E.V. Schmalhausen

1.0k total citations
52 papers, 834 citations indexed

About

E.V. Schmalhausen is a scholar working on Molecular Biology, Clinical Biochemistry and Materials Chemistry. According to data from OpenAlex, E.V. Schmalhausen has authored 52 papers receiving a total of 834 indexed citations (citations by other indexed papers that have themselves been cited), including 40 papers in Molecular Biology, 13 papers in Clinical Biochemistry and 12 papers in Materials Chemistry. Recurrent topics in E.V. Schmalhausen's work include Molecular Biology Techniques and Applications (22 papers), Enzyme Structure and Function (12 papers) and Metabolomics and Mass Spectrometry Studies (8 papers). E.V. Schmalhausen is often cited by papers focused on Molecular Biology Techniques and Applications (22 papers), Enzyme Structure and Function (12 papers) and Metabolomics and Mass Spectrometry Studies (8 papers). E.V. Schmalhausen collaborates with scholars based in Russia, Tajikistan and Italy. E.V. Schmalhausen's co-authors include Vladimir I. Muronetz, Irina Naletova, Luciano Saso, Marina V. Serebryakova, Pavel I. Semenyuk, A. V. Avetisyan, N.K. Nagradova, Antonio Caprioli, Е. Е. Брагина and M. A. Eldarov and has published in prestigious journals such as Analytical Biochemistry, Biochemical and Biophysical Research Communications and FEBS Letters.

In The Last Decade

E.V. Schmalhausen

51 papers receiving 826 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
E.V. Schmalhausen Russia 19 580 143 127 111 82 52 834
Alberto Jiménez Spain 25 1.3k 2.2× 74 0.5× 102 0.8× 93 0.8× 80 1.0× 50 1.7k
Andréa Hamann Germany 21 1.2k 2.1× 107 0.7× 203 1.6× 21 0.2× 11 0.1× 50 1.6k
Antti M. Haapalainen Finland 19 786 1.4× 130 0.9× 84 0.7× 220 2.0× 6 0.1× 36 1.2k
Giovanni Parisi Italy 10 491 0.8× 152 1.1× 169 1.3× 18 0.2× 9 0.1× 17 747
Mário H. Barros Brazil 23 1.6k 2.7× 177 1.2× 181 1.4× 34 0.3× 6 0.1× 56 2.0k
Laishram Rajendrakumar Singh India 17 532 0.9× 57 0.4× 83 0.7× 120 1.1× 5 0.1× 42 876
Lisa Wen United States 14 590 1.0× 56 0.4× 28 0.2× 142 1.3× 6 0.1× 50 959
Albena Momchilova Bulgaria 20 677 1.2× 26 0.2× 176 1.4× 9 0.1× 32 0.4× 91 1.1k
César H. Casale Argentina 20 519 0.9× 152 1.1× 227 1.8× 53 0.5× 5 0.1× 44 940
Xiaoyu Hu China 17 608 1.0× 62 0.4× 97 0.8× 37 0.3× 5 0.1× 20 943

Countries citing papers authored by E.V. Schmalhausen

Since Specialization
Citations

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

Fields of papers citing papers by E.V. Schmalhausen

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by E.V. Schmalhausen. 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 E.V. Schmalhausen. The network helps show where E.V. Schmalhausen may publish in the future.

Co-authorship network of co-authors of E.V. Schmalhausen

This figure shows the co-authorship network connecting the top 25 collaborators of E.V. Schmalhausen. A scholar is included among the top collaborators of E.V. Schmalhausen 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 E.V. Schmalhausen. E.V. Schmalhausen 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.
Kurochkina, Lidia P., et al.. (2025). Factors Affecting Pathological Amyloid Protein Transformation: From Post-Translational Modifications to Chaperones. Biochemistry (Moscow). 90(S1). S164–S192.
2.
Naletova, Irina, et al.. (2023). The role of sperm-specific glyceraldehyde-3-phosphate dehydrogenase in the development of pathologies—from asthenozoospermia to carcinogenesis. Frontiers in Molecular Biosciences. 10. 1256963–1256963. 9 indexed citations
3.
Kleimenov, S. Yu., et al.. (2023). S-nitrosylation and S-glutathionylation of GAPDH: Similarities, differences, and relationships. Biochimica et Biophysica Acta (BBA) - General Subjects. 1867(9). 130418–130418. 7 indexed citations
4.
Serebryakova, Marina V., et al.. (2022). Mechanism of inactivation of glyceraldehyde-3-phosphate dehydrogenase in the presence of methylglyoxal. Archives of Biochemistry and Biophysics. 733. 109485–109485. 13 indexed citations
5.
Muronetz, Vladimir I., et al.. (2021). Modification of Glyceraldehyde-3-Phosphate Dehydrogenase with Nitric Oxide: Role in Signal Transduction and Development of Apoptosis. Biomolecules. 11(11). 1656–1656. 15 indexed citations
6.
Serebryakova, Marina V., et al.. (2019). Modification by glyceraldehyde-3-phosphate prevents amyloid transformation of alpha-synuclein. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1867(4). 396–404. 12 indexed citations
7.
Muronetz, Vladimir I., et al.. (2017). Glycation, glycolysis, and neurodegenerative diseases: Is there any connection?. Biochemistry (Moscow). 82(8). 874–886. 34 indexed citations
8.
Serebryakova, Marina V., et al.. (2017). S-glutathionylation of glyceraldehyde-3-phosphate dehydrogenase induces formation of C150-C154 intrasubunit disulfide bond in the active site of the enzyme. Biochimica et Biophysica Acta (BBA) - General Subjects. 1861(12). 3167–3177. 40 indexed citations
9.
Muronetz, Vladimir I., et al.. (2016). Glyceraldehyde-3-phosphate dehydrogenase: Aggregation mechanisms and impact on amyloid neurodegenerative diseases. International Journal of Biological Macromolecules. 100. 55–66. 39 indexed citations
10.
Muronetz, Vladimir I., et al.. (2015). Sperm-Specific Glyceraldehyde-3-Phosphate Dehydrogenase–An Evolutionary Acquisition of Mammals. Biochemistry (Moscow). 80(13). 1672–1689. 9 indexed citations
11.
Muronetz, Vladimir I., et al.. (2015). Low concentrations of hydrogen peroxide activate the antioxidant defense system in human sperm cells. Biochemistry (Moscow). 80(9). 1178–1185. 19 indexed citations
13.
Semenyuk, Pavel I., et al.. (2014). Sperm-specific glyceraldehyde-3-phosphate dehydrogenase is stabilized by additional proline residues and an interdomain salt bridge. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1844(10). 1820–1826. 13 indexed citations
14.
Pyrkov, Timothy V., E.V. Schmalhausen, Andrey N. Shkoporov, et al.. (2013). Structure‐Based Design of Small‐Molecule Ligands of Phosphofructokinase‐2 Activating or Inhibiting Glycolysis. ChemMedChem. 8(8). 1322–1329. 6 indexed citations
15.
Naletova, Irina, et al.. (2011). Chaperonin TRiC assists the refolding of sperm-specific glyceraldehyde-3-phosphate dehydrogenase. Archives of Biochemistry and Biophysics. 516(1). 75–83. 5 indexed citations
16.
Брагина, Е. Е., et al.. (2011). Oxidation of glyceraldehyde-3-phosphate dehydrogenase decreases sperm motility. Biochemistry (Moscow). 76(2). 268–272. 33 indexed citations
17.
Брагина, Е. Е., et al.. (2008). Investigation of glyceraldehyde-3-phosphate dehydrogenase from human sperms. Biochemistry (Moscow). 73(2). 185–191. 12 indexed citations
18.
Naletova, Irina, Vladimir I. Muronetz, & E.V. Schmalhausen. (2006). Unfolded, oxidized, and thermoinactivated forms of glyceraldehyde-3-phosphate dehydrogenase interact with the chaperonin GroEL in different ways. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1764(4). 831–838. 31 indexed citations
19.
Schmalhausen, E.V., Vladimir I. Muronetz, & N.K. Nagradova. (1997). Rabbit muscle GAPDH: non‐phosphorylating dehydrogenase activity induced by hydrogen peroxide. FEBS Letters. 414(2). 247–252. 12 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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