B.T. Eger

3.3k total citations · 1 hit paper
23 papers, 2.6k citations indexed

About

B.T. Eger is a scholar working on Molecular Biology, Nephrology and Cellular and Molecular Neuroscience. According to data from OpenAlex, B.T. Eger has authored 23 papers receiving a total of 2.6k indexed citations (citations by other indexed papers that have themselves been cited), including 22 papers in Molecular Biology, 11 papers in Nephrology and 4 papers in Cellular and Molecular Neuroscience. Recurrent topics in B.T. Eger's work include Porphyrin Metabolism and Disorders (11 papers), Gout, Hyperuricemia, Uric Acid (11 papers) and Biochemical and Molecular Research (6 papers). B.T. Eger is often cited by papers focused on Porphyrin Metabolism and Disorders (11 papers), Gout, Hyperuricemia, Uric Acid (11 papers) and Biochemical and Molecular Research (6 papers). B.T. Eger collaborates with scholars based in Canada, Japan and United States. B.T. Eger's co-authors include E.F. Pai, Takeshi Nishino, Ken Okamoto, Tomoko Nishino, Cristofer Enroth, Shiro Kondo, Oliver P. Ernst, Jana Broecker, Russ Hille and Koji Matsumoto and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Journal of Biological Chemistry.

In The Last Decade

B.T. Eger

23 papers receiving 2.5k citations

Hit Papers

align trajectories

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.

Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: Structure-based mechanism of conversion

2000 575 citations Cristofer Enroth, B.T. Eger et al. Proceedings of the National Academy of Sciences profile →

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
B.T. Eger Canada	21	1.6k	967	332	261	241	23	2.6k
Takanori Kumagai Japan	28	1.2k 0.7×	304 0.3×	24 0.1×	66 0.3×	51 0.2×	87	2.6k
Raj Kumar India	37	1.6k 1.0×	284 0.3×	32 0.1×	88 0.3×	196 0.8×	121	4.5k
Hirofumi Nakano Japan	26	1.6k 1.0×	132 0.1×	10 0.0×	42 0.2×	72 0.3×	140	3.1k
Shiho Ohnishi Japan	21	845 0.5×	26 0.0×	73 0.2×	32 0.1×	90 0.4×	42	1.8k
Monica Galliano Italy	29	2.3k 1.4×	80 0.1×	13 0.0×	59 0.2×	97 0.4×	103	3.1k
Jian Zhang China	33	1.3k 0.8×	38 0.0×	14 0.0×	90 0.3×	165 0.7×	246	4.0k
R. Berni Italy	29	1.8k 1.1×	109 0.1×	21 0.1×	72 0.3×	23 0.1×	80	2.4k
Yuanxin Tian China	27	1.1k 0.7×	194 0.2×	10 0.0×	26 0.1×	187 0.8×	91	2.0k
Jianzhang Wu China	27	1.1k 0.7×	78 0.1×	11 0.0×	30 0.1×	116 0.5×	116	2.3k
Daniela Rossi Italy	30	1.2k 0.8×	242 0.3×	4 0.0×	466 1.8×	82 0.3×	147	2.8k

Countries citing papers authored by B.T. Eger

Since Specialization

Citations

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

Fields of papers citing papers by B.T. Eger

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of B.T. Eger

This figure shows the co-authorship network connecting the top 25 collaborators of B.T. Eger. A scholar is included among the top collaborators of B.T. Eger 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 B.T. Eger. B.T. Eger is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

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20 of 20 papers shown

Sander, Christopher L., B.T. Eger, Hui‐Woog Choe, et al.. (2021). Structural evidence for visual arrestin priming via complexation of phosphoinositols. Structure. 30(2). 263–277.e5. 17 indexed citations

Besaw, Jessica E., Takefumi Morizumi, B.T. Eger, et al.. (2020). The crystal structures of a chloride-pumping microbial rhodopsin and its proton-pumping mutant illuminate proton transfer determinants. Journal of Biological Chemistry. 295(44). 14793–14804. 25 indexed citations

Mabanglo, Mark, Elisa Leung, Siavash Vahidi, et al.. (2019). ClpP protease activation results from the reorganization of the electrostatic interaction networks at the entrance pores. Communications Biology. 2(1). 410–410. 29 indexed citations

Bandyopadhyay, Abhishek, Ned Van Eps, B.T. Eger, et al.. (2018). A Novel Polar Core and Weakly Fixed C-Tail in Squid Arrestin Provide New Insight into Interaction with Rhodopsin. Journal of Molecular Biology. 430(21). 4102–4118. 11 indexed citations

Broecker, Jana, B.T. Eger, & Oliver P. Ernst. (2017). Crystallogenesis of Membrane Proteins Mediated by Polymer-Bounded Lipid Nanodiscs. Biophysical Journal. 112(3). 356a–357a. 29 indexed citations

Broecker, Jana, B.T. Eger, & Oliver P. Ernst. (2017). Crystallogenesis of Membrane Proteins Mediated by Polymer-Bounded Lipid Nanodiscs. Structure. 25(2). 384–392. 120 indexed citations

Goodreid, Jordan D., John Janetzko, John P. Santa Maria, et al.. (2016). Development and Characterization of Potent Cyclic Acyldepsipeptide Analogues with Increased Antimicrobial Activity. Journal of Medicinal Chemistry. 59(2). 624–646. 46 indexed citations

Leung, Elisa, Alessandro Datti, Jordan D. Goodreid, et al.. (2011). Activators of Cylindrical Proteases as Antimicrobials: Identification and Development of Small Molecule Activators of ClpP Protease. Chemistry & Biology. 18(9). 1167–1178. 88 indexed citations

Ishikita, Hiroshi, B.T. Eger, Ken Okamoto, Takeshi Nishino, & E.F. Pai. (2011). Protein Conformational Gating of Enzymatic Activity in Xanthine Oxidoreductase. Journal of the American Chemical Society. 134(2). 999–1009. 49 indexed citations

10.

Okamoto, Ken, Yuko Kawaguchi, B.T. Eger, E.F. Pai, & Takeshi Nishino. (2010). Crystal Structures of Urate Bound Form of Xanthine Oxidoreductase: Substrate Orientation and Structure of the Key Reaction Intermediate. Journal of the American Chemical Society. 132(48). 17080–17083. 40 indexed citations

11.

Okamoto, Ken, B.T. Eger, Tomoko Nishino, E.F. Pai, & Takeshi Nishino. (2008). Mechanism of Inhibition of Xanthine Oxidoreductase by Allopurinol: Crystal Structure of Reduced Bovine Milk Xanthine Oxidoreductase Bound with Oxipurinol. Nucleosides Nucleotides & Nucleic Acids. 27(6-7). 888–893. 104 indexed citations

12.

Nishino, Tomoko, Ken Okamoto, B.T. Eger, E.F. Pai, & Takeshi Nishino. (2008). Mammalian xanthine oxidoreductase – mechanism of transition from xanthine dehydrogenase to xanthine oxidase. FEBS Journal. 275(13). 3278–3289. 295 indexed citations

13.

Nishino, Tomoko, Ken Okamoto, Yuko Kawaguchi, et al.. (2005). Mechanism of the Conversion of Xanthine Dehydrogenase to Xanthine Oxidase. Journal of Biological Chemistry. 280(26). 24888–24894. 124 indexed citations

14.

Fukunari, Atsushi, Ken Okamoto, Takeshi Nishino, et al.. (2004). Y-700 [1-[3-Cyano-4-(2,2-dimethylpropoxy)phenyl]-1 H-pyrazole-4-carboxylic Acid]: A Potent Xanthine Oxidoreductase Inhibitor with Hepatic Excretion. Journal of Pharmacology and Experimental Therapeutics. 311(2). 519–528. 101 indexed citations

15.

Okamoto, Ken, B.T. Eger, Tomoko Nishino, et al.. (2003). An Extremely Potent Inhibitor of Xanthine Oxidoreductase. Journal of Biological Chemistry. 278(3). 1848–1855. 358 indexed citations

16.

Eger, B.T., Ken Okamoto, Cristofer Enroth, et al.. (2000). Purification, crystallization and preliminary X-ray diffraction studies of xanthine dehydrogenase and xanthine oxidase isolated from bovine milk. Acta Crystallographica Section D Biological Crystallography. 56(12). 1656–1658. 28 indexed citations

17.

Enroth, Cristofer, B.T. Eger, Ken Okamoto, et al.. (2000). Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: Structure-based mechanism of conversion. Proceedings of the National Academy of Sciences. 97(20). 10723–10728. 575 indexed citations breakdown →

18.

Stoll, Vincent S., B.T. Eger, Rosemary C. Hynes, et al.. (1998). Differences in Binding Modes of Enantiomers of 1-Acetamido Boronic Acid Based Protease Inhibitors: Crystal Structures of γ-Chymotrypsin and Subtilisin Carlsberg Complexes^,. Biochemistry. 37(2). 451–462. 49 indexed citations

19.

Eger, B.T. & Stephen J. Benkovic. (1992). The minimal kinetic mechanism for misincorporation by DNA polymerase I (Klenow fragment). Biochemistry. 31(38). 9227–9236. 66 indexed citations

20.

Eger, B.T., et al.. (1991). Mechanism of DNA replication fidelity for three mutants of DNA polymerase I: Klenow fragment KF(exo+), KF(polA5), and KF(exo-). Biochemistry. 30(5). 1441–1448. 66 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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