Edward E. Melnikov

762 total citations
19 papers, 598 citations indexed

About

Edward E. Melnikov is a scholar working on Molecular Biology, Materials Chemistry and Genetics. According to data from OpenAlex, Edward E. Melnikov has authored 19 papers receiving a total of 598 indexed citations (citations by other indexed papers that have themselves been cited), including 16 papers in Molecular Biology, 14 papers in Materials Chemistry and 10 papers in Genetics. Recurrent topics in Edward E. Melnikov's work include Enzyme Structure and Function (14 papers), Bacterial Genetics and Biotechnology (10 papers) and RNA and protein synthesis mechanisms (6 papers). Edward E. Melnikov is often cited by papers focused on Enzyme Structure and Function (14 papers), Bacterial Genetics and Biotechnology (10 papers) and RNA and protein synthesis mechanisms (6 papers). Edward E. Melnikov collaborates with scholars based in Russia and United States. Edward E. Melnikov's co-authors include Т. В. Ротанова, Alla Gustchina, Alexander Wlodawer, Istvan Botos, Fatima Rasulova, Michael R. Maurizi, Scott Cherry, Joseph E. Tropea, Zbigniew Dauter and Mi Li and has published in prestigious journals such as Journal of Biological Chemistry, Journal of Molecular Biology and FEBS Letters.

In The Last Decade

Edward E. Melnikov

19 papers receiving 591 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Edward E. Melnikov Russia 10 509 234 219 86 68 19 598
Т. В. Ротанова Russia 15 726 1.4× 357 1.5× 315 1.4× 113 1.3× 84 1.2× 41 843
Fatima Rasulova United States 11 465 0.9× 262 1.1× 161 0.7× 76 0.9× 49 0.7× 12 664
Sreedevi Nallamsetty United States 10 572 1.1× 160 0.7× 72 0.3× 46 0.5× 58 0.9× 10 711
Noël Molière Germany 7 310 0.6× 186 0.8× 93 0.4× 44 0.5× 25 0.4× 7 408
Dominique Villeval France 11 314 0.6× 223 1.0× 57 0.3× 70 0.8× 41 0.6× 14 520
Paul Wolfe United States 9 740 1.5× 516 2.2× 128 0.6× 101 1.2× 48 0.7× 11 886
G W Henderson United States 6 322 0.6× 198 0.8× 92 0.4× 38 0.4× 25 0.4× 7 414
Lynn G. Kleina United States 8 923 1.8× 397 1.7× 133 0.6× 22 0.3× 44 0.6× 9 1.0k
Ahmad Jomaa United States 17 628 1.2× 224 1.0× 89 0.4× 127 1.5× 20 0.3× 24 733
Karen R. Silber United States 7 391 0.8× 231 1.0× 72 0.3× 31 0.4× 26 0.4× 8 467

Countries citing papers authored by Edward E. Melnikov

Since Specialization
Citations

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

Fields of papers citing papers by Edward E. Melnikov

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Edward E. Melnikov. 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 Edward E. Melnikov. The network helps show where Edward E. Melnikov may publish in the future.

Co-authorship network of co-authors of Edward E. Melnikov

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

All Works

19 of 19 papers shown
1.
Melnikov, Edward E. & Т. В. Ротанова. (2010). Molecular chaperones. Russian Journal of Bioorganic Chemistry. 36(1). 1–10. 9 indexed citations
2.
Li, Mi, Alla Gustchina, Fatima Rasulova, et al.. (2010). Structure of the N-terminal fragment ofEscherichia coliLon protease. Acta Crystallographica Section D Biological Crystallography. 66(8). 865–873. 30 indexed citations
3.
Melnikov, Edward E., et al.. (2010). Isolation and determination of the activity of IgA1 protease from Neisseria meningitidis. Russian Journal of Bioorganic Chemistry. 36(1). 81–89. 8 indexed citations
4.
Ротанова, Т. В. & Edward E. Melnikov. (2010). A novel view on the architecture of the non-catalytic N-terminal region of ATP-dependent LonA proteases. Biochemistry (Moscow) Supplement Series B Biomedical Chemistry. 4(4). 404–408. 7 indexed citations
5.
Ротанова, Т. В. & Edward E. Melnikov. (2008). The ATP-dependent proteases and proteolytic complexes involved into intracellular protein degradation. Biochemistry (Moscow) Supplement Series B Biomedical Chemistry. 2(3). 245–257. 5 indexed citations
6.
Melnikov, Edward E., Anton A. Stepnov, Istvan Botos, et al.. (2008). Limited proteolysis of E. coli ATP-dependent protease Lon - a unified view of the subunit architecture and characterization of isolated enzyme fragments.. Acta Biochimica Polonica. 55(2). 281–296. 18 indexed citations
7.
Melnikov, Edward E., Anton A. Stepnov, Istvan Botos, et al.. (2008). Limited proteolysis of E. coli ATP-dependent protease Lon - a unified view of the subunit architecture and characterization of isolated enzyme fragments.. PubMed. 55(2). 281–96. 19 indexed citations
8.
Ротанова, Т. В., Istvan Botos, Edward E. Melnikov, et al.. (2006). Slicing a protease: Structural features of the ATP‐dependent Lon proteases gleaned from investigations of isolated domains. Protein Science. 15(8). 1815–1828. 73 indexed citations
9.
Botos, Istvan, Edward E. Melnikov, Scott Cherry, et al.. (2005). Atomic-resolution Crystal Structure of the Proteolytic Domain of Archaeoglobus fulgidus Lon Reveals the Conformational Variability in the Active Sites of Lon Proteases. Journal of Molecular Biology. 351(1). 144–157. 43 indexed citations
10.
Li, Mi, Fatima Rasulova, Edward E. Melnikov, et al.. (2005). Crystal structure of the N‐terminal domain of E. coli Lon protease. Protein Science. 14(11). 2895–2900. 44 indexed citations
11.
Ротанова, Т. В., et al.. (2004). Classification of ATP‐dependent proteases Lon and comparison of the active sites of their proteolytic domains. European Journal of Biochemistry. 271(23-24). 4865–4871. 79 indexed citations
12.
Botos, Istvan, Edward E. Melnikov, Scott Cherry, et al.. (2004). The Catalytic Domain of Escherichia coli Lon Protease Has a Unique Fold and a Ser-Lys Dyad in the Active Site. Journal of Biological Chemistry. 279(9). 8140–8148. 152 indexed citations
13.
Botos, Istvan, Edward E. Melnikov, Scott Cherry, et al.. (2003). Crystal structure of the AAA+ α domain of E. coli Lon protease at 1.9Å resolution. Journal of Structural Biology. 146(1-2). 113–122. 69 indexed citations
14.
Melnikov, Edward E., et al.. (2003). Proteolysis Coupled to ATP Hydrolysis: Regulation of the Activity of Proteolytic Sites of Lon Protease from Escherichia coli. Russian Journal of Bioorganic Chemistry. 29(5). 441–449. 2 indexed citations
15.
Melnikov, Edward E., et al.. (2001). Coupling of Proteolysis to ATP Hydrolysis upon Escherichia coliLon Protease Functioning: II. Hydrolysis of ATP and Activity of the Enzyme Peptide Hydrolase Sites. Russian Journal of Bioorganic Chemistry. 27(2). 101–109. 6 indexed citations
16.
Melnikov, Edward E., et al.. (2000). Coupling of proteolysis to ATP hydrolysis uponEscherichia coli lon protease functioning: I. kinetic aspects of ATP hydrolysis. Russian Journal of Bioorganic Chemistry. 26(7). 474–481. 6 indexed citations
17.
Манухов, И. В., et al.. (1999). [A test system based on the lux-regulon from Vibrio fischeri for studying the functional activity of mutant forms of Escherichia coli lon-proteinase].. PubMed. 25(5). 365–8. 2 indexed citations
18.
Melnikov, Edward E., et al.. (1998). [In vitro coupling of ATP hydrolysis to proteolysis of ATP site mutant forms of Lon-proteinase from E.coli].. PubMed. 24(4). 293–9. 3 indexed citations
19.
Rasulova, Fatima, et al.. (1998). The isolated proteolytic domain of Escherichia coli ATP‐dependent protease Lon exhibits the peptidase activity. FEBS Letters. 432(3). 179–181. 23 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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