С. С. Савин

556 total citations
52 papers, 371 citations indexed

About

С. С. Савин is a scholar working on Molecular Biology, Materials Chemistry and Biochemistry. According to data from OpenAlex, С. С. Савин has authored 52 papers receiving a total of 371 indexed citations (citations by other indexed papers that have themselves been cited), including 41 papers in Molecular Biology, 24 papers in Materials Chemistry and 17 papers in Biochemistry. Recurrent topics in С. С. Савин's work include Enzyme Structure and Function (24 papers), Enzyme Catalysis and Immobilization (21 papers) and Amino Acid Enzymes and Metabolism (17 papers). С. С. Савин is often cited by papers focused on Enzyme Structure and Function (24 papers), Enzyme Catalysis and Immobilization (21 papers) and Amino Acid Enzymes and Metabolism (17 papers). С. С. Савин collaborates with scholars based in Russia, Tajikistan and Czechia. С. С. Савин's co-authors include В. И. Тишков, А. В. Алексеева, Sergey Y. Kleymenov, S. Yu. Kleimenov, I. V. Uporov, A.Y. Nikolaeva, Andrey V. Levashov, Konstantin M. Boyko, П. А. Левашов and T. A. Chubar and has published in prestigious journals such as International Journal of Molecular Sciences, Biochimie and Electrophoresis.

In The Last Decade

С. С. Савин

47 papers receiving 370 citations

Peers

С. С. Савин
C.L. Berthold Sweden
Ricardo Martí‐Arbona United States
Baifan Wang China
David Silverman United States
Sheng Wu China
Jason J. Reddick United States
Akiko Nakazawa Japan
Vinod Puthan Veetil Netherlands
Maria S. Brown United States
Bruno Brasil Horta Brazil
C.L. Berthold Sweden
С. С. Савин
Citations per year, relative to С. С. Савин С. С. Савин (= 1×) peers C.L. Berthold

Countries citing papers authored by С. С. Савин

Since Specialization
Citations

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

Fields of papers citing papers by С. С. Савин

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of С. С. Савин

This figure shows the co-authorship network connecting the top 25 collaborators of С. С. Савин. A scholar is included among the top collaborators of С. С. Савин 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 С. С. Савин. С. С. Савин 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.
Никулин, С. В., et al.. (2023). Микробиом и in vitro модели кишечника. Biotekhnologiya. 39(5). 82–96.
2.
Савин, С. С., Sergey Y. Kleymenov, Mikhail E. Minyaev, et al.. (2023). Structure–Functional Examination of Novel Ribonucleoside Hydrolase C (RihC) from Limosilactobacillus reuteri LR1. International Journal of Molecular Sciences. 25(1). 538–538. 3 indexed citations
3.
Тишков, В. И., et al.. (2023). PHYSIOLOGICAL ROLE OF D-AMINO ACIDS AND BIOANALYTICALPOTENTIAL OF D-AMINO ACID OXIDASES. 64(№2, 2023). 72–84.
4.
5.
Савин, С. С., et al.. (2023). Engineering the N-Terminal Sequence of Glycine max Soybean Formate Dehydrogenase. Moscow University Chemistry Bulletin. 78(4). 220–229. 1 indexed citations
6.
Elcheninov, Alexander G., et al.. (2023). Bioinformatics-Structural Approach to the Search for New D-Amino Acid Oxidases. PubMed. 14(4). 57–68. 2 indexed citations
7.
Тишков, В. И., et al.. (2023). Physiological Role of D-amino Acids and Bioanalytical Potential of D-amino Acid Oxidases. Moscow University Chemistry Bulletin. 78(1). 1–9.
8.
Савин, С. С., et al.. (2023). NAD+-Dependent Formate Dehydrogenase from Themotolerant Yeast Ogataea parapolymorpha: Properties and Protein Engineering of the N-Terminal Sequence. Biochemistry (Moscow). 88(9). 1378–1389. 2 indexed citations
9.
Савин, С. С., et al.. (2023). Kinetics of Thermoinactivation of D-Amino Acid Oxidase OPADAAO1 from the Ogataea parapolymorpha DL-1 Yeast. Moscow University Chemistry Bulletin. 78(2). 69–75. 1 indexed citations
10.
11.
Kleymenov, Sergey Y., et al.. (2020). Effect of His6-tag Position on the Expression and Properties of Phenylacetone Monooxygenase from Thermobifida fusca. Biochemistry (Moscow). 85(5). 575–582. 8 indexed citations
12.
Boyko, Konstantin M., et al.. (2020). Highly-Active Recombinant Formate Dehydrogenase from Pathogenic Bacterium Staphylococcus aureus: Preparation and Crystallization. Biochemistry (Moscow). 85(6). 689–696. 11 indexed citations
13.
Савин, С. С., et al.. (2018). Effect of Medium pH And Ion Strength on the Thermal Stability of Plant Formate Dehydrogenases. Moscow University Chemistry Bulletin. 73(4). 199–203. 1 indexed citations
14.
Левашов, П. А., et al.. (2017). Bacteriolytic Activity Of Human Interleukin-2, Chicken Egg Lysozyme In The Presence Of Potential Effectors. Acta Naturae. 9(2). 82–87. 5 indexed citations
15.
Савин, С. С., et al.. (2016). Influence of Met/Leu amino acid changes on catalytic properties and oxidative and thermal stability of yeast D-amino acid oxidase. Moscow University Chemistry Bulletin. 71(4). 243–252. 6 indexed citations
16.
Тишков, В. И., et al.. (2015). Role of a Structurally Equivalent Phenylalanine Residue in Catalysis and Thermal Stability of Formate Dehydrogenases from Different Sources. Biochemistry (Moscow). 80(13). 1690–1700. 16 indexed citations
17.
Kleimenov, S. Yu., et al.. (2015). Improvement of the soy formate dehydrogenase properties by rational design. Protein Engineering Design and Selection. 28(6). 171–178. 18 indexed citations
18.
Алексеева, А. В., et al.. (2012). Engineering catalytic properties and thermal stability of plant formate dehydrogenase by single-point mutations. Protein Engineering Design and Selection. 25(11). 781–788. 23 indexed citations
19.
Алексеева, А. В., et al.. (2012). Stabilization of plant formate dehydrogenase by rational design. Biochemistry (Moscow). 77(10). 1199–1209. 7 indexed citations
20.
Khoronenkova, S. V., et al.. (2010). The 3D-structural modeling of yeast D-amino acid oxidase. Moscow University Chemistry Bulletin. 65(3). 121–126. 2 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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