S. Rackovsky

3.3k total citations
86 papers, 2.7k citations indexed

About

S. Rackovsky is a scholar working on Molecular Biology, Materials Chemistry and Atomic and Molecular Physics, and Optics. According to data from OpenAlex, S. Rackovsky has authored 86 papers receiving a total of 2.7k indexed citations (citations by other indexed papers that have themselves been cited), including 68 papers in Molecular Biology, 35 papers in Materials Chemistry and 9 papers in Atomic and Molecular Physics, and Optics. Recurrent topics in S. Rackovsky's work include Protein Structure and Dynamics (54 papers), Enzyme Structure and Function (32 papers) and RNA and protein synthesis mechanisms (30 papers). S. Rackovsky is often cited by papers focused on Protein Structure and Dynamics (54 papers), Enzyme Structure and Function (32 papers) and RNA and protein synthesis mechanisms (30 papers). S. Rackovsky collaborates with scholars based in United States, Poland and Canada. S. Rackovsky's co-authors include Harold A. Scheraga, Matthew R. Pincus, Adam Liwo, Ryszard J. Wawak, Jooyoung Lee, H. A. Scheraga, R. Silbey, Igor B. Kuznetsov, H. Scher and Hagai Meirovitch and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Physical Review Letters and Journal of Biological Chemistry.

In The Last Decade

S. Rackovsky

84 papers receiving 2.6k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
S. Rackovsky United States 29 2.2k 1.3k 377 330 155 86 2.7k
Mark S. Friedrichs United States 23 1.7k 0.8× 744 0.6× 531 1.4× 493 1.5× 140 0.9× 38 2.7k
Christoph Klein United States 8 1.7k 0.8× 576 0.5× 304 0.8× 257 0.8× 249 1.6× 16 2.5k
Aritomo Shinozaki United States 9 1.4k 0.6× 721 0.6× 345 0.9× 158 0.5× 118 0.8× 10 2.5k
Osamu Miyashita Japan 26 1.8k 0.8× 986 0.8× 537 1.4× 253 0.8× 104 0.7× 115 2.8k
John Mongan United States 8 1.9k 0.8× 530 0.4× 499 1.3× 313 0.9× 317 2.0× 8 2.3k
Julia M. Goodfellow United Kingdom 25 1.8k 0.8× 665 0.5× 386 1.0× 341 1.0× 101 0.7× 84 2.4k
Wilson S. Ross United States 7 2.0k 0.9× 497 0.4× 368 1.0× 267 0.8× 239 1.5× 7 2.9k
Phineus R. L. Markwick United States 30 2.4k 1.1× 896 0.7× 445 1.2× 858 2.6× 149 1.0× 56 3.1k
Junichi Higo Japan 31 2.0k 0.9× 789 0.6× 517 1.4× 482 1.5× 234 1.5× 113 2.4k
Justin L. MacCallum Canada 25 3.3k 1.5× 915 0.7× 770 2.0× 484 1.5× 228 1.5× 53 4.0k

Countries citing papers authored by S. Rackovsky

Since Specialization
Citations

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

Fields of papers citing papers by S. Rackovsky

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of S. Rackovsky

This figure shows the co-authorship network connecting the top 25 collaborators of S. Rackovsky. A scholar is included among the top collaborators of S. Rackovsky 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 S. Rackovsky. S. Rackovsky 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.
Konkankit, Chilaluck C. & S. Rackovsky. (2023). Global Survey of Protein Dynamic Properties. The Journal of Physical Chemistry B. 127(27). 6073–6077. 1 indexed citations
2.
He, Yi, et al.. (2015). Alternative approach to protein structure prediction based on sequential similarity of physical properties. Proceedings of the National Academy of Sciences. 112(16). 5029–5032. 13 indexed citations
3.
He, Yi, Magdalena A. Mozolewska, Paweł Krupa, et al.. (2013). Lessons from application of the UNRES force field to predictions of structures of CASP10 targets. Proceedings of the National Academy of Sciences. 110(37). 14936–14941. 60 indexed citations
4.
Kuznetsov, Igor B. & S. Rackovsky. (2009). CFP: a web-server for constructing sequence-based protein conformational flexibility profiles. Bioinformation. 4(5). 176–178. 1 indexed citations
5.
Rackovsky, S., et al.. (2007). Information and discrimination in pairwise contact potentials. Proteins Structure Function and Bioinformatics. 71(3). 1071–1087. 15 indexed citations
6.
7.
Kuznetsov, Igor B. & S. Rackovsky. (2003). Class‐specific correlations between protein folding rate, structure‐derived, and sequence‐derived descriptors. Proteins Structure Function and Bioinformatics. 54(2). 333–341. 32 indexed citations
8.
Kuznetsov, Igor B. & S. Rackovsky. (2003). On the properties and sequence context of structurally ambivalent fragments in proteins. Protein Science. 12(11). 2420–2433. 37 indexed citations
9.
Kuznetsov, Igor B. & S. Rackovsky. (2003). Similarity between the C-terminal domain of the prion protein and chimpanzee cytomegalovirus glycoprotein UL9. Protein Engineering Design and Selection. 16(12). 861–863. 2 indexed citations
10.
Rackovsky, S., et al.. (2002). Optimally informative backbone structural propensities in proteins. Proteins Structure Function and Bioinformatics. 48(3). 463–486. 24 indexed citations
11.
Kuznetsov, Igor B. & S. Rackovsky. (2002). Discriminative ability with respect to amino acid types: Assessing the performance of knowledge‐based potentials without threading. Proteins Structure Function and Bioinformatics. 49(2). 266–284. 12 indexed citations
12.
Lee, Jooyoung, et al.. (1998). Conformational analysis of the 20-residue membrane-bound portion of melittin by conformational space annealing. Biopolymers. 46(2). 103–115. 60 indexed citations
13.
Lee, Jooyoung, Harold A. Scheraga, & S. Rackovsky. (1996). Computational study of packing a collagen-like molecule: Quasi-hexagonal vs “Smith” collagen microfibril model. Biopolymers. 40(6). 595–607. 11 indexed citations
14.
Kombo, David C., George Némethy, Kenneth D. Gibson, et al.. (1996). Effects on protein structure and function of replacing tryptophan with 5-hydroxytryptophan: Single-tryptophan mutants of the N-terminal domain of the bacteriophage λ repressor. Journal of Protein Chemistry. 15(1). 77–86. 3 indexed citations
15.
Liwo, Adam, Stanisław Ołdziej, Jerzy Ciarkowski, et al.. (1994). Prediction of conformation of rat galanin in the presence and absence of water with the use of monte Carlo methods and the ECEPP/3 force field. Journal of Protein Chemistry. 13(4). 375–380. 7 indexed citations
16.
Pincus, Matthew R., et al.. (1993). Unfolding and refolding of the native structure of bovine pancreatic trypsin inhibitor studied by computer simulations. Biochemistry. 32(37). 9614–9631. 26 indexed citations
17.
Liwo, Adam, Ryszard J. Wawak, Harold A. Scheraga, Matthew R. Pincus, & S. Rackovsky. (1993). Calculation of protein backbone geometry from α‐carbon coordinates based on peptide‐group dipole alignment. Protein Science. 2(10). 1697–1714. 81 indexed citations
18.
Chen, James, Grace Lee, Paul W. Brandt‐Rauf, et al.. (1990). Comparison of the predicted structure for the activated form of the P21 protein with the X-ray crystal structure. Journal of Protein Chemistry. 9(5). 543–547. 4 indexed citations
19.
Rackovsky, S.. (1990). Quantitative organization of the known protein x‐ray structures. I. Methods and short‐length‐scale results. Proteins Structure Function and Bioinformatics. 7(4). 378–402. 46 indexed citations
20.
Rackovsky, S. & Harold A. Scheraga. (1984). Differential geometry and protein folding. Accounts of Chemical Research. 17(6). 209–214. 28 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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