Tamara Azarashvili
About
Tamara Azarashvili is a scholar working on Molecular Biology, Cellular and Molecular Neuroscience and Physiology.
According to data from OpenAlex, Tamara Azarashvili has authored 34 papers receiving a total of 727 indexed citations (citations by other indexed papers that have themselves been cited), including 31 papers in Molecular Biology, 14 papers in Cellular and Molecular Neuroscience and 7 papers in Physiology. Recurrent topics in Tamara Azarashvili's work include Mitochondrial Function and Pathology (24 papers), ATP Synthase and ATPases Research (13 papers) and Neuroscience and Neuropharmacology Research (13 papers). Tamara Azarashvili is often cited by papers focused on Mitochondrial Function and Pathology (24 papers), ATP Synthase and ATPases Research (13 papers) and Neuroscience and Neuropharmacology Research (13 papers). Tamara Azarashvili collaborates with scholars based in Russia, Germany and United States. Tamara Azarashvili's co-authors include Olga Krestinina, Georg Reiser, Dmitry Grachev, Yulia Baburina, Rolf Stricker, Irina Odinokova, Yuri V. Evtodienko, Jaana Tyynelä, Vassilios Papadopoulos and Yu. V. Evtodienko and has published in prestigious journals such as FEBS Letters, International Journal of Molecular Sciences and Journal of Neurochemistry.
In The Last Decade
Tamara Azarashvili
33 papers receiving 723 citations
Peers — A (Enhanced Table)
Peers by citation overlap · career bar shows stage (early→late) cites · hero ref
| Name | h | Career | Trend | Papers | Cites | |||||
|---|---|---|---|---|---|---|---|---|---|---|
| Tamara Azarashvili Russia | 14 | 580 | 134 | 121 | 88 | 61 | 34 | 727 | ||
| Shin-Young Ryu United States | 15 | 594 1.0× | 150 1.1× | 147 1.2× | 102 1.2× | 58 1.0× | 16 | 875 | ||
| Olga Krestinina Russia | 18 | 705 1.2× | 128 1.0× | 152 1.3× | 123 1.4× | 66 1.1× | 65 | 953 | ||
| Yulia Baburina Russia | 15 | 464 0.8× | 60 0.4× | 116 1.0× | 85 1.0× | 31 0.5× | 52 | 658 | ||
| Linas Buntinas United States | 6 | 577 1.0× | 203 1.5× | 108 0.9× | 99 1.1× | 56 0.9× | 9 | 738 | ||
| Dmitry Grachev Russia | 11 | 320 0.6× | 80 0.6× | 73 0.6× | 50 0.6× | 26 0.4× | 12 | 401 | ||
| Claudia Savoia Italy | 12 | 560 1.0× | 119 0.9× | 132 1.1× | 31 0.4× | 80 1.3× | 14 | 794 | ||
| Ying Dun United States | 16 | 560 1.0× | 230 1.7× | 48 0.4× | 76 0.9× | 75 1.2× | 27 | 900 | ||
| Susan E. O’Donnell United States | 5 | 668 1.2× | 95 0.7× | 118 1.0× | 97 1.1× | 30 0.5× | 5 | 950 | ||
| Agnès Müller France | 14 | 371 0.6× | 186 1.4× | 187 1.5× | 62 0.7× | 52 0.9× | 23 | 735 | ||
| Annapurna Chalasani United Kingdom | 11 | 585 1.0× | 70 0.5× | 86 0.7× | 17 0.2× | 99 1.6× | 13 | 778 |
Countries citing papers authored by Tamara Azarashvili
Since
Specialization
Citations
This map shows the geographic impact of Tamara Azarashvili'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 Tamara Azarashvili with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Tamara Azarashvili more than expected).
Fields of papers citing papers by Tamara Azarashvili
Since
Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences
This network shows the impact of papers produced by Tamara Azarashvili. 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 Tamara Azarashvili. The network helps show where Tamara Azarashvili may publish in the future.
Co-authorship network of co-authors of Tamara Azarashvili
This figure shows the co-authorship network connecting the top 25 collaborators of Tamara Azarashvili. A scholar is included among the top collaborators of Tamara Azarashvili 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 Tamara Azarashvili. Tamara Azarashvili is excluded from the visualization to improve readability, since they are connected to all nodes in the network.
All Works
1.
Baburina, Yulia, et al.. (2018). Possible Involvement of 2′,3′-Cyclic Nucleotide-3′-Phosphodiesterase in the Protein Phosphorylation-Mediated Regulation of the Permeability Transition Pore. International Journal of Molecular Sciences. 19(11). 3499–3499.
2.
Krestinina, Olga, Irina Odinokova, Yulia Baburina, & Tamara Azarashvili. (2018). Detection of Protein Kinase A and C Target Proteins in Rat Brain Mitochondria. Biochemistry (Moscow) Supplement Series A Membrane and Cell Biology. 12(1). 70–73.
3.
Baburina, Yulia, Irina Odinokova, Tamara Azarashvili, et al.. (2016). 2′,3′-Cyclic nucleotide 3′-phosphodiesterase as a messenger of protection of the mitochondrial function during melatonin treatment in aging. Biochimica et Biophysica Acta (BBA) - Biomembranes. 1859(1). 94–103.
4.
Krestinina, Olga, Yulia Baburina, & Tamara Azarashvili. (2015). Effect of melatonin on stress-induced opening of non-selective pore in mitochondria from brain of young and old rats. Biochemistry (Moscow) Supplement Series A Membrane and Cell Biology. 9(2). 116–123.
5.
Baburina, Yulia, Tamara Azarashvili, Dmitry Grachev, et al.. (2015). Mitochondrial 2′, 3′-cyclic nucleotide 3′-phosphodiesterase (CNP) interacts with mPTP modulators and functional complexes (I–V) coupled with release of apoptotic factors. Neurochemistry International. 90. 46–55.
6.
Azarashvili, Tamara, Olga Krestinina, Yulia Baburina, et al.. (2015). Combined effect of G3139 and TSPO ligands on Ca2+-induced permeability transition in rat brain mitochondria. Archives of Biochemistry and Biophysics. 587. 70–77.
7.
Krestinina, Olga, Tamara Azarashvili, Yulia Baburina, et al.. (2014). In aging, the vulnerability of rat brain mitochondria is enhanced due to reduced level of 2′,3′-cyclic nucleotide-3′-phosphodiesterase (CNP) and subsequently increased permeability transition in brain mitochondria in old animals. Neurochemistry International. 80. 41–50.
8.
Baburina, Yulia, et al.. (2014). Interaction of myelin basic protein and 2′,3′-cyclic nucleotide phosphodiesterase with mitochondria. Biochemistry (Moscow). 79(6). 555–565.
9.
Azarashvili, Tamara, Olga Krestinina, Dmitry Grachev, et al.. (2014). Identification of phosphorylated form of 2′, 3′-cyclic nucleotide 3′-phosphodiesterase (CNPase) as 46 kDa phosphoprotein in brain non-synaptic mitochondria overloaded by calcium. Journal of Bioenergetics and Biomembranes. 46(2). 135–145.
10.
Azarashvili, Tamara, Yulia Baburina, Dmitry Grachev, et al.. (2014). Carbenoxolone induces permeability transition pore opening in rat mitochondria via the translocator protein TSPO and connexin43. Archives of Biochemistry and Biophysics. 558. 87–94.
11.
Krestinina, Olga, Irina Odinokova, Yulia Baburina, & Tamara Azarashvili. (2013). Age-related effect of melatonin on permeability transition pore opening in rat brain mitochondria. Biochemistry (Moscow) Supplement Series A Membrane and Cell Biology. 7(4). 286–293.
12.
Azarashvili, Tamara, Irina Odinokova, Olga Krestinina, et al.. (2011). Role of phosphorylation of porin (VDAC) in regulation of mitochondrial outer membrane under normal conditions and alcohol intoxication. Biochemistry (Moscow) Supplement Series A Membrane and Cell Biology. 5(1). 11–20.
13.
Azarashvili, Tamara, Rolf Stricker, & Georg Reiser. (2010). The mitochondria permeability transition pore complex in the brain with interacting proteins – promising targets for protection in neurodegenerative diseases. Biological Chemistry. 391(6). 619–29.
14.
Krestinina, Olga, Dmitry Grachev, Irina Odinokova, et al.. (2009). Effect of peripheral benzodiazepine receptor (PBR/TSPO) ligands on opening of Ca2+-induced pore and phosphorylation of 3.5-kDa polypeptide in rat brain mitochondria. Biochemistry (Moscow). 74(4). 421–429.
15.
Azarashvili, Tamara, Olga Krestinina, Dmitry Grachev, et al.. (2009). Ca2+-dependent permeability transition regulation in rat brain mitochondria by 2′,3′-cyclic nucleotides and 2′,3′-cyclic nucleotide 3′-phosphodiesterase. American Journal of Physiology-Cell Physiology. 296(6). C1428–C1439.
16.
Grachev, Dmitry, Tamara Azarashvili, Yulia Baburina, et al.. (2009). The brain‐specific protein, p42IP4(ADAP 1) is localized in mitochondria and involved in regulation of mitochondrial Ca2+. Journal of Neurochemistry. 109(6). 1701–1713.
17.
Azarashvili, Tamara, et al.. (2006). The peripheral-type benzodiazepine receptor is involved in control of Ca2+-induced permeability transition pore opening in rat brain mitochondria. Cell Calcium. 42(1). 27–39.
18.
Azarashvili, Tamara, Olga Krestinina, Irina Odinokova, Yu. V. Evtodienko, & Georg Reiser. (2003). Physiological Ca2+ level and Ca2+-induced Permeability Transition Pore control protein phosphorylation in rat brain mitochondria. Cell Calcium. 34(3). 253–259.
19.
Azarashvili, Tamara, et al.. (1999). Phosphorylation of a low-molecular-weight polypeptide in rat liver mitochondria and dependence of its phosphorylation on mitochondrial functional state.. PubMed. 64(5). 556–60.
20.
Evtodienko, Yuri V., Tamara Azarashvili, & Alexei P. Kudin. (1998). Calcium binding to polypeptides of rat liver and Zajdela hepatoma mitochondrial inner membranes. FEBS Letters. 423(1). 45–48.
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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