L. Reshetnikova

2.4k total citations · 1 hit paper
31 papers, 2.0k citations indexed

About

L. Reshetnikova is a scholar working on Molecular Biology, Materials Chemistry and Genetics. According to data from OpenAlex, L. Reshetnikova has authored 31 papers receiving a total of 2.0k indexed citations (citations by other indexed papers that have themselves been cited), including 26 papers in Molecular Biology, 18 papers in Materials Chemistry and 5 papers in Genetics. Recurrent topics in L. Reshetnikova's work include Enzyme Structure and Function (17 papers), RNA and protein synthesis mechanisms (16 papers) and Protein Structure and Dynamics (6 papers). L. Reshetnikova is often cited by papers focused on Enzyme Structure and Function (17 papers), RNA and protein synthesis mechanisms (16 papers) and Protein Structure and Dynamics (6 papers). L. Reshetnikova collaborates with scholars based in Russia, United States and Denmark. L. Reshetnikova's co-authors include Poul Nissen, Jens Nyborg, Søren Thirup, Galina Polekhina, Brian F.C. Clark, Morten Kjeldgaard, Rolf Hilgenfeld, Harald Berchtold, Norbert K. Schirmer and Mathias Sprinzl and has published in prestigious journals such as Nature, Science and Proceedings of the National Academy of Sciences.

In The Last Decade

L. Reshetnikova

31 papers receiving 2.0k citations

Hit Papers

align trajectories

What are hit papers?

Hit papers significantly outperform the citation benchmark for their cohort. A paper qualifies if it has ≥500 total citations, achieves ≥1.5× the top-1% citation threshold for papers in the same subfield and year (this is the minimum needed to enter the top 1%, not the average within it), or reaches the top citation threshold in at least one of its specific research topics.

Crystal Structure of the Ternary Complex of Phe-tRNA ^Phe , EF-Tu, and a GTP Analog

1995 718 citations Poul Nissen, Morten Kjeldgaard et al. profile →

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
L. Reshetnikova Russia	14	1.8k	424	299	137	99	31	2.0k
François Bontems France	23	1.5k 0.8×	610 1.4×	110 0.4×	148 1.1×	176 1.8×	49	1.9k
Hosahalli S. Subramanya India	12	1.6k 0.9×	500 1.2×	212 0.7×	50 0.4×	199 2.0×	19	1.8k
A.E. Hodel United States	19	1.6k 0.9×	172 0.4×	273 0.9×	42 0.3×	116 1.2×	26	1.9k
M. A. Tukalo Ukraine	22	2.7k 1.5×	474 1.1×	316 1.1×	34 0.2×	68 0.7×	100	3.0k
Gilbert Eriani France	26	3.1k 1.7×	616 1.5×	279 0.9×	155 1.1×	106 1.1×	87	3.4k
Kakoli Mitra United States	9	1.2k 0.7×	295 0.7×	255 0.9×	49 0.4×	132 1.3×	10	1.5k
Dmitri N. Ermolenko United States	25	2.5k 1.4×	394 0.9×	297 1.0×	201 1.5×	188 1.9×	49	2.7k
Vito Graziano United States	20	1.4k 0.8×	319 0.8×	219 0.7×	28 0.2×	119 1.2×	30	1.9k
Nancy C. Horton United States	20	1.7k 1.0×	532 1.3×	305 1.0×	27 0.2×	198 2.0×	49	2.0k
Richard C. Ogden United States	20	1.9k 1.0×	208 0.5×	271 0.9×	24 0.2×	111 1.1×	30	2.2k

Countries citing papers authored by L. Reshetnikova

Since Specialization

Citations

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

Fields of papers citing papers by L. Reshetnikova

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of L. Reshetnikova

This figure shows the co-authorship network connecting the top 25 collaborators of L. Reshetnikova. A scholar is included among the top collaborators of L. Reshetnikova 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 L. Reshetnikova. L. Reshetnikova is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

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20 of 20 papers shown

Reshetnikova, L., et al.. (2013). Purification, crystallization and preliminary X-ray crystallographic analysis of squid heavy meromyosin. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 69(3). 248–252. 6 indexed citations

Kumar, V.S.S., L. Reshetnikova, Jerry H. Brown, et al.. (2011). Crystal Structure of a Phosphorylated Light Chain Domain of Scallop Smooth-Muscle Myosin. Biophysical Journal. 101(9). 2185–2189. 3 indexed citations

Guo, Wei, Karen M. Routzahn, Yijun Gu, et al.. (2002). Crystallization and preliminary X-ray diffraction studies of NusG, a protein shared by the transcription and translation machines. Acta Crystallographica Section D Biological Crystallography. 58(12). 2157–2158. 6 indexed citations

Gu, Yijun, L. Reshetnikova, Yue Li, et al.. (2002). Crystal Structure of Shikimate Kinase from Mycobacterium tuberculosis Reveals the Dynamic Role of the LID Domain in Catalysis. Journal of Molecular Biology. 319(3). 779–789. 61 indexed citations

Gu, Yijun, L. Reshetnikova, Yue Li, et al.. (2001). Crystallization and preliminary X-ray diffraction analysis of shikimate kinase fromMycobacterium tuberculosisin complex with MgADP. Acta Crystallographica Section D Biological Crystallography. 57(12). 1870–1871. 6 indexed citations

Reshetnikova, L., Nina Moor, Olga I. Lavrik, & Dmitry G. Vassylyev. (1999). Crystal structures of phenylalanyl-tRNA synthetase complexed with phenylalanine and a phenylalanyl-adenylate analogue. Journal of Molecular Biology. 287(3). 555–568. 61 indexed citations

Goldgur, Yehuda, Lidia Mosyak, L. Reshetnikova, et al.. (1997). The crystal structure of phenylalanyl-tRNA synthetase from Thermus thermophilus complexed with cognate tRNAPhe. Structure. 5(1). 59–68. 167 indexed citations

Nyborg, Jens, Poul Nissen, Morten Kjeldgaard, et al.. (1997). Macromolecular mimicry in protein biosynthesis. PubMed. 2(3). S7–S11. 5 indexed citations

Kristensen, O., L. Reshetnikova, Poul Nissen, et al.. (1996). Isolation, crystallization and X‐ray analysis of the quaternary complex of Phe‐tRNA^Phe, EF‐Tu, a GTP analog and kirromycin. FEBS Letters. 399(1-2). 59–62. 10 indexed citations

10.

Nyborg, Jens, Poul Nissen, Søren Thirup, et al.. (1996). Structure of the ternary complex of EF-Tu: macromolecular mimicry in translation. Trends in Biochemical Sciences. 21(3). 81–82. 53 indexed citations

11.

Hoffman, Ross C., Beverly J. Castner, Mary Gerhart, et al.. (1995). Direct evidence of a heterotrimeric complex of human interleukin‐4 with its receptors. Protein Science. 4(3). 382–386. 10 indexed citations

12.

Wlodawer, Alexander, Alla Gustchina, L. Reshetnikova, et al.. (1995). Structure of an inhibitor complex of the proteinase from feline immunodeficiency virus. Nature Structural & Molecular Biology. 2(6). 480–488. 55 indexed citations

13.

Mosyak, Lidia, L. Reshetnikova, Yehuda Goldgur, Marc Delarue, & Mark Safro. (1995). Structure of phenylalanyl-tRNA synthetase from Thermus thermophilus. Nature Structural Biology. 2(7). 537–547. 133 indexed citations

14.

Nissen, Poul, L. Reshetnikova, Gunhild E. Siboska, et al.. (1994). Purification and crystallization of the ternary complex of elongation factor Tu:GTP and Phe‐tRNA^Phe. FEBS Letters. 356(2-3). 165–168. 12 indexed citations

15.

Reshetnikova, L., С. Н. Ходырева, Olga I. Lavrik, et al.. (1993). Crystals of the Phenylalanyl-tRNA Synthetase from Thermus thermophilus HB8 Complexed with tRNAPhe. Journal of Molecular Biology. 231(3). 927–929. 11 indexed citations

16.

Berchtold, Harald, L. Reshetnikova, Christian O. A. Reiser, et al.. (1993). Crystal structure of active elongation factor Tu reveals major domain rearrangements. Nature. 365(6442). 126–132. 463 indexed citations

17.

Reshetnikova, L., V.N. Ankilova, Olga I. Lavrik, et al.. (1992). Three‐dimensional structure of phenylalanyl‐transfer RNA synthetase from Thermus thermophilus HB8 at 0.6‐nm resolution. European Journal of Biochemistry. 208(2). 411–417. 9 indexed citations

18.

Reshetnikova, L., et al.. (1991). Crystals of intact elongation factor Tu from Thermus thermophilus diffracting to high resolution. Journal of Molecular Biology. 221(2). 375–377. 7 indexed citations

19.

Korolev, Sergey, et al.. (1987). Preliminary crystallographic study of the phenylalanyl-tRNA synthetase from Thermus thermophilus HB8. Journal of Molecular Biology. 198(3). 555–556. 19 indexed citations

20.

Reshetnikova, L., et al.. (1973). DOUBLE FLUORIDES OF COMPOSITION K3LNF6 (LN=SM-LU, Y). Proceedings of the USSR Academy of Sciences. 213(1). 98–100. 5 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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