Theodore M. Kamenecka

11.2k total citations · 2 hit papers
148 papers, 8.3k citations indexed

About

Theodore M. Kamenecka is a scholar working on Molecular Biology, Organic Chemistry and Physiology. According to data from OpenAlex, Theodore M. Kamenecka has authored 148 papers receiving a total of 8.3k indexed citations (citations by other indexed papers that have themselves been cited), including 93 papers in Molecular Biology, 25 papers in Organic Chemistry and 24 papers in Physiology. Recurrent topics in Theodore M. Kamenecka's work include Peroxisome Proliferator-Activated Receptors (27 papers), Receptor Mechanisms and Signaling (25 papers) and Adipose Tissue and Metabolism (17 papers). Theodore M. Kamenecka is often cited by papers focused on Peroxisome Proliferator-Activated Receptors (27 papers), Receptor Mechanisms and Signaling (25 papers) and Adipose Tissue and Metabolism (17 papers). Theodore M. Kamenecka collaborates with scholars based in United States, Australia and China. Theodore M. Kamenecka's co-authors include Patrick R. Griffin, Thomas P. Burris, Laura A. Solt, Michael D. Cameron, Samuel J. Danishefsky, Michael J. Chalmers, Youseung Shin, Douglas J. Kojetin, Bruce M. Spiegelman and Yuanjun He and has published in prestigious journals such as Nature, Cell and Proceedings of the National Academy of Sciences.

In The Last Decade

Theodore M. Kamenecka

147 papers receiving 8.2k citations

Hit Papers

Anti-diabetic drugs inhibit obesity-linked phosphorylatio... 2010 2026 2015 2020 2010 2012 200 400 600

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Theodore M. Kamenecka United States 45 4.0k 2.1k 1.6k 1.0k 900 148 8.3k
Michael D. Cameron United States 46 4.0k 1.0× 1.0k 0.5× 892 0.6× 929 0.9× 373 0.4× 171 7.5k
Zhihong Huang China 33 5.6k 1.4× 2.5k 1.2× 574 0.4× 371 0.4× 1.5k 1.7× 135 12.5k
Thomas P. Burris United States 64 6.4k 1.6× 3.0k 1.5× 3.0k 1.9× 492 0.5× 1.7k 1.9× 190 13.4k
Keisuke Hirai Japan 35 3.3k 0.8× 3.6k 1.7× 558 0.4× 417 0.4× 284 0.3× 110 7.7k
Simonetta Camandola United States 43 3.5k 0.9× 2.3k 1.1× 431 0.3× 191 0.2× 963 1.1× 77 8.1k
Lotte Bjerre Knudsen Denmark 50 4.4k 1.1× 1.5k 0.7× 1.2k 0.8× 223 0.2× 183 0.2× 105 10.5k
Bei B. Zhang United States 38 3.9k 1.0× 2.9k 1.4× 1.2k 0.8× 156 0.2× 350 0.4× 68 8.6k
Ana I. Rojo Spain 44 6.3k 1.6× 1.2k 0.6× 257 0.2× 580 0.6× 713 0.8× 75 9.5k
Kenneth Hensley United States 53 3.7k 0.9× 3.2k 1.6× 257 0.2× 741 0.7× 661 0.7× 130 9.7k
Miguel A. Pappolla United States 42 3.0k 0.7× 4.7k 2.3× 879 0.6× 371 0.4× 233 0.3× 103 8.3k

Countries citing papers authored by Theodore M. Kamenecka

Since Specialization
Citations

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

Fields of papers citing papers by Theodore M. Kamenecka

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Theodore M. Kamenecka. 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 Theodore M. Kamenecka. The network helps show where Theodore M. Kamenecka may publish in the future.

Co-authorship network of co-authors of Theodore M. Kamenecka

This figure shows the co-authorship network connecting the top 25 collaborators of Theodore M. Kamenecka. A scholar is included among the top collaborators of Theodore M. Kamenecka 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 Theodore M. Kamenecka. Theodore M. Kamenecka 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.
Chan, Priscilla, Theodore M. Kamenecka, Laura A. Solt, et al.. (2025). Advancing clinical response against glioblastoma: Evaluating SHP1705 CRY2 activator efficacy in preclinical models and safety in phase I trials. Neuro-Oncology. 27(7). 1772–1786. 6 indexed citations
2.
Munoz‐Tello, Paola, Xiaoyu Yu, Joel M. Harp, et al.. (2025). Structural Basis of PPARγ-Mediated Transcriptional Repression by the Covalent Inverse Agonist FX-909. Journal of Medicinal Chemistry. 68(16). 17587–17597.
3.
Voren, George, Christie D. Fowler, Qun Lu, et al.. (2024). SR9883 is a novel small-molecule enhancer of α4β2* nicotinic acetylcholine receptor signaling that decreases intravenous nicotine self-administration in rats. Frontiers in Molecular Neuroscience. 17. 1459098–1459098. 2 indexed citations
4.
Carver, Chase M., Elizabeth J. Atkinson, Jair Machado Espíndola‐Netto, et al.. (2024). IL-23R is a senescence-linked circulating and tissue biomarker of aging. Nature Aging. 5(2). 291–305. 10 indexed citations
5.
Liu, Chi‐Hsiu, Theodore M. Kamenecka, John Paul SanGiovanni, et al.. (2023). Genetic deficiency and pharmacological modulation of RORα regulate laser-induced choroidal neovascularization. Aging. 15(1). 37–52. 4 indexed citations
6.
Frkic, Rebecca L., Blagojce Jovcevski‬, Wioleta Kowalczyk, et al.. (2023). PPARγ Corepression Involves Alternate Ligand Conformation and Inflation of H12 Ensembles. ACS Chemical Biology. 18(5). 1115–1123. 5 indexed citations
7.
Huang, Shuo, Chi‐Hsiu Liu, Zhongxiao Wang, et al.. (2022). REV-ERBα regulates age-related and oxidative stress-induced degeneration in retinal pigment epithelium via NRF2. Redox Biology. 51. 102261–102261. 23 indexed citations
8.
Radnai, László, M. D. Surman, Erica J. Young, et al.. (2021). Discovery of Selective Inhibitors for In Vitro and In Vivo Interrogation of Skeletal Myosin II. ACS Chemical Biology. 16(11). 2164–2173. 4 indexed citations
9.
Klenk, Christoph, S.A. Eberle, Philipp Heine, et al.. (2021). Complexes of the neurotensin receptor 1 with small-molecule ligands reveal structural determinants of full, partial, and inverse agonism. Science Advances. 7(5). 33 indexed citations
10.
Lin, Hua, Kfir Sharabi, Lin Li, et al.. (2021). Structure–Activity Relationship and Biological Investigation of SR18292 (16), a Suppressor of Glucagon-Induced Glucose Production. Journal of Medicinal Chemistry. 64(2). 980–990. 4 indexed citations
11.
Munoz‐Tello, Paola, et al.. (2020). Assessment of NR4A Ligands That Directly Bind and Modulate the Orphan Nuclear Receptor Nurr1. Journal of Medicinal Chemistry. 63(24). 15639–15654. 46 indexed citations
12.
Chang, Mi Ra, Timothy S. Strutzenberg, Scott J. Novick, et al.. (2019). Unique Polypharmacology Nuclear Receptor Modulator Blocks Inflammatory Signaling Pathways. ACS Chemical Biology. 14(5). 1051–1062. 8 indexed citations
13.
Heidari, Zahra, Michelle D. Nemetchek, Scott J. Novick, et al.. (2019). Definition of functionally and structurally distinct repressive states in the nuclear receptor PPARγ. Nature Communications. 10(1). 5825–5825. 31 indexed citations
14.
Shang, Jinsai, Richard Brust, Patrick R. Griffin, Theodore M. Kamenecka, & Douglas J. Kojetin. (2019). Quantitative structural assessment of graded receptor agonism. Proceedings of the National Academy of Sciences. 116(44). 22179–22188. 29 indexed citations
15.
Strutzenberg, Timothy S., Rubén D. Garcia-Ordoñez, Scott J. Novick, et al.. (2019). HDX-MS reveals structural determinants for RORγ hyperactivation by synthetic agonists. eLife. 8. 12 indexed citations
16.
Tavares, Clint D.J., Kfir Sharabi, John E. Dominy, et al.. (2016). The Methionine Transamination Pathway Controls Hepatic Glucose Metabolism through Regulation of the GCN5 Acetyltransferase and the PGC-1α Transcriptional Coactivator. Journal of Biological Chemistry. 291(20). 10635–10645. 34 indexed citations
17.
Robinson, James, Anthony M. Smith, Emmanuel Sturchler, et al.. (2013). Development of a High-Throughput Screening–Compatible Cell-Based Functional Assay to Identify Small Molecule Probes of the Galanin 3 Receptor (GalR3). Assay and Drug Development Technologies. 11(8). 468–477. 12 indexed citations
18.
Shin, Youseung, Wei‐Ming Chen, Jeff E. Habel, et al.. (2009). Synthesis and SAR of piperazine amides as novel c-jun N-terminal kinase (JNK) inhibitors. Bioorganic & Medicinal Chemistry Letters. 19(12). 3344–3347. 24 indexed citations
19.
Hollander, Jonathan A., Qun Lu, Michael D. Cameron, Theodore M. Kamenecka, & Paul J. Kenny. (2008). Insular hypocretin transmission regulates nicotine reward. Proceedings of the National Academy of Sciences. 105(49). 19480–19485. 224 indexed citations
20.
Lin, Linus S., Thomas J. Lanza, Laurie A. Castonguay, et al.. (2004). Bioisosteric replacement of anilide with benzoxazole: potent and orally bioavailable antagonists of VLA-4. Bioorganic & Medicinal Chemistry Letters. 14(9). 2331–2334. 14 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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