Jure Stojan

3.2k total citations
96 papers, 2.5k citations indexed

About

Jure Stojan is a scholar working on Pharmacology, Molecular Biology and Computational Theory and Mathematics. According to data from OpenAlex, Jure Stojan has authored 96 papers receiving a total of 2.5k indexed citations (citations by other indexed papers that have themselves been cited), including 51 papers in Pharmacology, 44 papers in Molecular Biology and 36 papers in Computational Theory and Mathematics. Recurrent topics in Jure Stojan's work include Cholinesterase and Neurodegenerative Diseases (44 papers), Computational Drug Discovery Methods (36 papers) and Pesticide Exposure and Toxicity (16 papers). Jure Stojan is often cited by papers focused on Cholinesterase and Neurodegenerative Diseases (44 papers), Computational Drug Discovery Methods (36 papers) and Pesticide Exposure and Toxicity (16 papers). Jure Stojan collaborates with scholars based in Slovenia, France and Germany. Jure Stojan's co-authors include Didier Fournier, Tea Lanišnik Rižner, Jacques‐Philippe Colletier, Stanislav Gobec, Jerzy Adamski, Radovan Komel, Marko Goličnik, Boris Brus, Martin H. Weik and Samo Turk and has published in prestigious journals such as Journal of Biological Chemistry, The EMBO Journal and PLoS ONE.

In The Last Decade

Jure Stojan

95 papers receiving 2.5k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Jure Stojan Slovenia 26 1.2k 1.0k 755 556 477 96 2.5k
Cláudio Viegas Brazil 27 862 0.7× 1.1k 1.1× 438 0.6× 629 1.1× 1.4k 3.0× 88 3.3k
Jonathan Bisson United States 22 574 0.5× 1.4k 1.4× 205 0.3× 413 0.7× 284 0.6× 42 3.2k
Arie Ordentlich Israel 34 2.3k 1.9× 1.2k 1.1× 1.3k 1.7× 1.7k 3.0× 738 1.5× 62 3.6k
Cleydson B. R. Santos Brazil 26 405 0.3× 656 0.6× 761 1.0× 298 0.5× 620 1.3× 127 2.0k
Yacov Ashani Israel 34 1.7k 1.4× 1.3k 1.3× 630 0.8× 1.9k 3.5× 511 1.1× 94 3.9k
Zhili Zuo China 25 460 0.4× 796 0.8× 226 0.3× 271 0.5× 378 0.8× 101 1.8k
Goran Šinko Croatia 23 916 0.8× 352 0.3× 420 0.6× 668 1.2× 288 0.6× 51 1.7k
Jörg Heilmann Germany 40 966 0.8× 2.0k 2.0× 314 0.4× 1.4k 2.6× 1.1k 2.3× 172 4.6k
Vikas Jaitak India 27 313 0.3× 1.0k 1.0× 177 0.2× 605 1.1× 1.1k 2.3× 95 3.1k
James G. Graham United States 24 524 0.4× 1.5k 1.4× 160 0.2× 653 1.2× 365 0.8× 51 3.3k

Countries citing papers authored by Jure Stojan

Since Specialization
Citations

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

Fields of papers citing papers by Jure Stojan

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Jure Stojan

This figure shows the co-authorship network connecting the top 25 collaborators of Jure Stojan. A scholar is included among the top collaborators of Jure Stojan 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 Jure Stojan. Jure Stojan 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
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Stojan, Jure, Milan Hodošček, & Dušanka Janežič. (2021). Automatic Assembly and Calibration of Models of Enzymatic Reactions Based on Ordinary Differential Equations. Methods in molecular biology. 2385. 141–152. 1 indexed citations
4.
Fonović, Urša Pečar, Ana Mitrović, Damijan Knez, et al.. (2017). Identification and characterization of the novel reversible and selective cathepsin X inhibitors. Scientific Reports. 7(1). 11459–11459. 13 indexed citations
5.
Mashele, Samson S., Lidija Kovačič, Jure Stojan, et al.. (2014). Cytochrome P450 Monooxygenase CYP53 Family in Fungi: Comparative Structural and Evolutionary Analysis and Its Role as a Common Alternative Anti-Fungal Drug Target. PLoS ONE. 9(9). e107209–e107209. 55 indexed citations
6.
Perdih, Andrej, Matjaž Brvar, Ana Kroflič, et al.. (2013). Discovery of the first inhibitors of bacterial enzyme d-aspartate ligase from Enterococcus faecium (Aslfm). European Journal of Medicinal Chemistry. 67. 208–220. 19 indexed citations
7.
Stojan, Jure. (2012). The significance of low substrate concentration measurements for mechanistic interpretation in cholinesterases. Chemico-Biological Interactions. 203(1). 44–50. 6 indexed citations
8.
Konc, Janez, et al.. (2011). ENZO: A Web Tool for Derivation and Evaluation of Kinetic Models of Enzyme Catalyzed Reactions. PLoS ONE. 6(7). e22265–e22265. 62 indexed citations
9.
Stojan, Jure. (2008). Kinetic evaluation of multiple initial rate data by simultaneous analysis with two equations. Chemico-Biological Interactions. 175(1-3). 242–248. 4 indexed citations
10.
Nachon, Florian, Jure Stojan, & Didier Fournier. (2008). Insights into substrate and product traffic in the Drosophila melanogaster acetylcholinesterase active site gorge by enlarging a back channel. FEBS Journal. 275(10). 2659–2664. 19 indexed citations
11.
Kristan, Katja, Jure Stojan, Jerzy Adamski, & Tea Lanišnik Rižner. (2006). Rational design of novel mutants of fungal 17β-hydroxysteroid dehydrogenase. Journal of Biotechnology. 129(1). 123–130. 30 indexed citations
12.
Colletier, Jacques‐Philippe, Didier Fournier, Harry M. Greenblatt, et al.. (2006). Structural insights into substrate traffic and inhibition in acetylcholinesterase. The EMBO Journal. 25(12). 2746–2756. 167 indexed citations
13.
Florén, Anders, Ulla Sollenberg, Linda Lundström, et al.. (2005). Multiple interaction sites of galnon trigger its biological effects. Neuropeptides. 39(6). 547–558. 24 indexed citations
14.
Kristan, Katja, et al.. (2005). Phytoestrogens as inhibitors of fungal 17β-hydroxysteroid dehydrogenase. Steroids. 70(10). 694–703. 24 indexed citations
15.
Goličnik, Marko & Jure Stojan. (2004). Slow‐binding inhibition: A theoretical and practical course for students. Biochemistry and Molecular Biology Education. 32(4). 228–235. 25 indexed citations
16.
Lougarre, Andrée, et al.. (2004). Acetylcholinesterase alterations reveal the fitness cost of mutations conferring insecticide resistance. BMC Evolutionary Biology. 4(1). 5–5. 73 indexed citations
17.
Goličnik, Marko & Jure Stojan. (2002). Multi-step analysis as a tool for kinetic parameter estimation and mechanism discrimination in the reaction between tight-binding fasciculin 2 and electric eel acetylcholinesterase. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1597(1). 164–172. 11 indexed citations
18.
Stojan, Jure. (1998). Equations for Progress Curves of Some Kinetic Models of Enzyme-Single Substrate-Single Slow Binding Modifier System. Journal of enzyme inhibition. 13(3). 161–176. 4 indexed citations
19.
Stojan, Jure, et al.. (1997). Mechanism of Eserine Action on The Hydrolysis of Butyrylthiocholine by Butyrylcholinesterase. Journal of enzyme inhibition. 11(3). 199–208. 3 indexed citations
20.
Stojan, Jure, et al.. (1992). Velocity of Ellman's reaction and its implication for kinetic studies in the millisecond time range. Neurochemical Research. 17(12). 1207–1210. 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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