Gregory T. DeKoster

799 total citations
23 papers, 634 citations indexed

About

Gregory T. DeKoster is a scholar working on Molecular Biology, Oncology and Epidemiology. According to data from OpenAlex, Gregory T. DeKoster has authored 23 papers receiving a total of 634 indexed citations (citations by other indexed papers that have themselves been cited), including 14 papers in Molecular Biology, 7 papers in Oncology and 4 papers in Epidemiology. Recurrent topics in Gregory T. DeKoster's work include Drug Transport and Resistance Mechanisms (7 papers), Protein Structure and Dynamics (6 papers) and Protein Interaction Studies and Fluorescence Analysis (3 papers). Gregory T. DeKoster is often cited by papers focused on Drug Transport and Resistance Mechanisms (7 papers), Protein Structure and Dynamics (6 papers) and Protein Interaction Studies and Fluorescence Analysis (3 papers). Gregory T. DeKoster collaborates with scholars based in United States, Denmark and Germany. Gregory T. DeKoster's co-authors include David P. Cistola, Andrew D. Robertson, Katherine A. Henzler‐Wildman, Gregory P. Tochtrop, Douglas F. Covey, Taekjip Ha, Reza Vafabakhsh, Dorothee Kern, Michael W. Clarkson and Emma A. Morrison and has published in prestigious journals such as Nature, Proceedings of the National Academy of Sciences and Journal of the American Chemical Society.

In The Last Decade

Gregory T. DeKoster

23 papers receiving 629 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Gregory T. DeKoster United States 14 358 160 74 72 68 23 634
Abhinav Kumar United Kingdom 14 423 1.2× 109 0.7× 59 0.8× 141 2.0× 59 0.9× 38 791
Andrew F. Wilderspin United Kingdom 17 803 2.2× 165 1.0× 66 0.9× 50 0.7× 69 1.0× 26 1.2k
Thomas Tomasiak United States 11 393 1.1× 162 1.0× 55 0.7× 27 0.4× 42 0.6× 19 680
Bernhard Pfeiffer Switzerland 18 579 1.6× 157 1.0× 75 1.0× 54 0.8× 36 0.5× 46 1.1k
Agnes Rinaldo-Matthis Sweden 18 670 1.9× 101 0.6× 102 1.4× 16 0.2× 48 0.7× 35 1.0k
Shafinaz F. Chowdhury Canada 14 465 1.3× 104 0.7× 43 0.6× 21 0.3× 111 1.6× 21 850
Inmaculada Pérez‐Dorado Spain 15 507 1.4× 48 0.3× 116 1.6× 26 0.4× 83 1.2× 25 823
Maria U. Johansson Sweden 10 396 1.1× 49 0.3× 68 0.9× 31 0.4× 63 0.9× 13 637
K. Saraboji India 16 589 1.6× 54 0.3× 161 2.2× 47 0.7× 33 0.5× 51 996
S. Kumaran India 16 740 2.1× 108 0.7× 105 1.4× 30 0.4× 21 0.3× 41 1.0k

Countries citing papers authored by Gregory T. DeKoster

Since Specialization
Citations

This map shows the geographic impact of Gregory T. DeKoster'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 Gregory T. DeKoster with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Gregory T. DeKoster more than expected).

Fields of papers citing papers by Gregory T. DeKoster

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Gregory T. DeKoster. 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 Gregory T. DeKoster. The network helps show where Gregory T. DeKoster may publish in the future.

Co-authorship network of co-authors of Gregory T. DeKoster

This figure shows the co-authorship network connecting the top 25 collaborators of Gregory T. DeKoster. A scholar is included among the top collaborators of Gregory T. DeKoster 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 Gregory T. DeKoster. Gregory T. DeKoster 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.
Stuchell‐Brereton, Melissa D., Maxwell I. Zimmerman, Upasana L. Mallimadugula, et al.. (2023). Apolipoprotein E4 has extensive conformational heterogeneity in lipid-free and lipid-bound forms. Proceedings of the National Academy of Sciences. 120(7). e2215371120–e2215371120. 24 indexed citations
2.
Ruben, Eliza A., Prafull S. Gandhi, Zhiwei Chen, et al.. (2020). 19F NMR reveals the conformational properties of free thrombin and its zymogen precursor prethrombin-2. Journal of Biological Chemistry. 295(24). 8227–8235. 10 indexed citations
3.
Petroff, John T., et al.. (2020). Charge Reduction of Membrane Proteins in Native Mass Spectrometry Using Alkali Metal Acetate Salts. Analytical Chemistry. 92(9). 6622–6630. 9 indexed citations
4.
Yao, Yuewei, Gregory T. DeKoster, & William E. Buhro. (2019). Interchange of L-, Z-, and Bound-Ion-Pair X-Type Ligation on Cadmium Selenide Quantum Belts. Chemistry of Materials. 31(11). 4299–4312. 18 indexed citations
5.
Weber, Gert, et al.. (2018). Molecular principles underlying dual RNA specificity in the Drosophila SNF protein. Nature Communications. 9(1). 2220–2220. 4 indexed citations
6.
Mondal, Tridib, et al.. (2016). ApoE: In Vitro Studies of a Small Molecule Effector. Biochemistry. 55(18). 2613–2621. 14 indexed citations
7.
Horváth, Gergő, Ákos Bencsura, Ágnes Simon, et al.. (2015). Structural determinants of ligand binding in the ternary complex of human ileal bile acid binding protein with glycocholate and glycochenodeoxycholate obtained from solution NMR. FEBS Journal. 283(3). 541–555. 14 indexed citations
8.
Batchelor, Joseph D., et al.. (2014). Red Blood Cell Invasion by Plasmodium vivax: Structural Basis for DBP Engagement of DARC. PLoS Pathogens. 10(1). e1003869–e1003869. 81 indexed citations
9.
DeKoster, Gregory T., et al.. (2014). A Compare-and-Contrast NMR Dynamics Study of Two Related RRMs: U1A and SNF. Biophysical Journal. 107(1). 208–219. 6 indexed citations
10.
Morrison, Emma A., Gregory T. DeKoster, Supratik Dutta, et al.. (2011). Antiparallel EmrE exports drugs by exchanging between asymmetric structures. Nature. 481(7379). 45–50. 171 indexed citations
11.
Beck, Moriah R., Gregory T. DeKoster, David P. Cistola, & William E. Goldman. (2009). NMR structure of a fungal virulence factor reveals structural homology with mammalian saposin B. Molecular Microbiology. 72(2). 344–353. 24 indexed citations
12.
Lu, Jianyun, Minghe Chen, Gregory T. DeKoster, David P. Cistola, & Ellen Li. (2008). The RXRα C-terminus T462 is a NMR sensor for coactivator peptide binding. Biochemical and Biophysical Research Communications. 366(4). 932–937. 6 indexed citations
13.
Jastrzębska, Izabella, Jamie B. Scaglione, Gregory T. DeKoster, Nigam P. Rath, & Douglas F. Covey. (2007). Palladium-Catalyzed Potassium Enoxyborate Alkylation of Enantiopure Hajos−Parrish Indenone To Construct Rearranged Steroid Ring Systems. The Journal of Organic Chemistry. 72(13). 4837–4843. 17 indexed citations
14.
Scaglione, Jamie B., Brad Manion, Ann Benz, et al.. (2006). Neurosteroid Analogues. 11. Alternative Ring System Scaffolds:  γ-Aminobutyric Acid Receptor Modulation and Anesthetic Actions of Benz[f]indenes. Journal of Medicinal Chemistry. 49(15). 4595–4605. 13 indexed citations
15.
Tőke, Orsolya, John Monsey, Gregory T. DeKoster, et al.. (2005). Determinants of Cooperativity and Site Selectivity in Human Ileal Bile Acid Binding Protein. Biochemistry. 45(3). 727–737. 49 indexed citations
16.
DeKoster, Gregory T., et al.. (2004). The NMR structure of a stable and compact all‐β‐sheet variant of intestinal fatty acid‐binding protein. Protein Science. 13(5). 1227–1237. 12 indexed citations
17.
Tochtrop, Gregory P., Gregory T. DeKoster, David P. Cistola, & Douglas F. Covey. (2002). A Simple Efficient Synthesis of [23,24]-13C2-Labeled Bile Salts as NMR Probes of Protein–Ligand Interactions. Bioorganic & Medicinal Chemistry Letters. 12(3). 433–435. 10 indexed citations
18.
DeKoster, Gregory T. & Andrew D. Robertson. (1997). Thermodynamics of Unfolding for Kazal-Type Serine Protease Inhibitors:  Entropic Stabilization of Ovomucoid First Domain by Glycosylation. Biochemistry. 36(8). 2323–2331. 42 indexed citations
19.
DeKoster, Gregory T. & Andrew D. Robertson. (1997). Calorimetrically-derived parameters for protein interactions with urea and guanidine-HCl are not consistent with denaturant m values. Biophysical Chemistry. 64(1-3). 59–68. 18 indexed citations
20.
DeKoster, Gregory T. & Andrew D. Robertson. (1995). Cold Denaturation of CheY. Journal of Molecular Biology. 249(3). 529–534. 10 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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