Gary I. Dmitrienko

1.9k total citations
74 papers, 1.5k citations indexed

About

Gary I. Dmitrienko is a scholar working on Molecular Biology, Organic Chemistry and Molecular Medicine. According to data from OpenAlex, Gary I. Dmitrienko has authored 74 papers receiving a total of 1.5k indexed citations (citations by other indexed papers that have themselves been cited), including 36 papers in Molecular Biology, 32 papers in Organic Chemistry and 19 papers in Molecular Medicine. Recurrent topics in Gary I. Dmitrienko's work include Antibiotic Resistance in Bacteria (19 papers), Bioactive Compounds and Antitumor Agents (8 papers) and Enzyme Structure and Function (8 papers). Gary I. Dmitrienko is often cited by papers focused on Antibiotic Resistance in Bacteria (19 papers), Bioactive Compounds and Antitumor Agents (8 papers) and Enzyme Structure and Function (8 papers). Gary I. Dmitrienko collaborates with scholars based in Canada, United States and United Kingdom. Gary I. Dmitrienko's co-authors include Radoslaw S. Laufer, Thammaiah Viswanatha, Stefan Siemann, Anthony J. Clarke, Michael A. Parniak, Susan F. Vice, Nicholas J. Taylor, Gamini Weeratunga, Laura Marrone and Brian B. Hasinoff and has published in prestigious journals such as Journal of the American Chemical Society, Physical Review Letters and Journal of Molecular Biology.

In The Last Decade

Gary I. Dmitrienko

73 papers receiving 1.5k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Gary I. Dmitrienko Canada 22 677 498 333 309 300 74 1.5k
Arnaldo Fravolini Italy 22 670 1.0× 789 1.6× 244 0.7× 145 0.5× 339 1.1× 70 1.6k
Michael T. Flavin United States 21 995 1.5× 795 1.6× 405 1.2× 53 0.2× 294 1.0× 48 2.1k
Rubén Tommasi United States 18 363 0.5× 770 1.5× 326 1.0× 560 1.8× 278 0.9× 35 1.6k
Gregory S. Bisacchi United States 21 763 1.1× 639 1.3× 140 0.4× 123 0.4× 355 1.2× 35 1.7k
Ze‐Qi Xu United States 20 732 1.1× 490 1.0× 229 0.7× 51 0.2× 242 0.8× 50 1.4k
Tricia Naicker South Africa 24 1.3k 1.9× 664 1.3× 218 0.7× 125 0.4× 194 0.6× 142 2.5k
Martha S. Head United States 21 682 1.0× 1.8k 3.6× 333 1.0× 133 0.4× 311 1.0× 26 2.9k
Edmund L. Ellsworth United States 22 1.0k 1.5× 716 1.4× 197 0.6× 99 0.3× 141 0.5× 46 1.9k
Barbara Gatto Italy 29 951 1.4× 1.8k 3.7× 301 0.9× 92 0.3× 256 0.9× 87 2.8k
Dana E. Vanderwall United States 20 599 0.9× 1.3k 2.6× 307 0.9× 164 0.5× 213 0.7× 28 2.2k

Countries citing papers authored by Gary I. Dmitrienko

Since Specialization
Citations

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

Fields of papers citing papers by Gary I. Dmitrienko

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Gary I. Dmitrienko. 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 Gary I. Dmitrienko. The network helps show where Gary I. Dmitrienko may publish in the future.

Co-authorship network of co-authors of Gary I. Dmitrienko

This figure shows the co-authorship network connecting the top 25 collaborators of Gary I. Dmitrienko. A scholar is included among the top collaborators of Gary I. Dmitrienko 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 Gary I. Dmitrienko. Gary I. Dmitrienko 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.
O’Brien, Claire, Ebrahim Soleimani, Bradley Haltli, et al.. (2025). Amino-acid derived benzazaboroles: structure and function of a new chemotype. Organic & Biomolecular Chemistry. 23(34). 7786–7792.
2.
Assoud, Abdeljalil, et al.. (2019). Characterization of 3-[(Carboxymethyl)thio]picolinic Acid: A Novel Inhibitor of Phosphoenolpyruvate Carboxykinase. Biochemistry. 58(37). 3918–3926. 6 indexed citations
3.
Lu, Dawei, Hang Li, Denis‐Alexandre Trottier, et al.. (2015). Experimental Estimation of Average Fidelity of a Clifford Gate on a 7-Qubit Quantum Processor. Physical Review Letters. 114(14). 140505–140505. 38 indexed citations
4.
Marrone, Laura, Ahmad Ghavami, Geneviève Labbé, et al.. (2015). Arginine-containing peptides as potent inhibitors of VIM-2 metallo-β-lactamase. Biochimica et Biophysica Acta (BBA) - General Subjects. 1850(11). 2228–2238. 6 indexed citations
5.
Ghavami, Ahmad, Geneviève Labbé, Jürgen Brem, et al.. (2015). Assay for drug discovery: Synthesis and testing of nitrocefin analogues for use as β-lactamase substrates. Analytical Biochemistry. 486. 75–77. 15 indexed citations
6.
Labbé, Geneviève, et al.. (2011). Evaluation of four microbial Class II fructose 1,6-bisphosphate aldolase enzymes for use as biocatalysts. Protein Expression and Purification. 80(2). 224–233. 16 indexed citations
7.
O’Hara, Kimberley A., Gary I. Dmitrienko, & Brian B. Hasinoff. (2010). Kinamycin F downregulates cyclin D3 in human leukemia K562 cells. Chemico-Biological Interactions. 184(3). 396–402. 17 indexed citations
8.
Burk, Dan L., Ji‐Young Hwang, Ernest Y. Kwok, et al.. (2007). Structural Studies of the Final Enzyme in the α-Aminoadipate Pathway-Saccharopine Dehydrogenase from Saccharomyces cerevisiae. Journal of Molecular Biology. 373(3). 745–754. 17 indexed citations
9.
O’Hara, Kimberley A., Xing Wu, Daywin Patel, et al.. (2007). Mechanism of the cytotoxicity of the diazoparaquinone antitumor antibiotic kinamycin F. Free Radical Biology and Medicine. 43(8). 1132–1144. 40 indexed citations
10.
Viswanatha, Thammaiah, et al.. (2007). Assays for Β-Lactamase Activity and Inhibition. Methods in molecular medicine. 142. 239–260. 11 indexed citations
11.
Siemann, Stefan, Hamid R. Badiei, Vassili Karanassios, Thammaiah Viswanatha, & Gary I. Dmitrienko. (2005). 68Zn isotope exchange experiments reveal an unusual kinetic lability of the metal ions in the di-zinc form of IMP-1 metallo-β-lactamase. Chemical Communications. 532–534. 13 indexed citations
12.
Labbé, Geneviève, et al.. (2004). Molecular cloning, expression, purification, and characterization of fructose 1,6-bisphosphate aldolase from Mycobacterium tuberculosis—a novel Class II A tetramer. Protein Expression and Purification. 37(1). 220–228. 23 indexed citations
13.
Siemann, Stefan, Dyanne Brewer, Anthony J. Clarke, et al.. (2002). IMP-1 metallo-β-lactamase: effect of chelators and assessment of metal requirement by electrospray mass spectrometry. Biochimica et Biophysica Acta (BBA) - General Subjects. 1571(3). 190–200. 54 indexed citations
14.
Guo, Fusheng, et al.. (1999). The role of the non-conserved residue at position 104 of class A β-lactamases in susceptibility to mechanism-based inhibitors. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1431(1). 132–147. 6 indexed citations
15.
16.
Guo, Fusheng, Gary I. Dmitrienko, Anthony J. Clarke, & T. Viswanatha. (1996). The Role of the Nonconserved Residues at Position 167 of Class A β-Lactamases in Susceptibility to Mechanism-Based Inhibitors. Microbial Drug Resistance. 2(2). 261–268. 1 indexed citations
17.
Fletcher, Ronald S., Dominique Arion, Gadi Borkow, et al.. (1995). Synergistic Inhibition of HIV-1 Reverse Transcriptase DNA Polymerase Activity and Virus Replication in Vitro by Combinations of Carboxanilide Nonnucleoside Compounds. Biochemistry. 34(32). 10106–10112. 18 indexed citations
18.
Dmitrienko, Gary I., et al.. (1990). N-cyanoindoles and n-cyanoindole-4,7-diones: Construction of a bc ring synthon for the kinamycins. Tetrahedron Letters. 31(26). 3681–3684. 18 indexed citations
19.
Vice, Susan F., et al.. (1985). Selective side-chain bromination of n-acyl-2,3-dialkylindoles: synthesis and chemical modification of pyrrolo[1,2-a]indoles. Tetrahedron Letters. 26(43). 5253–5256. 15 indexed citations
20.
Vice, Susan F. & Gary I. Dmitrienko. (1982). The bromination–methanolysis of N-acetyl-2,3-dimethylindole. Canadian Journal of Chemistry. 60(10). 1233–1237. 13 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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