Л. Д. Румш

970 total citations
68 papers, 800 citations indexed

About

Л. Д. Румш is a scholar working on Molecular Biology, Oncology and Microbiology. According to data from OpenAlex, Л. Д. Румш has authored 68 papers receiving a total of 800 indexed citations (citations by other indexed papers that have themselves been cited), including 33 papers in Molecular Biology, 28 papers in Oncology and 13 papers in Microbiology. Recurrent topics in Л. Д. Румш's work include Peptidase Inhibition and Analysis (27 papers), Bacterial Infections and Vaccines (11 papers) and Enzyme Production and Characterization (10 papers). Л. Д. Румш is often cited by papers focused on Peptidase Inhibition and Analysis (27 papers), Bacterial Infections and Vaccines (11 papers) and Enzyme Production and Characterization (10 papers). Л. Д. Румш collaborates with scholars based in Russia, Mexico and Belarus. Л. Д. Румш's co-authors include N. S. Andreeva, V.K. Antonov, Lioudmila Fomina, Thomas Haertlé, E. A. Bonch-Osmolovskaya, Ilya V. Kublanov, Т. В. Ротанова, Serguei Fomine, G. B. Slobodkina and Anna A. Perevalova and has published in prestigious journals such as Applied and Environmental Microbiology, Macromolecules and FEBS Letters.

In The Last Decade

Л. Д. Румш

67 papers receiving 773 citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Л. Д. Румш Russia	14	480	193	151	93	89	68	800
Jean‐François Petit France	19	424 0.9×	117 0.6×	73 0.5×	88 0.9×	107 1.2×	28	1.0k
G.A. Bezerra Brazil	20	481 1.0×	105 0.5×	72 0.5×	77 0.8×	133 1.5×	46	894
Yeon Gyu Yu South Korea	20	790 1.6×	72 0.4×	90 0.6×	203 2.2×	81 0.9×	73	1.2k
Nicholas C. Price United Kingdom	16	667 1.4×	76 0.4×	93 0.6×	179 1.9×	89 1.0×	24	1.2k
N.R. Silvaggi United States	20	557 1.2×	195 1.0×	55 0.4×	268 2.9×	153 1.7×	37	1.2k
M. Fairhead United Kingdom	18	679 1.4×	80 0.4×	109 0.7×	94 1.0×	102 1.1×	30	1.3k
Éva Moussong Hungary	5	712 1.5×	71 0.4×	62 0.4×	135 1.5×	65 0.7×	7	1.1k
Otto Phanstiel United States	24	1.1k 2.3×	136 0.7×	85 0.6×	85 0.9×	443 5.0×	76	1.7k
Caroline Louis‐Jeune Canada	4	546 1.1×	54 0.3×	53 0.4×	77 0.8×	51 0.6×	4	776
Jozef Ševčı́k Slovakia	16	891 1.9×	67 0.3×	185 1.2×	284 3.1×	70 0.8×	34	1.3k

Countries citing papers authored by Л. Д. Румш

Since Specialization

Citations

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

Fields of papers citing papers by Л. Д. Румш

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Л. Д. Румш. 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 Л. Д. Румш. The network helps show where Л. Д. Румш may publish in the future.

Co-authorship network of co-authors of Л. Д. Румш

This figure shows the co-authorship network connecting the top 25 collaborators of Л. Д. Румш. A scholar is included among the top collaborators of Л. Д. Румш 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 Л. Д. Румш. Л. Д. Румш 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

Гордеева, Е. А., et al.. (2019). Protective potency of recombinant meningococcal IgA1 protease and its structural derivatives upon animal invasion with meningococcal and pneumococcal infections. Microbes and Infection. 21(7). 336–340. 5 indexed citations

Zinchenko, Anatoly, et al.. (2018). Peculiarities of the Formation of Antimeningococcus Immunity in Mice Immunized with Fragments of N. meningitidis IgA1 Protease. Bulletin of Experimental Biology and Medicine. 165(6). 763–766. 1 indexed citations

Zakharova, Maria Yu., А. А. Кузнецова, A. V. Kolesnikov, et al.. (2017). Evolution of inhibitor-resistant natural mutant forms of HIV-1 protease probed by pre-steady state kinetic analysis. Biochimie. 142. 125–134. 1 indexed citations

Zinchenko, Anatoly, et al.. (2016). Potential Polyvaccine Based on Microbial IgA1 Protease for Prophylaxis of Bacterial Meningitis. Epidemiology and Vaccinal Prevention. 15(6). 88–94. 1 indexed citations

Zinchenko, Anatoly, et al.. (2016). Serological Analysis of Immunogenic Properties of Recombinant Meningococcus IgA1 Protease-Based Proteins. Bulletin of Experimental Biology and Medicine. 161(3). 391–394. 10 indexed citations

Nekrasov, A. N., et al.. (2015). Truncated variants of Serratia proteamaculans oligopeptidase B having different activities. Biochemistry (Moscow). 80(10). 1331–1343. 8 indexed citations

Серова, О. В., et al.. (2015). A new methodological approach to estimation of IgA1 and IgA2 content in human serum using recombinant IgA1 protease from Neisseria meningitidis. Biotechnology Letters. 37(11). 2289–2293. 1 indexed citations

Khairullin, Rafil, Ilya V. Demidyuk, Sergey V. Kostrov, et al.. (2013). Cloning, sequencing, expression, and characterization of thermostability of oligopeptidase B from Serratia proteamaculans, a novel psychrophilic protease. Protein Expression and Purification. 93. 63–76. 27 indexed citations

Khairullin, Rafil, et al.. (2012). Oligopeptidase B from Serratia proteamaculans. III. Inhibition analysis. Specific interactions with metalloproteinase inhibitors. Biochemistry (Moscow). 77(3). 300–306. 5 indexed citations

10.

Khairullin, Rafil, et al.. (2011). Oligopeptidase B from Serratia proteamaculans. II. Enzymatic characteristics: Substrate analysis, influence of calcium ions, pH and temperature dependences. Biochemistry (Moscow). 76(4). 480–490. 7 indexed citations

11.

Горбачева, Л. Р., et al.. (2010). Effect of enteropeptidase on survival of cultured hippocampal neurons under conditions of glutamate toxicity. Biochemistry (Moscow). 75(9). 1153–1159. 2 indexed citations

12.

Khairullin, Rafil, et al.. (2009). Oligopeptidase B from Serratia proteamaculans. I. Determination of primary structure, isolation, and purification of wild-type and recombinant enzyme variants. Biochemistry (Moscow). 74(10). 1164–1172. 8 indexed citations

13.

Teich, Niels, et al.. (2007). The Ways of Realization of High Specificity and Efficiency of Enteropeptidase. Protein and Peptide Letters. 14(3). 227–232. 11 indexed citations

14.

Khairullin, Rafil, et al.. (2006). Psychrophilic trypsin-type protease from Serratia proteamaculans. Biochemistry (Moscow). 71(5). 563–570. 13 indexed citations

15.

Румш, Л. Д., et al.. (2004). New Aspartic Proteinase of Ulysses Retrotransposon from Drosophila virilis. Biochemistry (Moscow). 69(6). 697–701. 1 indexed citations

16.

Марквичева, Елена, et al.. (2004). Application of bioencapsulated proteinases and peptides for wound gealing. Open Repository and Bibliography (University of Liège). 58. 2 indexed citations

17.

Марквичева, Елена, С. В. Купцова, Vladimír Babák, et al.. (2000). PROTEASES ENTRAPPED IN POLYMER COMPOSITE HYDROGELS: PREPARATION METHODS AND APPLICATIONS. 7 indexed citations

18.

Koroleva, Ekaterina P., et al.. (1998). Mutations in the proteolytic domain of Escherichia coli protease Lon impair the ATPase activity of the enzyme. FEBS Letters. 422(2). 218–220. 37 indexed citations

19.

Amerik, Alexander Y., et al.. (1996). HIV-I protease. Applied Biochemistry and Biotechnology. 61(1-2). 97–107. 13 indexed citations

20.

Марквичева, Елена, et al.. (1994). Immobilization of proteases in composite hydrogel based on poly(N-vinyl caprolactam). Biotechnology Techniques. 8(3). 143–148. 11 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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