Alexey Bulychev

507 total citations
15 papers, 409 citations indexed

About

Alexey Bulychev is a scholar working on Molecular Medicine, Molecular Biology and Pharmacology. According to data from OpenAlex, Alexey Bulychev has authored 15 papers receiving a total of 409 indexed citations (citations by other indexed papers that have themselves been cited), including 10 papers in Molecular Medicine, 7 papers in Molecular Biology and 5 papers in Pharmacology. Recurrent topics in Alexey Bulychev's work include Antibiotic Resistance in Bacteria (10 papers), Antibiotics Pharmacokinetics and Efficacy (3 papers) and Enzyme Structure and Function (3 papers). Alexey Bulychev is often cited by papers focused on Antibiotic Resistance in Bacteria (10 papers), Antibiotics Pharmacokinetics and Efficacy (3 papers) and Enzyme Structure and Function (3 papers). Alexey Bulychev collaborates with scholars based in United States and France. Alexey Bulychev's co-authors include Shahriar Mobashery, Irina Massova, Jui‐Yoa Chang, Jean‐Pierre Samama, Li Li, Kazuyuki Miyashita, Marvin J. Miller, Laurent Maveyraud, Dasantila Golemi‐Kotra and Sergei B. Vakulenko and has published in prestigious journals such as Journal of the American Chemical Society, Journal of Biological Chemistry and Biochemistry.

In The Last Decade

Alexey Bulychev

15 papers receiving 395 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Alexey Bulychev United States 13 241 185 135 64 58 15 409
Monica A. Totir United States 10 254 1.1× 170 0.9× 162 1.2× 38 0.6× 55 0.9× 11 383
Marianne P. Carey United States 10 224 0.9× 183 1.0× 146 1.1× 35 0.5× 38 0.7× 11 420
Liza de Castro Canada 8 227 0.9× 252 1.4× 99 0.7× 37 0.6× 61 1.1× 8 448
Heinrich Delbrück Germany 12 172 0.7× 280 1.5× 57 0.4× 69 1.1× 90 1.6× 14 508
Celia C. H. Chen United States 10 162 0.7× 240 1.3× 83 0.6× 31 0.5× 140 2.4× 13 430
Jean Marie Frère Belgium 7 222 0.9× 187 1.0× 89 0.7× 28 0.4× 17 0.3× 8 372
Dasantila Golemi United States 9 415 1.7× 237 1.3× 215 1.6× 33 0.5× 64 1.1× 10 617
Julia A. Cricco Argentina 13 215 0.9× 333 1.8× 57 0.4× 48 0.8× 38 0.7× 25 659
Pablo E. Tomatis Argentina 11 274 1.1× 229 1.2× 106 0.8× 19 0.3× 53 0.9× 15 467
V Knott-Hunziker United Kingdom 10 473 2.0× 248 1.3× 206 1.5× 77 1.2× 47 0.8× 11 585

Countries citing papers authored by Alexey Bulychev

Since Specialization
Citations

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

Fields of papers citing papers by Alexey Bulychev

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Alexey Bulychev. 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 Alexey Bulychev. The network helps show where Alexey Bulychev may publish in the future.

Co-authorship network of co-authors of Alexey Bulychev

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

All Works

15 of 15 papers shown
1.
Golemi‐Kotra, Dasantila, Samy O. Meroueh, Choon Kim, et al.. (2004). The Importance of a Critical Protonation State and the Fate of the Catalytic Steps in Class A β-Lactamases and Penicillin-binding Proteins. Journal of Biological Chemistry. 279(33). 34665–34673. 61 indexed citations
2.
Chang, Jui‐Yoa, Alexey Bulychev, & Li Li. (2000). A stabilized molten globule protein. FEBS Letters. 487(2). 298–300. 15 indexed citations
3.
Chang, Jui‐Yoa, Li Li, & Alexey Bulychev. (2000). The Underlying Mechanism for the Diversity of Disulfide Folding Pathways. Journal of Biological Chemistry. 275(12). 8287–8289. 46 indexed citations
4.
Bulychev, Alexey, E O’Brien, Peter J. Crocker, et al.. (2000). N-Sulfonyloxy-β-lactam Inhibitors for β-Lactamases. Tetrahedron. 56(31). 5719–5728. 16 indexed citations
5.
Mourey, Lionel, Lakshmi P. Kotra, Alexey Bulychev, et al.. (1999). Inhibition of the Broad Spectrum Nonmetallocarbapenamase of Class A (NMC-A) β-Lactamase from Enterobacter cloacae by Monocyclic β-Lactams. Journal of Biological Chemistry. 274(36). 25260–25265. 14 indexed citations
6.
Bulychev, Alexey & Jui‐Yoa Chang. (1999). Unfolding of Hirudin Characterized by the Composition of Denatured Scrambled Isomers. Journal of Protein Chemistry. 18(7). 771–778. 12 indexed citations
7.
Massova, Irina, Alexey Bulychev, Laurent Maveyraud, et al.. (1999). Elucidation of Mechanism of Inhibition and X-ray Structure of the TEM-1 β-Lactamase from Escherichia coli Inhibited by a N-Sulfonyloxy-β-lactam. Journal of the American Chemical Society. 121(23). 5353–5359. 19 indexed citations
8.
Golemi, Dasantila, Stéphanie Cabantous, Alexey Bulychev, et al.. (1999). X-ray Structure of the Asn276Asp Variant of the Escherichia coli TEM-1 β-Lactamase:  Direct Observation of Electrostatic Modulation in Resistance to Inactivation by Clavulanic Acid,. Biochemistry. 38(30). 9570–9576. 40 indexed citations
9.
Bulychev, Alexey & Shahriar Mobashery. (1999). Class C β-Lactamases Operate at the Diffusion Limit for Turnover of Their Preferred Cephalosporin Substrates. Antimicrobial Agents and Chemotherapy. 43(7). 1743–1746. 32 indexed citations
10.
Massova, Irina, et al.. (1998). Templates for design of inhibitors for serine proteases: Application of the program dock to the discovery of novel inhibitors for thrombin. Bioorganic & Medicinal Chemistry Letters. 8(18). 2463–2466. 5 indexed citations
11.
Mourey, Lionel, et al.. (1998). Inhibition of the NMC-A β-Lactamase by a Penicillanic Acid Derivative and the Structural Bases for the Increase in Substrate Profile of This Antibiotic Resistance Enzyme. Journal of the American Chemical Society. 120(36). 9382–9383. 40 indexed citations
12.
Li, Zhihong, Alexey Bulychev, Lakshmi P. Kotra, Irina Massova, & Shahriar Mobashery. (1998). Hydrogen Bonding and Attenuation of the Rate of Enzymic Catalysis. Journal of the American Chemical Society. 120(50). 13003–13007. 6 indexed citations
13.
Bulychev, Alexey, Irina Massova, Kazuyuki Miyashita, & Shahriar Mobashery. (1997). Nuances of Mechanisms and Their Implications for Evolution of the Versatile β-Lactamase Activity:  From Biosynthetic Enzymes to Drug Resistance Factors. Journal of the American Chemical Society. 119(33). 7619–7625. 55 indexed citations
14.
Bulychev, Alexey, E O’Brien, Irina Massova, et al.. (1995). Potent mechanism-based inhibition of the TEM-1 .beta.-lactamase by novel N-sulfonyloxy .beta.-lactams. Journal of the American Chemical Society. 117(22). 5938–5943. 23 indexed citations
15.
Bulychev, Alexey, Irina Massova, Stephen A. Lerner, & Shahriar Mobashery. (1995). Penem BRL 42715: An Effective Inactivator for .beta.-Lactamases. Journal of the American Chemical Society. 117(17). 4797–4801. 25 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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