S. Trakhanov

2.8k total citations
31 papers, 2.1k citations indexed

About

S. Trakhanov is a scholar working on Molecular Biology, Materials Chemistry and Oncology. According to data from OpenAlex, S. Trakhanov has authored 31 papers receiving a total of 2.1k indexed citations (citations by other indexed papers that have themselves been cited), including 26 papers in Molecular Biology, 11 papers in Materials Chemistry and 5 papers in Oncology. Recurrent topics in S. Trakhanov's work include RNA and protein synthesis mechanisms (14 papers), Enzyme Structure and Function (10 papers) and Protein Structure and Dynamics (9 papers). S. Trakhanov is often cited by papers focused on RNA and protein synthesis mechanisms (14 papers), Enzyme Structure and Function (10 papers) and Protein Structure and Dynamics (9 papers). S. Trakhanov collaborates with scholars based in United States, Russia and Germany. S. Trakhanov's co-authors include Harry F. Noller, Martin Laurberg, А.A. Коростелев, Florante A. Quiocho, Haruichi Asahara, Jianyu Zhu, Dirk Görlich, Laura Lancaster, Tino Pleiner and Hema Chug and has published in prestigious journals such as Nature, Science and Cell.

In The Last Decade

S. Trakhanov

31 papers receiving 2.1k 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. Trakhanov United States 22 1.8k 412 300 200 125 31 2.1k
Voula Kanelis Canada 20 1.8k 1.0× 282 0.7× 265 0.9× 175 0.9× 97 0.8× 34 2.4k
Lisa D. Cabrita United Kingdom 28 1.6k 0.9× 285 0.7× 325 1.1× 148 0.7× 151 1.2× 57 2.1k
Oliver Ohlenschläger Germany 29 1.4k 0.8× 141 0.3× 323 1.1× 159 0.8× 120 1.0× 102 2.1k
Thorsten Dieckmann United States 27 1.7k 0.9× 164 0.4× 149 0.5× 99 0.5× 53 0.4× 58 2.1k
Gabriela C. Pérez-Alvarado United States 16 1.4k 0.8× 132 0.3× 277 0.9× 104 0.5× 78 0.6× 17 1.8k
Alex U. Singer Canada 18 2.2k 1.2× 255 0.6× 505 1.7× 201 1.0× 100 0.8× 28 3.0k
Tai-he Xia Sweden 5 1.5k 0.8× 179 0.4× 319 1.1× 134 0.7× 78 0.6× 6 1.8k
Lukáš Trantı́rek Czechia 30 2.2k 1.2× 165 0.4× 174 0.6× 87 0.4× 67 0.5× 83 2.6k
Jason Key United States 13 1.3k 0.7× 184 0.4× 172 0.6× 128 0.6× 44 0.4× 20 1.9k
Woonghee Lee United States 18 1.9k 1.0× 136 0.3× 370 1.2× 151 0.8× 145 1.2× 62 2.4k

Countries citing papers authored by S. Trakhanov

Since Specialization
Citations

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

Fields of papers citing papers by S. Trakhanov

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

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

This figure shows the co-authorship network connecting the top 25 collaborators of S. Trakhanov. A scholar is included among the top collaborators of S. Trakhanov 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. Trakhanov. S. Trakhanov 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.
Fu, Zhenglin, Thomas Güttler, S. Trakhanov, et al.. (2024). A checkpoint function for Nup98 in nuclear pore formation suggested by novel inhibitory nanobodies. The EMBO Journal. 43(11). 2198–2232. 4 indexed citations
2.
Trakhanov, S., et al.. (2016). Structure of the exportin Xpo4 in complex with RanGTP and the hypusine-containing translation factor eIF5A. Nature Communications. 7(1). 11952–11952. 42 indexed citations
3.
Zhou, Jie, Laura Lancaster, S. Trakhanov, & Harry F. Noller. (2011). Crystal structure of release factor RF3 trapped in the GTP state on a rotated conformation of the ribosome. RNA. 18(2). 230–240. 70 indexed citations
4.
Laurberg, Martin, Haruichi Asahara, А.A. Коростелев, et al.. (2008). Structural basis for translation termination on the 70S ribosome. Nature. 454(7206). 852–857. 269 indexed citations
5.
Коростелев, А.A., Haruichi Asahara, Laura Lancaster, et al.. (2008). Crystal structure of a translation termination complex formed with release factor RF2. Proceedings of the National Academy of Sciences. 105(50). 19684–19689. 198 indexed citations
6.
Коростелев, А.A., S. Trakhanov, Martin Laurberg, & Harry F. Noller. (2006). Crystal Structure of a 70S Ribosome-tRNA Complex Reveals Functional Interactions and Rearrangements. Cell. 126(6). 1065–1077. 400 indexed citations
7.
8.
Segelke, Brent W., Michael Forstner, S. Trakhanov, et al.. (2000). Conformational flexibility in the apolipoprotein E amino‐terminal domain structure determined from three new crystal forms: Implications for lipid binding. Protein Science. 9(5). 886–897. 41 indexed citations
9.
Trakhanov, S., Sean Parkin, Robert L. Raffaı̈, et al.. (1999). Structure of a monoclonal 2E8 Fab antibody fragment specific for the low-density lipoprotein-receptor binding region of apolipoprotein E refined at 1.9 Å. Acta Crystallographica Section D Biological Crystallography. 55(1). 122–128. 12 indexed citations
10.
11.
Dong, Liming, Sean Parkin, S. Trakhanov, et al.. (1996). Novel mechanism for defective receptor binding of apolipoprotein E2 in type III hyperlipoproteinemia. Nature Structural & Molecular Biology. 3(8). 718–722. 99 indexed citations
12.
Trakhanov, S., et al.. (1995). 2 .ANG. Resolution Structure of DppA, a Periplasmic Dipeptide Transport/Chemosensory Receptor. Biochemistry. 34(51). 16585–16595. 78 indexed citations
13.
Trakhanov, S. & Florante A. Quiocho. (1995). Influence of divalent cations in protein crystallization. Protein Science. 4(9). 1914–1919. 40 indexed citations
14.
Yao, Nanhua, S. Trakhanov, & Florante A. Quiocho. (1994). Refined 1.89-.ANG. Structure of the Histidine-Binding Protein Complexed with Histidine and Its Relationship with Many Other Active Transport/Chemosensory Proteins. Biochemistry. 33(16). 4769–4779. 91 indexed citations
15.
Trakhanov, S., A. I. Grebenko, Vladimir A. Shirokov, et al.. (1991). Crystallization of protein and ribosomal particles in microgravity. Journal of Crystal Growth. 110(1-2). 317–321. 22 indexed citations
16.
Mikhailov, A.M., et al.. (1990). Crystallization and preliminary x‐ray diffraction study of neurotoxin‐I from Naja naja oxiana VENOM. FEBS Letters. 269(1). 255–257. 3 indexed citations
17.
Trakhanov, S., et al.. (1989). Crystallization and preliminary X-ray crystallographic data of a histidine-binding protein from Escherichia coli. Journal of Molecular Biology. 207(4). 847–849. 10 indexed citations
18.
Trakhanov, S., Marat Yusupov, В. Б. Широков, et al.. (1989). Preliminary X-ray investigation of 70 S ribosome crystals from Thermus thermophilus. Journal of Molecular Biology. 209(2). 327–328. 35 indexed citations
19.
Yusupov, Marat, et al.. (1988). A new crystalline form of 30 S ribosomal subunits from Thermus thermophilus. FEBS Letters. 238(1). 113–115. 16 indexed citations
20.
Плетнев, В. З., et al.. (1981). Three‐dimensional structure of actinoxanthin. III. A 4‐Å resolution. Biopolymers. 20(4). 679–694. 6 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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