique signaling pair in the TGF-β family. Proceedings of the National Academy of Sciences. 118(26). 32 indexed citations
7.
Liu, Min, et al.. (2019). Functional recombinant apolipoprotein A5 that is stable at high concentrations at physiological pH. Journal of Lipid Research. 61(2). 244–251. 2 indexed citations
8.
Walker, Ryan G., Magdalena Czepnik, Adam Hagg, et al.. (2018). Molecular characterization of latent GDF8 reveals mechanisms of activation. Proceedings of the National Academy of Sciences. 115(5). E866–E875. 29 indexed citations
9.
Cotton, Thomas R., Gerhard W. Fischer, Xuelu Wang, et al.. (2018). Structure of the human myostatin precursor and determinants of growth factor latency. The EMBO Journal. 37(3). 367–383. 49 indexed citations
10.
Walker, Ryan G., Magdalena Czepnik, Erich J. Goebel, et al.. (2017). Structural basis for potency differences between GDF8 and GDF11. BMC Biology. 15(1). 19–19. 83 indexed citations
11.
Melchior, John, Ryan G. Walker, Jamie Morris, et al.. (2017). A consensus model of human apolipoprotein A-I in its monomeric and lipid-free state. Nature Structural & Molecular Biology. 24(12). 1093–1099. 52 indexed citations
12.
Nolan, Kristof, Chandramohan Kattamuri, Scott A. Rankin, et al.. (2016). Structure of Gremlin-2 in Complex with GDF5 Gives Insight into DAN-Family-Mediated BMP Antagonism. Cell Reports. 16(8). 2077–2086. 37 indexed citations
13.
Walker, Ryan G., Xiaodi Deng, John Melchior, et al.. (2014). The Structure of Human Apolipoprotein A-IV as Revealed by Stable Isotope-assisted Cross-linking, Molecular Dynamics, and Small Angle X-ray Scattering. Journal of Biological Chemistry. 289(9). 5596–5608. 25 indexed citations
14.
Rodgers, Buel D., et al.. (2014). Myostatin Stimulates, Not Inihibits, C2C12 Myoblast Proliferation. Endocrinology. 155(3). 670–675. 37 indexed citations
16.
Kattamuri, Chandramohan, Kristof Nolan, Scott A. Rankin, et al.. (2012). Members of the DAN Family Are BMP Antagonists That Form Highly Stable Noncovalent Dimers. Journal of Molecular Biology. 424(5). 313–327. 44 indexed citations
17.
Syed, Khajamohiddin, Chandramohan Kattamuri, Thomas B. Thompson, & Jagjit S. Yadav. (2011). Cytochrome b5 reductase–cytochrome b5 as an active P450 redox enzyme system in Phanerochaete chrysosporium: Atypical properties and in vivo evidence of electron transfer capability to CYP63A2. Archives of Biochemistry and Biophysics. 509(1). 26–32. 30 indexed citations
18.
Cash, Jennifer N., Elizabeth Angerman, Chandramohan Kattamuri, et al.. (2011). Structure of Myostatin·Follistatin-like 3. Journal of Biological Chemistry. 287(2). 1043–1053. 66 indexed citations
19.
Thompson, Thomas B., Thomas F. Lerch, Robert W. Cook, Teresa K. Woodruff, & Theodore S. Jardetzky. (2005). The Structure of the Follistatin:Activin Complex Reveals Antagonism of Both Type I and Type II Receptor Binding. Developmental Cell. 9(4). 535–543. 231 indexed citations
20.
Thompson, Thomas B., Kinya Katayama, Kenji Watanabe, C. Richard Hutchinson, & Ivan Rayment. (2004). Structural and Functional Analysis of Tetracenomycin F2 Cyclase from Streptomyces glaucescens. Journal of Biological Chemistry. 279(36). 37956–37963. 48 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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