Д. Т. Гуранда

487 total citations
25 papers, 413 citations indexed

About

Д. Т. Гуранда is a scholar working on Molecular Biology, Organic Chemistry and Spectroscopy. According to data from OpenAlex, Д. Т. Гуранда has authored 25 papers receiving a total of 413 indexed citations (citations by other indexed papers that have themselves been cited), including 18 papers in Molecular Biology, 7 papers in Organic Chemistry and 5 papers in Spectroscopy. Recurrent topics in Д. Т. Гуранда's work include Enzyme Catalysis and Immobilization (12 papers), Chemical Synthesis and Analysis (9 papers) and Amino Acid Enzymes and Metabolism (4 papers). Д. Т. Гуранда is often cited by papers focused on Enzyme Catalysis and Immobilization (12 papers), Chemical Synthesis and Analysis (9 papers) and Amino Acid Enzymes and Metabolism (4 papers). Д. Т. Гуранда collaborates with scholars based in Russia, Tajikistan and Netherlands. Д. Т. Гуранда's co-authors include Vytas K. Švedas, Luuk M. van Langen, Roger A. Sheldon, Fred van Rantwijk, R. Ann Sheldon, Н. И. Ларионова, Н. Г. Балабушевич, E. N. Shapovalova, А. S. Yanenko and Ghermes G. Chilov and has published in prestigious journals such as FEBS Letters, Annals of the New York Academy of Sciences and Carbohydrate Polymers.

In The Last Decade

Д. Т. Гуранда

23 papers receiving 404 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Д. Т. Гуранда Russia 13 317 94 66 57 42 25 413
Bryan J. Jones United States 10 377 1.2× 77 0.8× 56 0.8× 71 1.2× 60 1.4× 16 535
Hyun-Won Kim South Korea 11 311 1.0× 46 0.5× 61 0.9× 61 1.1× 29 0.7× 31 521
Maxim I. Youshko Russia 11 354 1.1× 93 1.0× 46 0.7× 71 1.2× 15 0.4× 16 413
Grant Ganshaw United States 9 302 1.0× 36 0.4× 47 0.7× 113 2.0× 34 0.8× 13 372
Lung‐Chi Yuan United States 7 258 0.8× 90 1.0× 86 1.3× 44 0.8× 14 0.3× 10 422
Riccardo Torosantucci Netherlands 11 297 0.9× 73 0.8× 48 0.7× 29 0.5× 19 0.5× 12 443
Masayori Hagimori Japan 14 241 0.8× 92 1.0× 107 1.6× 94 1.6× 30 0.7× 36 514
Eric Johansson United Kingdom 6 213 0.7× 229 2.4× 25 0.4× 39 0.7× 82 2.0× 6 470
Vania Bernardes‐Génisson France 15 242 0.8× 292 3.1× 23 0.3× 42 0.7× 43 1.0× 35 594
Sara Drioli Italy 13 215 0.7× 199 2.1× 25 0.4× 48 0.8× 32 0.8× 43 507

Countries citing papers authored by Д. Т. Гуранда

Since Specialization
Citations

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

Fields of papers citing papers by Д. Т. Гуранда

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Д. Т. Гуранда. 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 Д. Т. Гуранда. The network helps show where Д. Т. Гуранда may publish in the future.

Co-authorship network of co-authors of Д. Т. Гуранда

This figure shows the co-authorship network connecting the top 25 collaborators of Д. Т. Гуранда. A scholar is included among the top collaborators of Д. Т. Гуранда 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 Д. Т. Гуранда. Д. Т. Гуранда 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.
Гуранда, Д. Т., et al.. (2023). Penicillin Acylase: A Retrospective Study of the Kinetics and Thermodynamics of Practically Significant Reactions. Moscow University Chemistry Bulletin. 78(4). 187–200.
2.
3.
Chelysheva, Ekaterina, Anna Turkina, Evgeniya Polushkina, et al.. (2017). Placental transfer of tyrosine kinase inhibitors used for chronic myeloid leukemia treatment. Leukemia & lymphoma. 59(3). 733–738. 30 indexed citations
4.
Гуранда, Д. Т., et al.. (2016). COMPARATIVE PHARMACOKINETICS AND EFFECT ON THE HEMODYNAMICS OF ORIGINAL AND GENERIC NEBIVOLOL IN HEALTHY VOLUNTEERS. Rational Pharmacotherapy in Cardiology. 12(2). 171–175. 1 indexed citations
5.
Гуранда, Д. Т., et al.. (2011). Thermodynamics of phenylacetamides synthesis: Linear free energy relationship with the pK of amine. Journal of Molecular Catalysis B Enzymatic. 74(1-2). 48–53. 5 indexed citations
6.
Гуранда, Д. Т., et al.. (2010). Preparation of drug polymorphs (a review). Pharmaceutical Chemistry Journal. 44(5). 254–260. 11 indexed citations
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8.
Grinberg, V. Ya., Tatiana V. Burova, Natalia V. Grinberg, et al.. (2008). Thermodynamic and kinetic stability of penicillin acylase from Escherichia coli. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1784(5). 736–746. 12 indexed citations
9.
Ларионова, Н. И., et al.. (2008). Colorimetric assay of chitosan in presence of proteins and polyelectrolytes by using o-phthalaldehyde. Carbohydrate Polymers. 75(4). 724–727. 37 indexed citations
10.
11.
Гуранда, Д. Т., et al.. (2005). Aliphatic Amidase from Rhodococcus rhodochrous M8 Is Related to the Nitrilase/Cyanide Hydratase Family. Biochemistry (Moscow). 70(11). 1280–1287. 18 indexed citations
12.
13.
Гуранда, Д. Т., et al.. (2004). pH stability of penicillin acylase from Escherichia coli. Biochemistry (Moscow). 69(12). 1386–1390. 13 indexed citations
14.
Гуранда, Д. Т., et al.. (2004). An ‘easy-on, easy-off’ protecting group for the enzymatic resolution of (±)-1-phenylethylamine in an aqueous medium. Tetrahedron Asymmetry. 15(18). 2901–2906. 17 indexed citations
15.
Гуранда, Д. Т., Luuk M. van Langen, Fred van Rantwijk, Roger A. Sheldon, & Vytas K. Švedas. (2001). Highly efficient and enantioselective enzymatic acylation of amines in aqueous medium. Tetrahedron Asymmetry. 12(11). 1645–1650. 44 indexed citations
16.
Langen, Luuk M. van, et al.. (2000). Penicillin acylase-catalyzed resolution of amines in aqueous organic solvents. Tetrahedron Asymmetry. 11(22). 4593–4600. 54 indexed citations
17.
Гуранда, Д. Т., et al.. (2000). The role of hydrophobic interactions on alcohol binding in the active center of penicillin acylases.. PubMed. 65(8). 963–6. 2 indexed citations
18.
Youshko, Maxim I., et al.. (1998). Specific substrates for spectrophotometric determination of penicillin acylase activity.. PubMed. 63(9). 1104–9. 13 indexed citations
19.
Švedas, Vytas K., et al.. (1997). Kinetic study of penicillin acylase from Alcaligenes faecalis. FEBS Letters. 417(3). 414–418. 55 indexed citations
20.
Гуранда, Д. Т., et al.. (1996). Enantioselective Penicillin Acylase—catalyzed Reactions. Annals of the New York Academy of Sciences. 799(1). 659–669. 42 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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