Douglas J. Kojetin

Scripps Research Institute — United States

Biochemistry, Genetics and Molecular Biology · Life Sciences

43h-index6.3kcitations189works2.92yr avg
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Research Topics

Peroxisome Proliferator-Activated Receptors(51), Estrogen and related hormone effects(41), Nuclear Receptors and Signaling(33), Receptor Mechanisms and Signaling(25), Computational Drug Discovery Methods(19)

Publications189 total

Reviewer #1 (Public review): Shifting the PPARγ conformational ensemble towards a transcriptionally repressive state improves covalent inhibitor efficacy
2026Open Access
Reviewer #2 (Public review): Shifting the PPARγ conformational ensemble towards a transcriptionally repressive state improves covalent inhibitor efficacy
2026Open Access
Author response: Shifting the PPARγ conformational ensemble towards a transcriptionally repressive state improves covalent inhibitor efficacy
2026Open Access
Shifting the PPARγ conformational ensemble towards a transcriptionally repressive state improves covalent inhibitor efficacy
2026Open Access
Structural insights into IMP2 dimerization and RNA binding
Journal of Structural Biology·2025· 1 citedOpen Access
Structural Basis of PPARγ-Mediated Transcriptional Repression by the Covalent Inverse Agonist FX-909
Journal of Medicinal Chemistry·2025· 2 citedOpen Access
Towards a unified molecular mechanism for ligand-dependent activation of NR4A-RXR heterodimers
2025· 1 citedOpen Access
Towards a unified molecular mechanism for ligand-dependent activation of NR4A-RXR heterodimers
2025Open Access
A tethering mechanism underlies Pin1-catalyzed proline <i>cis–trans</i> isomerization at a noncanonical site
Proceedings of the National Academy of Sciences·2025Open Access
Shifting the PPARγ conformational ensemble toward a transcriptionally repressive state improves covalent inhibitor efficacy
eLife·2025Open Access
Shifting the PPARγ conformational ensemble towards a transcriptionally repressive state improves covalent inhibitor efficacy
2025Open Access
Structural basis of PPARγ-mediated transcriptional repression by the covalent inverse agonist FX-909
2025· 1 citedOpen Access
Correction: Molecular basis of ligand-dependent Nurr1-RXRα activation
eLife·2025· 1 citedOpen Access
Towards a unified molecular mechanism for ligand-dependent activation of NR4A-RXR heterodimers
2025Open Access
Shifting the PPARγ conformational ensemble towards a transcriptionally repressive state improves covalent inhibitor efficacy
2025Open Access
Ligand efficacy shifts a nuclear receptor conformational ensemble between transcriptionally active and repressive states
Nature Communications·2025· 20 citedOpen Access
The endocannabinoid anandamide mediates anti‐inflammatory effects through activation of NR4A nuclear receptors
British Journal of Pharmacology·2024· 8 citedOpen Access
Unanticipated mechanisms of covalent inhibitor and synthetic ligand cobinding to PPARγ
eLife·2024Open Access
Author response: Unanticipated mechanisms of covalent inhibitor and synthetic ligand cobinding to PPARγ
2024Open Access
Unanticipated mechanisms of covalent inhibitor and synthetic ligand cobinding to PPARγ
2024Open Access
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Frequent Co-authors

Tudor Hughes(15), Patrick R. Griffin(15), Jinsai Shang(15), Theodore M. Kamenecka(14), Thomas P. Burris(14), Ian Mitchelle S. de Vera(13), Richard Brust(11), Laura A. Solt(10), Sarah A. Mosure(8), Jakob Fuhrmann(7), J.C. Nwachukwu(6), K.W. Nettles(6), Paola Munoz‐Tello(6), David Marciano(5), Mark Rance(5), Jason Nowak(5), Jie Zheng(5), John Cavanagh(5), Yongjun Wang(4), Michael D. Cameron(4)