Aavo Aaviksaar

712 total citations
37 papers, 565 citations indexed

About

Aavo Aaviksaar is a scholar working on Molecular Biology, Pharmacology and Organic Chemistry. According to data from OpenAlex, Aavo Aaviksaar has authored 37 papers receiving a total of 565 indexed citations (citations by other indexed papers that have themselves been cited), including 22 papers in Molecular Biology, 15 papers in Pharmacology and 9 papers in Organic Chemistry. Recurrent topics in Aavo Aaviksaar's work include Cholinesterase and Neurodegenerative Diseases (13 papers), Computational Drug Discovery Methods (6 papers) and Enzyme Catalysis and Immobilization (6 papers). Aavo Aaviksaar is often cited by papers focused on Cholinesterase and Neurodegenerative Diseases (13 papers), Computational Drug Discovery Methods (6 papers) and Enzyme Catalysis and Immobilization (6 papers). Aavo Aaviksaar collaborates with scholars based in Estonia, Germany and Czechia. Aavo Aaviksaar's co-authors include Hans‐Dieter Jakubke, R. Raba, Matthias Schuster, Jaak Järv, Ferdinand Hucho, Hans‐Jürgen Kreienkamp, Christoph Weise, Tönu Kesvatera, Vello Tõugu and Jindřich Kopeček and has published in prestigious journals such as Proceedings of the National Academy of Sciences, The EMBO Journal and Biochemical Journal.

In The Last Decade

Aavo Aaviksaar

35 papers receiving 543 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Aavo Aaviksaar Estonia 15 328 227 157 154 63 37 565
Pavel Bobáľ Czechia 15 266 0.8× 61 0.3× 58 0.4× 337 2.2× 35 0.6× 49 651
Xulin Pan China 12 228 0.7× 44 0.2× 59 0.4× 166 1.1× 71 1.1× 14 480
Gregory S. Welmaker United States 15 478 1.5× 128 0.6× 176 1.1× 359 2.3× 18 0.3× 20 894
Raghuram Rao Akkinepally India 15 238 0.7× 117 0.5× 100 0.6× 480 3.1× 19 0.3× 49 800
Robert S. Rush United States 15 326 1.0× 261 1.1× 160 1.0× 83 0.5× 106 1.7× 22 731
Melissa D’Ascenzio Italy 24 505 1.5× 410 1.8× 112 0.7× 805 5.2× 43 0.7× 32 1.2k
Youchao Deng China 11 300 0.9× 138 0.6× 157 1.0× 154 1.0× 23 0.4× 31 629
Dong-Woo Shin United States 9 302 0.9× 154 0.7× 195 1.2× 200 1.3× 21 0.3× 21 638
Bao Cheng China 15 231 0.7× 103 0.5× 36 0.2× 102 0.7× 63 1.0× 28 479
Hartwig Müller Germany 9 356 1.1× 295 1.3× 75 0.5× 453 2.9× 78 1.2× 19 858

Countries citing papers authored by Aavo Aaviksaar

Since Specialization
Citations

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

Fields of papers citing papers by Aavo Aaviksaar

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Aavo Aaviksaar

This figure shows the co-authorship network connecting the top 25 collaborators of Aavo Aaviksaar. A scholar is included among the top collaborators of Aavo Aaviksaar 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 Aavo Aaviksaar. Aavo Aaviksaar 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.
Aaviksaar, Aavo, et al.. (2003). Hydroxystilbenes in the roots of Rheum rhaponticum. Proceedings of the Estonian Academy of Sciences Chemistry. 52(3). 99–107. 15 indexed citations
2.
Tõugu, Vello, et al.. (1995). Aminolysis of acyl-chymotrypsins by amino acids. Kinetic appearance of concentration effect in peptide yield enhancement by freezing. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1247(2). 272–276. 9 indexed citations
3.
Tõugu, Vello, et al.. (1994). Electrostatic effects in trypsin reactions. European Journal of Biochemistry. 222(2). 475–481. 7 indexed citations
4.
Tõugu, Vello, et al.. (1993). Peptide synthesis by chymotrypsin in frozen solutions. FEBS Letters. 329(1-2). 40–42. 24 indexed citations
5.
Schuster, Matthias, Aavo Aaviksaar, & Hans‐Dieter Jakubke. (1992). α-Chymotrypsin-catalyzed (3 + 7) segment synthesis of the luteinizing hormone releasing hormone. Tetrahedron Letters. 33(20). 2799–2802. 3 indexed citations
6.
Kreienkamp, Hans‐Jürgen, Christoph Weise, R. Raba, Aavo Aaviksaar, & Ferdinand Hucho. (1991). Anionic subsites of the catalytic center of acetylcholinesterase from Torpedo and from cobra venom.. Proceedings of the National Academy of Sciences. 88(14). 6117–6121. 38 indexed citations
7.
Schellenberger, Volker, et al.. (1991). Electrostatic effects in the α-chymotrypsin-catalyzed acyl transfer. I. Influence of different inorganic salts. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1078(1). 1–7. 13 indexed citations
8.
Weise, Christoph, Hans‐Jürgen Kreienkamp, R. Raba, Aavo Aaviksaar, & Ferdinand Hucho. (1990). The active site and partial sequence of cobra venom acetylcholinesterase. Journal of Protein Chemistry. 9(1). 53–57. 14 indexed citations
9.
Järv, Jaak, et al.. (1990). The Influence of Inorganic Salts on the Inhibition of Acetylcholinesterase by O,O-Diethylthiophosphates. Phosphorus, sulfur, and silicon and the related elements. 51(1-4). 407–407.
10.
Schuster, Matthias, Aavo Aaviksaar, Volker Schellenberger, & Hans‐Dieter Jakubke. (1990). Characterization of the S′-subsite specificity of V8 proteinase via acyl transfer to added nucleophiles. Biochimica et Biophysica Acta (BBA) - General Subjects. 1036(3). 245–247. 9 indexed citations
11.
Strukova, S. M., Alexander E Kogan, Mahmood Tara, & Aavo Aaviksaar. (1989). Anticoagulant effect of the protease from Agkistrodon venom mediated by protein C activation in rats. Thrombosis Research. 55(1). 149–153. 2 indexed citations
12.
Aaviksaar, Aavo. (1988). Medium effects in enzyme specificity. Journal of Molecular Catalysis. 47(2-3). 265–270. 2 indexed citations
13.
Kesvatera, Tönu, et al.. (1988). High-concentration salt effects in acetylcholinesterase reactions. Bioorganic Chemistry. 16(4). 429–439. 7 indexed citations
14.
Tõugu, Vello, et al.. (1987). Acetylcholinesterase as polyelectrolyte in reaction with cationic substrates. FEBS Letters. 225(1-2). 77–81. 16 indexed citations
15.
Sikk, Peeter, et al.. (1985). Irreversible inhibition of pancreatic lipase by bis‐p‐nitrophenyl methylphosphonate. FEBS Letters. 184(2). 193–196. 7 indexed citations
16.
Raba, R. & Aavo Aaviksaar. (1982). Cobra Venom Acetylcholinesterase: Nature of Charge Isoforms. European Journal of Biochemistry. 127(3). 507–512. 9 indexed citations
17.
Kesvatera, Tönu, Mart Ustav, & Aavo Aaviksaar. (1979). Cobra venom acetylcholinesterase—II. Substrate specifity. Comparative Biochemistry and Physiology Part C Comparative Pharmacology. 62(2). 193–197. 6 indexed citations
18.
Järv, Jaak, et al.. (1977). The arrangement of substrate and organophosphorus-inhibitor leaving groups in acetylcholinesterase active site. Biochemical Journal. 167(3). 823–825. 15 indexed citations
19.
Osa, A., et al.. (1977). Preparative purification of alkyl methylphosphonic acid p-nitrophenyl esters on Sephadex LH-20. Journal of Chromatography A. 135(1). 196–199. 4 indexed citations
20.
Aaviksaar, Aavo, et al.. (1976). Synthesis of some O, O-diethylphosphoric acid thioesters. Russian Chemical Bulletin. 25(2). 407–409.

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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