Oleg B. Ptitsyn

11.1k total citations · 4 hit papers
130 papers, 9.5k citations indexed

About

Oleg B. Ptitsyn is a scholar working on Molecular Biology, Materials Chemistry and Cell Biology. According to data from OpenAlex, Oleg B. Ptitsyn has authored 130 papers receiving a total of 9.5k indexed citations (citations by other indexed papers that have themselves been cited), including 91 papers in Molecular Biology, 62 papers in Materials Chemistry and 19 papers in Cell Biology. Recurrent topics in Oleg B. Ptitsyn's work include Protein Structure and Dynamics (71 papers), Enzyme Structure and Function (53 papers) and RNA and protein synthesis mechanisms (21 papers). Oleg B. Ptitsyn is often cited by papers focused on Protein Structure and Dynamics (71 papers), Enzyme Structure and Function (53 papers) and RNA and protein synthesis mechanisms (21 papers). Oleg B. Ptitsyn collaborates with scholars based in Russia, United States and United Kingdom. Oleg B. Ptitsyn's co-authors include Alexei V. Finkelstein, Valentina E. Bychkova, Vladimir N. Uversky, Gennady V. Semisotnov, Roger H. Pain, Д. А. Долгих, Rudolf Gilmanshin, Eva Žerovnik, E. I. Tiktopulo and Е. В. Бражников and has published in prestigious journals such as Nature, Journal of Molecular Biology and Biochemistry.

In The Last Decade

Oleg B. Ptitsyn

127 papers receiving 9.2k citations

Hit Papers

Molten Globule and Protein Folding 1981 2026 1996 2011 1995 1990 1981 1987 250 500 750 1000

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Oleg B. Ptitsyn Russia 50 7.6k 4.2k 1.1k 1.0k 924 130 9.5k
D. Wayne Bolen United States 44 7.3k 1.0× 3.5k 0.8× 1.3k 1.1× 567 0.6× 911 1.0× 70 9.3k
J. Martin Scholtz United States 45 8.5k 1.1× 3.0k 0.7× 748 0.7× 492 0.5× 1.2k 1.3× 91 10.9k
Jen Tsi Yang United States 42 8.9k 1.2× 1.7k 0.4× 1.3k 1.2× 644 0.6× 2.0k 2.2× 127 12.4k
George D. Rose United States 52 10.9k 1.4× 5.1k 1.2× 846 0.8× 390 0.4× 1.9k 2.0× 112 12.6k
F.M. Richards United States 31 8.7k 1.1× 3.1k 0.7× 1.0k 0.9× 225 0.2× 1.5k 1.6× 47 11.4k
Thomas E. Creighton United Kingdom 66 12.0k 1.6× 4.4k 1.1× 3.8k 3.4× 538 0.5× 1.2k 1.3× 141 14.6k
P. Kraulis Sweden 16 12.1k 1.6× 4.2k 1.0× 1.6k 1.5× 594 0.6× 678 0.7× 18 16.1k
John F. Brandts United States 39 6.1k 0.8× 1.8k 0.4× 684 0.6× 326 0.3× 913 1.0× 71 8.0k
Robert W. Woody United States 46 8.3k 1.1× 2.2k 0.5× 914 0.8× 439 0.4× 2.4k 2.6× 114 11.9k
Kunihiro Kuwajima Japan 43 6.8k 0.9× 4.1k 1.0× 729 0.7× 1.8k 1.8× 629 0.7× 141 8.2k

Countries citing papers authored by Oleg B. Ptitsyn

Since Specialization
Citations

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

Fields of papers citing papers by Oleg B. Ptitsyn

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Oleg B. Ptitsyn. 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 Oleg B. Ptitsyn. The network helps show where Oleg B. Ptitsyn may publish in the future.

Co-authorship network of co-authors of Oleg B. Ptitsyn

This figure shows the co-authorship network connecting the top 25 collaborators of Oleg B. Ptitsyn. A scholar is included among the top collaborators of Oleg B. Ptitsyn 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 Oleg B. Ptitsyn. Oleg B. Ptitsyn 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.
Ptitsyn, Oleg B.. (1998). Protein folding and protein evolution: common folding nucleus in different subfamilies of c-type cytochromes?. Journal of Molecular Biology. 278(3). 655–666. 111 indexed citations
2.
Ptitsyn, Oleg B.. (1996). How molten is the molten globule?. Nature Structural & Molecular Biology. 3(6). 488–490. 54 indexed citations
3.
Ptitsyn, Oleg B., Valentina E. Bychkova, & Vladimir N. Uversky. (1995). Kinetic and equilibrium folding intermediates. Philosophical Transactions of the Royal Society B Biological Sciences. 348(1323). 35–41. 93 indexed citations
4.
Ptitsyn, Oleg B.. (1994). Kinetic and equilibrium intermediates in protein folding. Protein Engineering Design and Selection. 7(5). 593–596. 76 indexed citations
5.
Ptitsyn, Oleg B. & Vladimir N. Uversky. (1994). The molten globule is a third thermodynamical state of protein molecules. FEBS Letters. 341(1). 15–18. 142 indexed citations
6.
Ptitsyn, Oleg B., et al.. (1993). Mechanism of pH‐induced release of retinol from retinol‐binding protein. FEBS Letters. 317(3). 181–184. 18 indexed citations
7.
Fedorov, A. N., Д. А. Долгих, Violetta V. Chemeris, et al.. (1992). De novo design, synthesis and study of albebetin, a polypeptide with a predetermined three-dimensional structure. Journal of Molecular Biology. 225(4). 927–931. 52 indexed citations
8.
Crane‐Robinson, Colyn & Oleg B. Ptitsyn. (1989). Binding of the globular domain of linker histones H5/H1 to the nucleosome: a hypothesis. Protein Engineering Design and Selection. 2(8). 577–582. 34 indexed citations
9.
Ptitsyn, Oleg B. & Alexei V. Finkelstein. (1989). Prediction of protein secondary structure based on physical theory. Histones. Protein Engineering Design and Selection. 2(6). 443–447. 15 indexed citations
10.
Semisotnov, Gennady V., et al.. (1987). Sequential mechanism of refolding of carbonic anhydrase B. FEBS Letters. 224(1). 9–13. 185 indexed citations
11.
Damaschun, G., et al.. (1986). Large-angle diffuse X-ray scattering from a homopolypeptide and some proteins. 112. 213–219. 1 indexed citations
12.
Ptitsyn, Oleg B.. (1985). Random sequences and protein folding. Journal of Molecular Structure THEOCHEM. 24(1-2). 45–65. 2 indexed citations
13.
Бражников, Е. В., Yu. N. Chirgadze, Д. А. Долгих, & Oleg B. Ptitsyn. (1985). Noncooperative temperature melting of a globular protein without specific tertiary structure: Acid form of bovine carbonic anhydrase B. Biopolymers. 24(10). 1899–1907. 28 indexed citations
14.
Ptitsyn, Oleg B., Alexei V. Finkelstein, & Alexey G. Murzin. (1985). Structural model for interferons. FEBS Letters. 186(2). 143–148. 21 indexed citations
16.
Ptitsyn, Oleg B., et al.. (1971). Thermodynamic parameters of helix‐coil transition in polypeptide chains I. Poly‐(L‐glutamic acid). Biopolymers. 10(11). 2161–2179. 56 indexed citations
17.
Birshtein, T.M. & Oleg B. Ptitsyn. (1967). The structure and flexibility of stereoregular macromolecules. The model of statistical zigzag chain. Journal of Polymer Science Part C Polymer Symposia. 16(8). 4617–4622. 3 indexed citations
18.
Nekrasova, T. N., et al.. (1965). Potentiometric titration of polyacrylic acid, polymethacrylic acid and poly-l-glutamic acid. Polymer Science U.S.S.R.. 7(5). 1008–1018. 21 indexed citations
19.
Ptitsyn, Oleg B.. (1960). Geometry of linear polymers—VI. The theory of volume effects in polymer chains. Polymer Science U.S.S.R.. 1(2). 259–275. 2 indexed citations
20.
Birshtein, T.M. & Oleg B. Ptitsyn. (1960). Stereospecificity of polymers as a function of the conditions of polymerization. Polymer Science U.S.S.R.. 1(2). 288–294. 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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