J. Symerský

2.5k total citations
47 papers, 2.0k citations indexed

About

J. Symerský is a scholar working on Molecular Biology, Materials Chemistry and Spectroscopy. According to data from OpenAlex, J. Symerský has authored 47 papers receiving a total of 2.0k indexed citations (citations by other indexed papers that have themselves been cited), including 30 papers in Molecular Biology, 10 papers in Materials Chemistry and 9 papers in Spectroscopy. Recurrent topics in J. Symerský's work include Enzyme Structure and Function (9 papers), ATP Synthase and ATPases Research (7 papers) and Mitochondrial Function and Pathology (5 papers). J. Symerský is often cited by papers focused on Enzyme Structure and Function (9 papers), ATP Synthase and ATPases Research (7 papers) and Mitochondrial Function and Pathology (5 papers). J. Symerský collaborates with scholars based in United States, Czechia and China. J. Symerský's co-authors include David M. Mueller, Min Lu, Rongxin Nie, James Mottonen, Dennis E. Danley, Elizabeth J. Goldsmith, Robert D. Gerard, Kieran F. Geoghegan, D. Eric Walters and Martha Radchenko and has published in prestigious journals such as Nature, Science and Proceedings of the National Academy of Sciences.

In The Last Decade

J. Symerský

46 papers receiving 1.9k citations

Peers

J. Symerský
H.T. Wright United States
Richard A. Pauptit United Kingdom
David H. Drewry United States
Scott Cherry United States
M.P. Coles Germany
Dale T. Blankenship United States
Frank J. Schoenen United States
Nir London Israel
Raymond Gilmour United Kingdom
Stephen A. Margosiak United States
H.T. Wright United States
J. Symerský
Citations per year, relative to J. Symerský J. Symerský (= 1×) peers H.T. Wright

Countries citing papers authored by J. Symerský

Since Specialization
Citations

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

Fields of papers citing papers by J. Symerský

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of J. Symerský

This figure shows the co-authorship network connecting the top 25 collaborators of J. Symerský. A scholar is included among the top collaborators of J. Symerský 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 J. Symerský. J. Symerský 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.
Luo, Min, Wenchang Zhou, Hiral Patel, et al.. (2020). Bedaquiline inhibits the yeast and human mitochondrial ATP synthases. Communications Biology. 3(1). 452–452. 40 indexed citations
2.
Wu, Hsin-Hui, J. Symerský, & Min Lu. (2020). Structure and mechanism of a redesigned multidrug transporter from the Major Facilitator Superfamily. Scientific Reports. 10(1). 3949–3949. 11 indexed citations
3.
Wu, Hsin-Hui, J. Symerský, & Min Lu. (2019). Structure of an engineered multidrug transporter MdfA reveals the molecular basis for substrate recognition. Communications Biology. 2(1). 210–210. 14 indexed citations
4.
Srivastava, Anurag P., Min Luo, Wenchang Zhou, et al.. (2018). High-resolution cryo-EM analysis of the yeast ATP synthase in a lipid membrane. Science. 360(6389). 155 indexed citations
5.
Radchenko, Martha, J. Symerský, Rongxin Nie, & Min Lu. (2015). Structural basis for the blockade of MATE multidrug efflux pumps. Nature Communications. 6(1). 7995–7995. 97 indexed citations
6.
Lu, Min, J. Symerský, Martha Radchenko, et al.. (2013). Structures of a Na + -coupled, substrate-bound MATE multidrug transporter. Proceedings of the National Academy of Sciences. 110(6). 2099–2104. 114 indexed citations
7.
Lu, Min, Martha Radchenko, J. Symerský, Rongxin Nie, & Yi Guo. (2013). Structural insights into H+-coupled multidrug extrusion by a MATE transporter. Nature Structural & Molecular Biology. 20(11). 1310–1317. 82 indexed citations
8.
Symerský, J., et al.. (2012). Oligomycin frames a common drug-binding site in the ATP synthase. Proceedings of the National Academy of Sciences. 109(35). 13961–13965. 204 indexed citations
9.
Symerský, J., Vijayakanth Pagadala, Alexander Krah, et al.. (2012). Structure of the c10 ring of the yeast mitochondrial ATP synthase in the open conformation. Nature Structural & Molecular Biology. 19(5). 485–491. 103 indexed citations
10.
Pagadala, Vijayakanth, Luke Vistain, J. Symerský, & David M. Mueller. (2011). Characterization of the mitochondrial ATP synthase from yeast Saccharomyces cerevisae. Journal of Bioenergetics and Biomembranes. 43(4). 333–347. 11 indexed citations
11.
Oh, Kyoung Joon, Pawan Singh, Minji Park, et al.. (2010). Conformational Changes in BAK, a Pore-forming Proapoptotic Bcl-2 Family Member, upon Membrane Insertion and Direct Evidence for the Existence of BH3-BH3 Contact Interface in BAK Homo-oligomers. Journal of Biological Chemistry. 285(37). 28924–28937. 79 indexed citations
12.
Symerský, J., et al.. (2010). Crystal Structures of Mutant Forms of the Yeast F1 ATPase Reveal Two Modes of Uncoupling. Journal of Biological Chemistry. 285(47). 36561–36569. 16 indexed citations
13.
Nishiyama, Yasuhiro, Stephanie Planque, Yukie Mitsuda, et al.. (2009). Toward Effective HIV Vaccination. Journal of Biological Chemistry. 284(44). 30627–30642. 13 indexed citations
14.
Taguchi, Hiroaki, Stephanie Planque, Yasuhiro Nishiyama, et al.. (2007). Autoantibody-catalyzed Hydrolysis of Amyloid β Peptide. Journal of Biological Chemistry. 283(8). 4714–4722. 68 indexed citations
15.
Vassylyev, Dmitry G. & J. Symerský. (2007). Crystal Structure of Pyruvate Dehydrogenase Phosphatase 1 and its Functional Implications. Journal of Molecular Biology. 370(3). 417–426. 39 indexed citations
16.
Symerský, J., Anna Perederina, Marina N. Vassylyeva, et al.. (2005). Regulation through the RNA Polymerase Secondary Channel. Journal of Biological Chemistry. 281(3). 1309–1312. 37 indexed citations
17.
Symerský, J., et al.. (2003). Structural genomics of Caenorhabditis elegans: Structure of dihydropteridine reductase. Proteins Structure Function and Bioinformatics. 53(4). 944–946. 2 indexed citations
18.
Devedjiev, Y., J. Symerský, Raj Singh, et al.. (2001). Stabilization of active-site loops in NH3-dependent NAD+synthetase fromBacillus subtilis. Acta Crystallographica Section D Biological Crystallography. 57(6). 806–812. 24 indexed citations
19.
Symerský, J., Joseph M. Patti, Mike Carson, et al.. (1997). Structure of the collagen-binding domain from a Staphylococcus aureus adhesin. Nature Structural Biology. 4(10). 833–838. 124 indexed citations
20.
Hossain, M. Belal, et al.. (1993). Structure of 1-{4-[2-(diethylamino)ethoxy]phenyl}-2-(4-methoxyphenyl)-1-phenylethan-1-ol, the non-steroidal antiestrogen MER25. Acta Crystallographica Section C Crystal Structure Communications. 49(3). 500–504.

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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