Elizabeth A. Dierks

1.3k total citations
20 papers, 786 citations indexed

About

Elizabeth A. Dierks is a scholar working on Molecular Biology, Oncology and Pharmacology. According to data from OpenAlex, Elizabeth A. Dierks has authored 20 papers receiving a total of 786 indexed citations (citations by other indexed papers that have themselves been cited), including 9 papers in Molecular Biology, 7 papers in Oncology and 6 papers in Pharmacology. Recurrent topics in Elizabeth A. Dierks's work include Drug Transport and Resistance Mechanisms (6 papers), Pharmacogenetics and Drug Metabolism (6 papers) and Hemoglobin structure and function (3 papers). Elizabeth A. Dierks is often cited by papers focused on Drug Transport and Resistance Mechanisms (6 papers), Pharmacogenetics and Drug Metabolism (6 papers) and Hemoglobin structure and function (3 papers). Elizabeth A. Dierks collaborates with scholars based in United States, Germany and Sweden. Elizabeth A. Dierks's co-authors include Judith N. Burstyn, Anita E. Yu, S. Ball, Heng‐Keang Lim, Hong‐Xing Zhang, Georgia Cornelius, Paul R. Ortiz de Montellano, John H. Dawson, Kathleen M. Vogel and Songzhou Hu and has published in prestigious journals such as Journal of the American Chemical Society, Journal of Biological Chemistry and Neurology.

In The Last Decade

Elizabeth A. Dierks

20 papers receiving 758 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Elizabeth A. Dierks United States 13 309 269 234 161 147 20 786
Thomas M. Shea United States 11 537 1.7× 273 1.0× 325 1.4× 117 0.7× 125 0.9× 16 1.1k
Jung-Ja P. Kim United States 10 758 2.5× 408 1.5× 294 1.3× 192 1.2× 158 1.1× 10 1.3k
Rosemary Paschke United States 9 979 3.2× 344 1.3× 213 0.9× 136 0.8× 103 0.7× 10 1.5k
H. Shimada Japan 13 568 1.8× 367 1.4× 70 0.3× 133 0.8× 220 1.5× 16 1.2k
Satya Prakash Panda United States 18 247 0.8× 208 0.8× 138 0.6× 109 0.7× 42 0.3× 31 803
Chuanwu Xia United States 13 469 1.5× 292 1.1× 109 0.5× 139 0.9× 53 0.4× 20 772
Carmela Gnerre Switzerland 18 288 0.9× 192 0.7× 72 0.3× 234 1.5× 27 0.2× 39 1.1k
Laird A. Trimble Canada 24 578 1.9× 189 0.7× 89 0.4× 94 0.6× 72 0.5× 63 1.5k
David L. Roberts United States 6 591 1.9× 261 1.0× 89 0.4× 104 0.6× 67 0.5× 7 907
Benjamin C. Lewis Australia 19 360 1.2× 436 1.6× 69 0.3× 238 1.5× 20 0.1× 27 938

Countries citing papers authored by Elizabeth A. Dierks

Since Specialization
Citations

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

Fields of papers citing papers by Elizabeth A. Dierks

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Elizabeth A. Dierks

This figure shows the co-authorship network connecting the top 25 collaborators of Elizabeth A. Dierks. A scholar is included among the top collaborators of Elizabeth A. Dierks 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 Elizabeth A. Dierks. Elizabeth A. Dierks 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.
Subbaiah, Murugaiah A. M., Srikanth Sridhar, Manoj Chiney, et al.. (2024). Prodrug Strategy to Address Impaired Oral Absorption of a Weakly Basic TYK2 Inhibitor Caused by a Gastric Acid-Reducing Agent. Journal of Medicinal Chemistry. 67(22). 20664–20681. 5 indexed citations
2.
Bunin, Anna, Seong Lee, Simone M. Nicholson, et al.. (2024). Novel Bispecific Degrader BHV-1300 Achieves Rapid, Robust, and Selective IgG Reduction in Preclinical Models Including Nonhuman Primates (S43.004). Neurology. 102(7_supplement_1). 1 indexed citations
3.
Lupisella, John A., Stéphane St-Onge, Marilyn Carrier, et al.. (2022). Molecular Mechanisms of Desensitization Underlying the Differential Effects of Formyl Peptide Receptor 2 Agonists on Cardiac Structure–Function Post Myocardial Infarction. ACS Pharmacology & Translational Science. 5(10). 892–906. 12 indexed citations
4.
Wurtz, Nicholas R., James A. Johnson, Andrew Q. Viet, et al.. (2022). Discovery of Heteroaryl Urea Isosteres for Formyl Peptide Receptor 2 Agonists. ACS Medicinal Chemistry Letters. 13(6). 943–948. 4 indexed citations
5.
Dierks, Elizabeth A., et al.. (2019). Application of ultrasound‐guided cholecystocentesis to the evaluation of the metabolite profiling in bile of dogs and cynomolgus monkeys. Pharmacology Research & Perspectives. 7(3). e00488–e00488. 3 indexed citations
6.
Chang, Shu, et al.. (2018). Assessment of pre‐operative maropitant citrate use in macaque (Macaca fasicularis & Macaca mulatta) neurosurgical procedures. Journal of Medical Primatology. 47(3). 178–184. 2 indexed citations
7.
Dierks, Elizabeth A., et al.. (2018). Single-species Allometric Scaling: A Strategic Approach to Support Drug Discovery. Journal of Pharmaceutical Research International. 22(3). 1–7. 2 indexed citations
8.
Luettgen, Joseph M., Pancras C. Wong, Vidya Perera, et al.. (2017). Abstract TMP117: Preclinical and Early Clinical Characterization of a Parenterally Administered Direct Factor XIa Inhibitor. Stroke. 48(suppl_1). 3 indexed citations
9.
Morse, Bridget L., Hong Cai, Lisa Zhang, et al.. (2015). Rosuvastatin Liver Partitioning in Cynomolgus Monkeys: Measurement In Vivo and Prediction Using In Vitro Monkey Hepatocyte Uptake. Drug Metabolism and Disposition. 43(11). 1788–1794. 22 indexed citations
10.
Sun, Qin, Timothy W. Harper, Elizabeth A. Dierks, et al.. (2011). 1-Aminobenzotriazole, a Known Cytochrome P450 Inhibitor, Is a Substrate and Inhibitor of N-Acetyltransferase. Drug Metabolism and Disposition. 39(9). 1674–1679. 34 indexed citations
11.
12.
Dierks, Elizabeth A., et al.. (2001). A method for the simultaneous evaluation of the activities of seven major human drug-metabolizing cytochrome P450s using an in vitro cocktail of probe substrates and fast gradient liquid chromatography tandem mass spectrometry.. PubMed. 29(1). 23–9. 204 indexed citations
13.
Vogel, Kathleen M., Songzhou Hu, Thomas G. Spiro, et al.. (1999). Variable forms of soluble guanylyl cyclase: protein-ligand interactions and the issue of activation by carbon monoxide. JBIC Journal of Biological Inorganic Chemistry. 4(6). 804–813. 47 indexed citations
14.
Dierks, Elizabeth A. & Judith N. Burstyn. (1998). The Deactivation of Soluble Guanylyl Cyclase by Redox-Active Agents,. Archives of Biochemistry and Biophysics. 351(1). 1–7. 36 indexed citations
15.
Dierks, Elizabeth A., Stephanie Davis, & Paul R. Ortiz de Montellano. (1998). Glu-320 and Asp-323 Are Determinants of the CYP4A1 Hydroxylation Regiospecificity and Resistance to Inactivation by 1-Aminobenzotriazole. Biochemistry. 37(7). 1839–1847. 54 indexed citations
16.
Halpert, James R., Tammy L. Domanski, Orhan Adalı, et al.. (1998). Structure-function of cytochromes P450 and flavin-containing monooxygenases: implications for drug metabolism.. PubMed. 26(12). 1223–31. 15 indexed citations
17.
Dierks, Elizabeth A., Zhoupeng Zhang, Eric F. Johnson, & Paul R. Ortiz de Montellano. (1998). The Catalytic Site of Cytochrome P4504A11 (CYP4A11) and Its L131F Mutant. Journal of Biological Chemistry. 273(36). 23055–23061. 32 indexed citations
18.
Dierks, Elizabeth A., Songzhou Hu, Kathleen M. Vogel, et al.. (1997). Demonstration of the Role of Scission of the Proximal Histidine−Iron Bond in the Activation of Soluble Guanylyl Cyclase through Metalloporphyrin Substitution Studies. Journal of the American Chemical Society. 119(31). 7316–7323. 70 indexed citations
19.
Dierks, Elizabeth A. & Judith N. Burstyn. (1996). Nitric oxide (NO•), the only nitrogen monoxide redox form capable of activating soluble guanylyl cyclase. Biochemical Pharmacology. 51(12). 1593–1600. 83 indexed citations
20.

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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