А.М. Рубцов

410 total citations
31 papers, 359 citations indexed

About

А.М. Рубцов is a scholar working on Molecular Biology, Physiology and Pharmacology. According to data from OpenAlex, А.М. Рубцов has authored 31 papers receiving a total of 359 indexed citations (citations by other indexed papers that have themselves been cited), including 18 papers in Molecular Biology, 7 papers in Physiology and 6 papers in Pharmacology. Recurrent topics in А.М. Рубцов's work include Ion Transport and Channel Regulation (10 papers), Ion channel regulation and function (7 papers) and Healthcare and Venom Research (6 papers). А.М. Рубцов is often cited by papers focused on Ion Transport and Channel Regulation (10 papers), Ion channel regulation and function (7 papers) and Healthcare and Venom Research (6 papers). А.М. Рубцов collaborates with scholars based in Russia, Tajikistan and Canada. А.М. Рубцов's co-authors include O. D. Lopina, Kenneth B. Storey, Olga A. Akimova, Sergei N. Orlov, Erika Geimonen, Pavel Hamet, А. А. Болдырев, Johanne Tremblay, Michael Gekle and Rustam Ziganshin and has published in prestigious journals such as Biochemistry, Biochemical and Biophysical Research Communications and FEBS Letters.

In The Last Decade

А.М. Рубцов

29 papers receiving 348 citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
А.М. Рубцов Russia	10	180	134	55	43	33	31	359
Norma Oviedo Mexico	12	217 1.2×	58 0.4×	11 0.2×	17 0.4×	51 1.5×	35	404
Xiaoping Ning United States	9	261 1.4×	70 0.5×	33 0.6×	63 1.5×	92 2.8×	10	958
Satoko Nakajima Japan	12	132 0.7×	41 0.3×	17 0.3×	29 0.7×	25 0.8×	31	373
Nanni Din Denmark	15	472 2.6×	257 1.9×	14 0.3×	119 2.8×	74 2.2×	19	703
Jean‐Christophe Peter France	12	161 0.9×	56 0.4×	23 0.4×	16 0.4×	16 0.5×	17	359
J. P. Petrali United States	10	107 0.6×	28 0.2×	17 0.3×	26 0.6×	22 0.7×	26	372
Nadejda L. Korneeva United States	12	379 2.1×	33 0.2×	11 0.2×	22 0.5×	30 0.9×	23	515
Carmen Bordallo Spain	12	264 1.5×	48 0.4×	14 0.3×	38 0.9×	23 0.7×	21	351
М. Н. Перцева Russia	14	276 1.5×	82 0.6×	10 0.2×	30 0.7×	48 1.5×	60	543
Naoko Nakamura Japan	9	186 1.0×	41 0.3×	11 0.2×	19 0.4×	13 0.4×	17	274

Countries citing papers authored by А.М. Рубцов

Since Specialization

Citations

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

Fields of papers citing papers by А.М. Рубцов

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by А.М. Рубцов. 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 А.М. Рубцов. The network helps show where А.М. Рубцов may publish in the future.

Co-authorship network of co-authors of А.М. Рубцов

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

All Works

Sort: Min cites: Since: Top N: Style:

20 of 20 papers shown

Storey, Kenneth B., et al.. (2014). Regulation of glucokinase activity in liver of hibernating ground squirrel Spermophilus undulatus. Biochemistry (Moscow). 79(7). 727–732. 2 indexed citations

Akimova, Olga A., O. D. Lopina, А.М. Рубцов, Pavel Hamet, & Sergei N. Orlov. (2010). Investigation of mechanism of p38 MAPK activation in renal epithelial cell from distal tubules triggered by cardiotonic steroids. Biochemistry (Moscow). 75(8). 971–978. 6 indexed citations

Lopina, O. D., et al.. (2010). Seasonal Changes in Microsomal Fraction Enriched with Na,K-ATPase from Kidneys of the Ground Squirrel Spermophilus undulatus. Biochemistry (Moscow). 75(11). 1408–1416. 1 indexed citations

Petrushanko, Irina Yu., et al.. (2010). Neutral endopeptidase neprilysin is copurified with Na,K-ATPase from rabbit outer medulla and hydrolyzes its α-subunit. Biochemistry (Moscow). 75(10). 1281–1284. 1 indexed citations

Akimova, Olga A., O. D. Lopina, А.М. Рубцов, et al.. (2009). Death of ouabain-treated renal epithelial cells: evidence for p38 MAPK-mediated Na i + /K i + -independent signaling. APOPTOSIS. 14(11). 1266–1273. 23 indexed citations

Рубцов, А.М., et al.. (2008). Effect of colchicine on sensitivity of duck salt gland Na,K-ATPase to Na+. Biochemistry (Moscow). 73(9). 990–994. 3 indexed citations

Dolgova, Natalia V., et al.. (2007). A protein whose binding to Na,K-ATPase is regulated by ouabain. Biochemistry (Moscow). 72(8). 863–871. 2 indexed citations

Dolgova, Natalia V., et al.. (2004). Melittin induces both time-dependent aggregation and inhibition of Na,K-ATPase from duck salt glands however these two processes appear to occur independently. Biochimica et Biophysica Acta (BBA) - Biomembranes. 1661(2). 188–195. 5 indexed citations

Akimova, Olga A., et al.. (2003). Revealing of Proteins Interacting with Na,K-ATPase. Biochemistry (Moscow). 68(9). 1040–1047. 4 indexed citations

10.

Рубцов, А.М.. (2001). Molecular Mechanisms of Regulation of the Activity of Sarcoplasmic Reticulum Ca-Release Channels (Ryanodine Receptors), Muscle Fatigue, and Severin's Phenomenon. Biochemistry (Moscow). 66(10). 1132–1143. 30 indexed citations

11.

Malysheva, Anna, Kenneth B. Storey, Rustam Ziganshin, O. D. Lopina, & А.М. Рубцов. (2001). Characteristics of Sarcoplasmic Reticulum Membrane Preparations Isolated from Skeletal Muscles of Active and Hibernating Ground Squirrel Spermophilus undulatus. Biochemistry (Moscow). 66(8). 918–925. 16 indexed citations

12.

Рубцов, А.М., et al.. (2001). Phosphorylation of the α-Subunit of Na,K-ATPase from Duck Salt Glands by cAMP-Dependent Protein Kinase Inhibits the Enzyme Activity. Biochemistry (Moscow). 66(8). 865–874. 5 indexed citations

13.

Рубцов, А.М. & O. D. Lopina. (2000). Ankyrins. FEBS Letters. 482(1-2). 1–5. 96 indexed citations

14.

Рубцов, А.М., et al.. (1997). Histidine-containing dipeptides as endogenous regulators of the activity of sarcoplasmic reticulum Ca-release channels. Biochimica et Biophysica Acta (BBA) - Biomembranes. 1324(1). 142–150. 63 indexed citations

15.

Lopina, O. D., et al.. (1997). Melittin-Induced Inhibition and Aggregation of Ca-ATPase in Skeletal Muscle Sarcoplasmic Reticulum: A Comparative Study. Biochemistry. 36(44). 13455–13460. 12 indexed citations

16.

Lopina, O. D., et al.. (1995). Phosphorylation of alpha-subunit of Na,K-ATPase from duck salt gland and dog kidney by protein kinase A and C. Biophysical Journal. 68. 308–308. 2 indexed citations

17.

Geimonen, Erika, et al.. (1994). Thermal Uncoupling of the Ca²⁺‐transporting ATPase in Sarcoplasmic Reticulum. European Journal of Biochemistry. 225(1). 347–354. 12 indexed citations

18.

Рубцов, А.М., et al.. (1988). Caffeine interaction with the Ca-release channels of heavy sarcoplasmic reticulum. Evidence that 170 kD Ca-binding protein is a caffeine receptor of the Ca-channels. Biochemical and Biophysical Research Communications. 154(1). 462–468. 20 indexed citations

19.

Рубцов, А.М., Peter J. Quinn, & А. А. Болдырев. (1988). Pathways of calcium release from heavy sarcoplasmic reticulum vesicles isolated from rabbit skeletal muscle. FEBS Letters. 238(2). 240–244. 6 indexed citations

20.

Рубцов, А.М., O. D. Lopina, & A. A. Boldyrev. (1982). EFFECTS OF DIVALENT-CATIONS AND ATP ON THE KINETIC-PROPERTIES OF THE SULFHYDRYL-GROUPS OF SARCOPLASMIC-RETICULUM MEMBRANES AND PURIFIED CA-ATPASE. General Physiology and Biophysics. 1(3). 161–173. 2 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.

Explore authors with similar magnitude of impact