Robert T. Szerencsei

1.6k total citations
46 papers, 1.2k citations indexed

About

Robert T. Szerencsei is a scholar working on Molecular Biology, Cellular and Molecular Neuroscience and Cell Biology. According to data from OpenAlex, Robert T. Szerencsei has authored 46 papers receiving a total of 1.2k indexed citations (citations by other indexed papers that have themselves been cited), including 42 papers in Molecular Biology, 25 papers in Cellular and Molecular Neuroscience and 9 papers in Cell Biology. Recurrent topics in Robert T. Szerencsei's work include Retinal Development and Disorders (29 papers), Photoreceptor and optogenetics research (20 papers) and Ion channel regulation and function (10 papers). Robert T. Szerencsei is often cited by papers focused on Retinal Development and Disorders (29 papers), Photoreceptor and optogenetics research (20 papers) and Ion channel regulation and function (10 papers). Robert T. Szerencsei collaborates with scholars based in Canada, United States and United Kingdom. Robert T. Szerencsei's co-authors include Paul P. M. Schnetkamp, Robert J. Winkfein, KyeongJin Kang, Clemens Prinsen, Xibao Li, Joseph E. Tucker, Rebecca S. Ginger, Martin R. Green, Nansi Jo Colley and Tatiana P. Rogasevskaia and has published in prestigious journals such as Journal of Biological Chemistry, Journal of Neuroscience and The Journal of Cell Biology.

In The Last Decade

Robert T. Szerencsei

46 papers receiving 1.2k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Robert T. Szerencsei Canada 22 987 586 246 240 163 46 1.2k
Larisa Tsavaler United States 8 670 0.7× 369 0.6× 369 1.5× 159 0.7× 401 2.5× 9 1.2k
Lee P. Haynes United Kingdom 22 953 1.0× 493 0.8× 536 2.2× 62 0.3× 286 1.8× 37 1.5k
Salvador Viniegra Spain 25 1.3k 1.3× 493 0.8× 755 3.1× 17 0.1× 28 0.2× 56 1.6k
A.G. Filoteo United States 13 1.2k 1.2× 298 0.5× 232 0.9× 90 0.4× 95 0.6× 14 1.4k
T R Cheek United Kingdom 19 1.0k 1.1× 730 1.2× 313 1.3× 29 0.1× 149 0.9× 25 1.5k
Neil R. Brandt United States 22 1.4k 1.4× 456 0.8× 325 1.3× 29 0.1× 159 1.0× 41 1.6k
Stefano Longoni Switzerland 11 1.1k 1.1× 374 0.6× 112 0.5× 46 0.2× 41 0.3× 13 1.2k
Igor V. Peshenko United States 29 2.0k 2.0× 923 1.6× 242 1.0× 107 0.4× 35 0.2× 63 2.1k
A Ferroni Italy 17 1.1k 1.1× 734 1.3× 49 0.2× 22 0.1× 42 0.3× 49 1.4k
Michael G. Erickson United States 8 1.0k 1.0× 606 1.0× 162 0.7× 19 0.1× 103 0.6× 9 1.2k

Countries citing papers authored by Robert T. Szerencsei

Since Specialization
Citations

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

Fields of papers citing papers by Robert T. Szerencsei

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Robert T. Szerencsei

This figure shows the co-authorship network connecting the top 25 collaborators of Robert T. Szerencsei. A scholar is included among the top collaborators of Robert T. Szerencsei 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 Robert T. Szerencsei. Robert T. Szerencsei 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.
Szerencsei, Robert T., et al.. (2019). Structure-function relationships of K+-dependent Na+/Ca2+ exchangers (NCKX). Cell Calcium. 86. 102153–102153. 14 indexed citations
2.
Cai, Shitian, et al.. (2018). Residues important for K+ ion transport in the K+-dependent Na+-Ca2+ exchanger (NCKX2). Cell Calcium. 74. 61–72. 8 indexed citations
3.
Kondo, Colleen, Robert B. Clark, Darrell D. Belke, et al.. (2018). ATP triggers a robust intracellular [Ca 2+ ]‐mediated signalling pathway in human synovial fibroblasts. Experimental Physiology. 103(8). 1101–1122. 5 indexed citations
4.
Liu, Guohong, et al.. (2018). Residues important for Ca2+ ion transport in the neuronal K+-dependent Na+-Ca2+ exchanger (NCKX2). Cell Calcium. 74. 187–197. 7 indexed citations
5.
Rogasevskaia, Tatiana P., et al.. (2016). A Functional Study of Mutations in K+-dependent Na+-Ca2+ Exchangers Associated with Amelogenesis Imperfecta and Non-syndromic Oculocutaneous Albinism. Journal of Biological Chemistry. 291(25). 13113–13123. 19 indexed citations
6.
Szerencsei, Robert T., et al.. (2015). Cation dependencies and turnover rates of the human K+-dependent Na+-Ca2+ exchangers NCKX1, NCKX2, NCKX3 and NCKX4. Cell Calcium. 59(1). 1–11. 24 indexed citations
7.
Szerencsei, Robert T., et al.. (2013). The topology of the C-terminal sections of the NCX1 Na+/Ca2+exchanger and the NCKX2 Na+/Ca2+-K+exchanger. Channels. 7(2). 109–114. 22 indexed citations
8.
Shibukawa, Yukinao, KyeongJin Kang, Robert T. Szerencsei, et al.. (2007). Structure–Function Relationships of the NCKX2 Na+/Ca2+‐K+ Exchanger. Annals of the New York Academy of Sciences. 1099(1). 16–28. 7 indexed citations
9.
Shibukawa, Yoshiyuki, KyeongJin Kang, Robert T. Szerencsei, Takashi Suzuki, & Paul P. M. Schnetkamp. (2005). Substitution of a Single Residue, Asp575, Renders the NCKX2 K+-dependent Na+/Ca2+Exchanger Independent of K+. 2 indexed citations
10.
Kang, KyeongJin, et al.. (2005). Site-Directed Disulfide Mapping of Residues Contributing to the Ca2+ and K+ Binding Pocket of the NCKX2 Na+/Ca2+-K+ Exchanger. Biochemistry. 44(21). 7787–7795. 15 indexed citations
11.
Winkfein, Robert J., Bret J. Pearson, R. Matthew Ward, et al.. (2004). Molecular characterization, functional expression and tissue distribution of a second NCKX Na+/Ca2+-K+ exchanger from Drosophila. Cell Calcium. 36(2). 147–155. 13 indexed citations
12.
Kang, KyeongJin, et al.. (2004). Residues Contributing to the Ca2+ and K+ Binding Pocket of the NCKX2 Na+/Ca2+-K+ Exchanger. Journal of Biological Chemistry. 280(8). 6823–6833. 34 indexed citations
13.
Szerencsei, Robert T., et al.. (2003). Topology of the Retinal Cone NCKX2 Na/Ca−K Exchanger. Biochemistry. 42(8). 2485–2491. 38 indexed citations
14.
Szerencsei, Robert T., et al.. (2002). The Na/Ca‐K Exchanger Gene Family. Annals of the New York Academy of Sciences. 976(1). 41–52. 10 indexed citations
15.
Pearson, Bret J., et al.. (2002). Potassium‐Dependent Sodium‐Calcium Exchange through the Eye of the Fly. Annals of the New York Academy of Sciences. 976(1). 300–314. 8 indexed citations
16.
Szerencsei, Robert T., et al.. (2000). [56] Spectrofluorometric detection of exchange. Methods in enzymology on CD-ROM/Methods in enzymology. 315. 847–864. 10 indexed citations
18.
Schnetkamp, Paul P. M., et al.. (1991). The Stoichiometry or Na ‐ Ca + K Exchange in Rod Outer Segments Isolated from Bovine Retinasa. Annals of the New York Academy of Sciences. 639(1). 10–21. 13 indexed citations
19.
Schnetkamp, Paul P. M., et al.. (1991). Unidirectional Na+, Ca2+, and K+ fluxes through the bovine rod outer segment Na-Ca-K exchanger.. Journal of Biological Chemistry. 266(1). 198–206. 39 indexed citations
20.
Schnetkamp, Paul P. M. & Robert T. Szerencsei. (1989). Silver ions induce a rapid Ca2+ release from isolated intact bovine rod outer segments by a cooperative mechanism. The Journal of Membrane Biology. 108(1). 91–102. 8 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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