A.G. Pavlovsky

2.8k total citations
37 papers, 1.5k citations indexed

About

A.G. Pavlovsky is a scholar working on Molecular Biology, Materials Chemistry and Oncology. According to data from OpenAlex, A.G. Pavlovsky has authored 37 papers receiving a total of 1.5k indexed citations (citations by other indexed papers that have themselves been cited), including 21 papers in Molecular Biology, 15 papers in Materials Chemistry and 7 papers in Oncology. Recurrent topics in A.G. Pavlovsky's work include Enzyme Structure and Function (15 papers), Peptidase Inhibition and Analysis (6 papers) and Protease and Inhibitor Mechanisms (6 papers). A.G. Pavlovsky is often cited by papers focused on Enzyme Structure and Function (15 papers), Peptidase Inhibition and Analysis (6 papers) and Protease and Inhibitor Mechanisms (6 papers). A.G. Pavlovsky collaborates with scholars based in United States, Russia and United Kingdom. A.G. Pavlovsky's co-authors include Ronald E. Viola, Alla Gustchina, Daniel F. Ortwine, Xuying Liu, Ruslan Sanishvili, Christine Humblet, Richard D. Dyer, Linda L. Johnson, K. M. Polyakov and Adam R. Johnson and has published in prestigious journals such as Nature, Journal of Biological Chemistry and Nature Communications.

In The Last Decade

A.G. Pavlovsky

37 papers receiving 1.4k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
A.G. Pavlovsky United States 23 827 359 340 268 232 37 1.5k
Wynne Aherne United Kingdom 27 1.5k 1.9× 509 1.4× 270 0.8× 90 0.3× 161 0.7× 58 2.3k
S. Terzyan United States 25 1.1k 1.3× 256 0.7× 147 0.4× 226 0.8× 131 0.6× 53 2.2k
K. Ulrich Wendt Germany 18 662 0.8× 246 0.7× 271 0.8× 100 0.4× 167 0.7× 29 1.0k
David J. Hosfield United States 28 2.2k 2.7× 359 1.0× 241 0.7× 235 0.9× 173 0.7× 37 3.0k
Michele McTigue United States 18 1.7k 2.1× 1.0k 2.8× 264 0.8× 143 0.5× 388 1.7× 25 2.9k
Robert E. Babine United States 14 709 0.9× 299 0.8× 217 0.6× 70 0.3× 473 2.0× 26 1.3k
Richard Cummings United States 26 1.2k 1.5× 417 1.2× 147 0.4× 141 0.5× 353 1.5× 52 2.4k
Yan Ling United States 23 1.0k 1.3× 230 0.6× 144 0.4× 133 0.5× 251 1.1× 60 1.8k
Neil Moss United States 19 1.1k 1.3× 362 1.0× 137 0.4× 98 0.4× 623 2.7× 34 1.7k
Swee Y. Sharp United Kingdom 25 2.0k 2.5× 750 2.1× 198 0.6× 269 1.0× 417 1.8× 45 2.8k

Countries citing papers authored by A.G. Pavlovsky

Since Specialization
Citations

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

Fields of papers citing papers by A.G. Pavlovsky

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by A.G. Pavlovsky. 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 A.G. Pavlovsky. The network helps show where A.G. Pavlovsky may publish in the future.

Co-authorship network of co-authors of A.G. Pavlovsky

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

All Works

20 of 20 papers shown
1.
Wang, Yunmei, Huiyun Gao, Can Shi, et al.. (2017). Leukocyte integrin Mac-1 regulates thrombosis via interaction with platelet GPIbα. Nature Communications. 8(1). 15559–15559. 127 indexed citations
2.
Pavlovsky, A.G., et al.. (2014). Structure of homoserineO-acetyltransferase fromStaphylococcus aureus: the first Gram-positive ortholog structure. Acta Crystallographica Section F Structural Biology Communications. 70(10). 1340–1345. 10 indexed citations
3.
Pavlovsky, A.G., et al.. (2014). A cautionary tale of structure-guided inhibitor development against an essential enzyme in the aspartate-biosynthetic pathway. Acta Crystallographica Section D Biological Crystallography. 70(12). 3244–3252. 9 indexed citations
4.
Pavlovsky, A.G., et al.. (2014). Structure of an unusualS-adenosylmethionine synthetase fromCampylobacter jejuni. Acta Crystallographica Section D Biological Crystallography. 70(2). 442–450. 5 indexed citations
5.
Wang, Lin, et al.. (2012). Molecular docking and enzymatic evaluation to identify selective inhibitors of aspartate semialdehyde dehydrogenase. Bioorganic & Medicinal Chemistry. 20(9). 2950–2956. 14 indexed citations
6.
Viola, Ronald E., et al.. (2010). The Catalytic Machinery of a Key Enzyme in Amino Acid Biosynthesis. PubMed. 2011. 1–11. 28 indexed citations
7.
Gao, Geng, Xuying Liu, A.G. Pavlovsky, & Ronald E. Viola. (2010). Identification of Selective Enzyme Inhibitors by Fragment Library Screening. SLAS DISCOVERY. 15(9). 1042–1050. 22 indexed citations
8.
Warmus, Joseph S., Cathlin Flamme, Stephen D. Barrett, et al.. (2008). 2-Alkylamino- and alkoxy-substituted 2-amino-1,3,4-oxadiazoles—O-Alkyl benzohydroxamate esters replacements retain the desired inhibition and selectivity against MEK (MAP ERK kinase). Bioorganic & Medicinal Chemistry Letters. 18(23). 6171–6174. 60 indexed citations
9.
Pavlovsky, A.G., et al.. (2008). The Structural Basis for Allosteric Inhibition of a Threonine-sensitive Aspartokinase. Journal of Biological Chemistry. 283(23). 16216–16225. 25 indexed citations
10.
Pfefferkorn, Jeffrey A., Chulho Choi, Yuntao Song, et al.. (2007). Design and synthesis of novel, conformationally restricted HMG-CoA reductase inhibitors. Bioorganic & Medicinal Chemistry Letters. 17(16). 4531–4537. 30 indexed citations
11.
Johnson, Adam R., A.G. Pavlovsky, Daniel F. Ortwine, et al.. (2007). Discovery and Characterization of a Novel Inhibitor of Matrix Metalloprotease-13 That Reduces Cartilage Damage in Vivo without Joint Fibroplasia Side Effects. Journal of Biological Chemistry. 282(38). 27781–27791. 176 indexed citations
12.
Faehnle, C.R., Xuying Liu, A.G. Pavlovsky, & Ronald E. Viola. (2006). The initial step in the archaeal aspartate biosynthetic pathway catalyzed by a monofunctional aspartokinase. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 62(10). 962–966. 25 indexed citations
13.
Polyakov, K. M., Andrey A. Lebedev, Andrei L. Okorokov, et al.. (2002). The structure of substrate-free microbial ribonuclease binase and of its complexes with 3′GMP and sulfate ions. Acta Crystallographica Section D Biological Crystallography. 58(5). 744–750. 20 indexed citations
14.
Johnson, Linda L., A.G. Pavlovsky, Adam R. Johnson, et al.. (2000). A Rationalization of the Acidic pH Dependence for Stromelysin-1 (Matrix Metalloproteinase-3) Catalysis and Inhibition. Journal of Biological Chemistry. 275(15). 11026–11033. 64 indexed citations
15.
Johnson, Linda L., et al.. (1999). Effect of Species Differences on Stromelysin-1 (MMP-3) Inhibitor Potency. Journal of Biological Chemistry. 274(35). 24881–24887. 12 indexed citations
16.
Pavlovsky, A.G., Mark Williams, Daniel F. Ortwine, et al.. (1999). X‐ray structure of human stromelysin catalytic domain complexed with nonpeptide inhibitors: Implications for inhibitor selectivity. Protein Science. 8(7). 1455–1462. 65 indexed citations
17.
Tummino, Peter J., J. V. N. Vara Prasad, Donna Ferguson, et al.. (1996). Discovery and optimization of nonpeptide HIV-1 protease inhibitors. Bioorganic & Medicinal Chemistry. 4(9). 1401–1410. 22 indexed citations
18.
19.
Sanishvili, Ruslan, et al.. (1990). Comparison of active sites of some microbial ribonucleases: structural basis for guanylic specificity. Trends in Biochemical Sciences. 15(4). 158–162. 64 indexed citations
20.
Protasevich, Irina I., et al.. (1987). Distribution of Charges inBacillus intermedins 7PRibonuclease Determines the Number of Cooperatively Melting Regions of the Globule. Journal of Biomolecular Structure and Dynamics. 4(5). 885–893. 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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