M.Ya. Karpeisky

803 total citations
42 papers, 612 citations indexed

About

M.Ya. Karpeisky is a scholar working on Molecular Biology, Materials Chemistry and Organic Chemistry. According to data from OpenAlex, M.Ya. Karpeisky has authored 42 papers receiving a total of 612 indexed citations (citations by other indexed papers that have themselves been cited), including 28 papers in Molecular Biology, 23 papers in Materials Chemistry and 9 papers in Organic Chemistry. Recurrent topics in M.Ya. Karpeisky's work include Enzyme Structure and Function (23 papers), DNA and Nucleic Acid Chemistry (12 papers) and Protein Structure and Dynamics (10 papers). M.Ya. Karpeisky is often cited by papers focused on Enzyme Structure and Function (23 papers), DNA and Nucleic Acid Chemistry (12 papers) and Protein Structure and Dynamics (10 papers). M.Ya. Karpeisky collaborates with scholars based in Russia, Slovakia and United Kingdom. M.Ya. Karpeisky's co-authors include V. I. Ivanov, Sergey N. Mikhailov, A.G. Pavlovsky, V. L. Florentiev, Andrei L. Okorokov, Gennady I. Yakovlev, Kostya I. Panov, Valentin Ilyin, S.N. Borisova and V.V. Borisov and has published in prestigious journals such as Nature, Journal of Molecular Biology and Biochemical Journal.

In The Last Decade

M.Ya. Karpeisky

42 papers receiving 532 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
M.Ya. Karpeisky Russia 17 439 231 129 72 54 42 612
William F. Benisek United States 18 483 1.1× 202 0.9× 37 0.3× 92 1.3× 73 1.4× 36 665
William Eventoff United States 9 418 1.0× 196 0.8× 58 0.4× 24 0.3× 98 1.8× 10 583
Aldonia Valasinas Argentina 20 810 1.8× 155 0.7× 271 2.1× 111 1.5× 46 0.9× 48 956
L. Timothy Laughlin United States 11 391 0.9× 134 0.6× 126 1.0× 41 0.6× 40 0.7× 11 580
Marilynn S. Doscher United States 12 495 1.1× 296 1.3× 19 0.1× 46 0.6× 48 0.9× 19 604
Richard S. Brody United States 9 397 0.9× 108 0.5× 49 0.4× 49 0.7× 19 0.4× 11 484
Rudolf Weil Austria 14 362 0.8× 45 0.2× 80 0.6× 74 1.0× 41 0.8× 30 549
H. Groendijk Netherlands 11 399 0.9× 162 0.7× 84 0.7× 24 0.3× 34 0.6× 15 544
Gerald M. Alter United States 13 420 1.0× 108 0.5× 22 0.2× 39 0.5× 57 1.1× 34 597
Anthony A. Morollo United States 8 394 0.9× 222 1.0× 138 1.1× 43 0.6× 9 0.2× 8 512

Countries citing papers authored by M.Ya. Karpeisky

Since Specialization
Citations

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

Fields of papers citing papers by M.Ya. Karpeisky

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by M.Ya. Karpeisky. 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 M.Ya. Karpeisky. The network helps show where M.Ya. Karpeisky may publish in the future.

Co-authorship network of co-authors of M.Ya. Karpeisky

This figure shows the co-authorship network connecting the top 25 collaborators of M.Ya. Karpeisky. A scholar is included among the top collaborators of M.Ya. Karpeisky 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 M.Ya. Karpeisky. M.Ya. Karpeisky 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.
Polyakov, K. M., Andrey A. Lebedev, Andrei L. Okorokov, et al.. (2002). The structure of substrate-free microbial ribonuclease binase and of its complexes with 3′GMP and sulfate ions. Acta Crystallographica Section D Biological Crystallography. 58(5). 744–750. 20 indexed citations
2.
Reinholz, Gregory G., et al.. (2002). Distinct mechanisms of bisphosphonate action between osteoblasts and breast cancer cells: identity of a potent new bisphosphonate analogue. Breast Cancer Research and Treatment. 71(3). 257–268. 39 indexed citations
3.
Kochetkov, Sergey N., et al.. (2001). Interaction of HIV-1 Reverse Transcriptase and T7 RNA Polymerase with Phosphonate Analogs of NTP and Inorganic Pyrophosphate. Molecular Biology. 35(5). 717–729. 13 indexed citations
4.
Scheltinga, Anke C. Terwisscha van, et al.. (2000). Localization and analysis of nonpolar regions in onconase. Cellular and Molecular Life Sciences. 57(8). 1306–1316. 8 indexed citations
5.
Dixon, H. B. F., et al.. (1999). Synthesis and Properties of Novel NTP Derivatives. Nucleosides and Nucleotides. 18(4-5). 1013–1014. 4 indexed citations
6.
Okorokov, Andrei L., Kostya I. Panov, Wendy A. Offen, et al.. (1997). RNA cleavage without hydrolysis. Splitting the catalytic activities of binase with Asn101 and Thr101 mutations. Protein Engineering Design and Selection. 10(3). 273–278. 16 indexed citations
7.
Marković-Housley, Z., Tilman Schirmer, Erhard Hohenester, et al.. (1996). Crystal Structures and Solution Studies of Oxime Adducts of Mitochondrial Aspartate Aminotransferase. European Journal of Biochemistry. 236(3). 1025–1032. 28 indexed citations
8.
Panov, Kostya I., Andrei L. Okorokov, Tatiana B. Panova, et al.. (1996). Ribonuclease A mutant His119Asn: the role of histidine in catalysis. FEBS Letters. 398(1). 57–60. 18 indexed citations
9.
Okorokov, Andrei L., Kostya I. Panov, M.Ya. Karpeisky, et al.. (1996). Site‐directed mutagenesis of the base recognition loop of ribonuclease from Bacillus intermedius (binase). FEBS Letters. 384(2). 143–146. 7 indexed citations
10.
Okorokov, Andrei L., Kostya I. Panov, Robert te Poele, et al.. (1995). An Efficient System for Active Bovine Pancreatic Ribonuclease Expression in Escherichia coli. Protein Expression and Purification. 6(4). 472–480. 10 indexed citations
11.
Karpeisky, M.Ya., et al.. (1994). Formation and properties of S‐protein complex with S‐peptide‐containing fusion protein. FEBS Letters. 339(3). 209–212. 23 indexed citations
12.
Кулаева, О. Н., et al.. (1992). Biological activities of human interferon and 2??5? oligoadenylates in plants. Plant Molecular Biology. 20(3). 383–393. 14 indexed citations
13.
Karpeisky, M.Ya., et al.. (1992). Intramolecular interactions in pancreatic ribonucleases. Protein Science. 1(8). 1050–1060. 9 indexed citations
14.
Delbaere, Louis T. J., Joerg Kallen, Z. Marković-Housley, et al.. (1989). Complexes of aspartate aminotransferase with hydroxylamine derivatives: spectral studies in solution and in the crystalline state. Biochimie. 71(4). 449–459. 11 indexed citations
15.
Karpeisky, M.Ya., et al.. (1988). A route to 2′,5′‐oligoadenylates with increased stability towards phosphodiesterases. FEBS Letters. 236(2). 325–328. 10 indexed citations
16.
Karpeisky, M.Ya., et al.. (1987). A new scheme for the synthesis of 5′-nucleotide phosphonate analogs. Tetrahedron Letters. 28(31). 3623–3626. 8 indexed citations
17.
Ivanov, V. I., et al.. (1973). Conformational Properties and Catalytic Function of Aspartate Aminotransferase. European Journal of Biochemistry. 40(2). 519–526. 18 indexed citations
18.
Ivanov, V. I. & M.Ya. Karpeisky. (1969). Dynamic Three‐Dimensional Model for Enzymic Transamination. Advances in enzymology and related areas of molecular biology/Advances in enzymology and related subjects. 32. 21–53. 36 indexed citations
19.
Ivanov, V. I., et al.. (1968). The characteristics of alkyl substituted analogues of pyridoxal phosphate as coenzymes for aspartate transaminase. Biochemical and Biophysical Research Communications. 30(5). 459–464. 22 indexed citations
20.
Ivanov, V. I., et al.. (1964). Circular dichroism of aspartate transaminase. Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects. 92(2). 388–391. 17 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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