S. Turley

3.7k total citations
43 papers, 2.9k citations indexed

About

S. Turley is a scholar working on Molecular Biology, Epidemiology and Biochemistry. According to data from OpenAlex, S. Turley has authored 43 papers receiving a total of 2.9k indexed citations (citations by other indexed papers that have themselves been cited), including 23 papers in Molecular Biology, 8 papers in Epidemiology and 7 papers in Biochemistry. Recurrent topics in S. Turley's work include Biochemical and Molecular Research (7 papers), Trypanosoma species research and implications (7 papers) and Enzyme Structure and Function (6 papers). S. Turley is often cited by papers focused on Biochemical and Molecular Research (7 papers), Trypanosoma species research and implications (7 papers) and Enzyme Structure and Function (6 papers). S. Turley collaborates with scholars based in United States, Belgium and Japan. S. Turley's co-authors include Elinor T. Adman, Wim G. J. Hol, M.E.P. Murphy, Larry C. Sieker, Jean LeGall, Arnthór Aevarsson, W. J. Payne, Rachada Sirawaraporn, D.C. Teller and Worachart Sirawaraporn and has published in prestigious journals such as Science, Proceedings of the National Academy of Sciences and Journal of Biological Chemistry.

In The Last Decade

S. Turley

43 papers receiving 2.8k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
S. Turley United States 27 1.7k 500 486 450 324 43 2.9k
Hsiu‐Ju Chiu United States 20 1.2k 0.7× 350 0.7× 511 1.1× 290 0.6× 145 0.4× 37 2.2k
S.V. Antonyuk United Kingdom 36 2.0k 1.2× 817 1.6× 825 1.7× 431 1.0× 311 1.0× 106 4.3k
Keiichi Fukuyama Japan 39 3.0k 1.8× 796 1.6× 766 1.6× 1.1k 2.4× 356 1.1× 200 4.9k
Vilmos Fülöp United Kingdom 35 2.5k 1.5× 607 1.2× 644 1.3× 221 0.5× 211 0.7× 120 4.7k
Edward A. Berry United States 34 4.2k 2.5× 633 1.3× 575 1.2× 606 1.3× 98 0.3× 65 5.5k
Julian C. Rutherford United Kingdom 21 1.6k 1.0× 181 0.4× 270 0.6× 280 0.6× 90 0.3× 25 3.2k
George D. Markham United States 37 2.7k 1.6× 251 0.5× 679 1.4× 117 0.3× 424 1.3× 112 4.0k
Ryosuke Nakashima Japan 17 4.1k 2.5× 632 1.3× 610 1.3× 265 0.6× 74 0.2× 45 6.3k
Matthew M. Benning United States 28 2.8k 1.6× 405 0.8× 775 1.6× 166 0.4× 140 0.4× 45 4.6k
P Aisen United States 28 1.6k 0.9× 440 0.9× 294 0.6× 167 0.4× 76 0.2× 51 4.3k

Countries citing papers authored by S. Turley

Since Specialization
Citations

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

Fields of papers citing papers by S. Turley

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of S. Turley

This figure shows the co-authorship network connecting the top 25 collaborators of S. Turley. A scholar is included among the top collaborators of S. Turley 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 S. Turley. S. Turley 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.
Barros-Álvarez, Ximena, Cho Yeow Koh, S. Turley, et al.. (2017). Leishmania donovani tyrosyl-tRNA synthetase structure in complex with a tyrosyl adenylate analog and comparisons with human and protozoan counterparts. Biochimie. 138. 124–136. 13 indexed citations
2.
Turley, S., Young‐Jun Park, Kelly K. Lee, et al.. (2013). Hexamers of the Type II Secretion ATPase GspE from Vibrio cholerae with Increased ATPase Activity. Structure. 21(9). 1707–1717. 47 indexed citations
3.
Turley, S., Els Pardon, Jan Steyaert, et al.. (2013). The structure of the D3 domain of Plasmodium falciparum myosin tail interacting protein MTIP in complex with a nanobody. Molecular and Biochemical Parasitology. 190(2). 87–91. 15 indexed citations
4.
Korotkov, Konstantin V., Tanya L. Johnson, Michael G. Jobling, et al.. (2011). Structural and Functional Studies on the Interaction of GspC and GspD in the Type II Secretion System. PLoS Pathogens. 7(9). e1002228–e1002228. 78 indexed citations
5.
Korotkov, Konstantin V., et al.. (2009). Calcium Is Essential for the Major Pseudopilin in the Type 2 Secretion System. Journal of Biological Chemistry. 284(38). 25466–25470. 41 indexed citations
6.
Bosch, Jürgen, S. Turley, Thomas M. Daly, et al.. (2006). Structure of the MTIP–MyoA complex, a key component of the malaria parasite invasion motor. Proceedings of the National Academy of Sciences. 103(13). 4852–4857. 57 indexed citations
7.
Hol, Wim G. J., Janice Deng, Jan Abendroth, et al.. (2005). Molecular machines and tropical pathogens. Acta Crystallographica Section A Foundations of Crystallography. 61(a1). c93–c93. 1 indexed citations
8.
Deng, Junpeng, Nancy Lewis Ernst, S. Turley, Kenneth Stuart, & Wim G. J. Hol. (2005). Structural basis for UTP specificity of RNA editing TUTases from Trypanosoma brucei. The EMBO Journal. 24(23). 4007–4017. 67 indexed citations
9.
Robien, M.A., Kiet T. Nguyen, Abhinav Kumar, et al.. (2004). An improved crystal form of Plasmodium falciparum peptide deformylase. Protein Science. 13(4). 1155–1163. 21 indexed citations
10.
Martinez, Sergio E., Albert Y. Wu, Natalie A. Glavas, et al.. (2002). The two GAF domains in phosphodiesterase 2A have distinct roles in dimerization and in cGMP binding. Proceedings of the National Academy of Sciences. 99(20). 13260–13265. 206 indexed citations
11.
Kumar, Abhinav, et al.. (2002). Crystals of Peptide Deformylase from Plasmodium falciparum Reveal Critical Characteristics of the Active Site for Drug Design. Structure. 10(3). 357–367. 37 indexed citations
12.
Kumar, Abhinav, et al.. (2001). An unexpected extended conformation for the third TPR motif of the peroxin PEX5 from Trypanosoma brucei. Journal of Molecular Biology. 307(1). 271–282. 43 indexed citations
13.
Li, Rongbao, Rachada Sirawaraporn, P. Chitnumsub, et al.. (2000). Three-dimensional structure of M. tuberculosis dihydrofolate reductase reveals opportunities for the design of novel tuberculosis drugs. Journal of Molecular Biology. 295(2). 307–323. 170 indexed citations
14.
Aevarsson, Arnthór, Jacinta L. Chuang, Richard Wynn, et al.. (2000). Crystal structure of human branched-chain α-ketoacid dehydrogenase and the molecular basis of multienzyme complex deficiency in maple syrup urine disease. Structure. 8(3). 277–291. 133 indexed citations
15.
Kim, Youngsoo, et al.. (2000). The 2.0 Å Crystal Structure of Cephalosporin Acylase. Structure. 8(10). 1059–1068. 84 indexed citations
16.
Murphy, M.E.P., S. Turley, & Elinor T. Adman. (1997). Structure of Nitrite Bound to Copper-containing Nitrite Reductase from Alcaligenes faecalis. Journal of Biological Chemistry. 272(45). 28455–28460. 176 indexed citations
18.
Kukimoto‐Niino, Mutsuko, Makoto Nishiyama, Tatsuya Ohnuki, et al.. (1995). Identification of interaction site of pseudoazurin with its redox partner, copper-containing nitrite reductase from Alcaligenes faecalis S-6. Protein Engineering Design and Selection. 8(2). 153–158. 64 indexed citations
19.
Nishiyama, Makoto, Junko Suzuki, Tatsuya Ohnuki, et al.. (1992). Site-directed mutagenesis of pseudoazurin from Alcatigenes faecalis S-6; Pro80Ala mutant exhibits marked increase in reduction potential. Protein Engineering Design and Selection. 5(2). 177–184. 19 indexed citations
20.
Turley, S., et al.. (1988). Crystallization of nitrite reductase from Achromobacter cycloclastes. Journal of Molecular Biology. 200(2). 417–419. 11 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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