Author
D. Kojetin
Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.
Biology Disciplines
Click to filter author papersSignature Assays, Organisms & Methods
Click to filter · or open tagActivity by Year
2018-2022 · peak 3/yrCo-Author Collaboration Network
10 top collaborators · 32 mutual co-author links8 papers
Recent·Most cited
Structural basis of interdomain communication in PPARγ
S. A. Mosure, P. Munoz-Tello, K.-T. Kuo, B. MacTavish, X. Yu, D. Scholl, C. C. Williams, T. S. Strutzenberg, J. Li, J. Bass, R. Brust, E. Kalkhoven, A. A. Deniz, P. R. Griffin, D. Kojetin
This study identifies a conserved Trp-Pro motif in PPARγ AF-1 that undergoes cis/trans isomerization, enabling interdomain communication with the LBD and affecting transcriptional activity.
bioRxiv · Jul 13, 2022 · PreprintBiophysics
Structural Mechanism Underlying Ligand Binding and Activation of PPARγ
This study reveals that PPARγ ligand binding involves a two-step induced fit mechanism, supported by NMR, SPR, and ITC analyses, with ligand entry through a surface pore and conformational changes leading to active helix 12 exposure.
bioRxiv · Sep 22, 2020Biophysics
Chemical Systems Biology Reveals Mechanisms of Glucocorticoid Receptor Signaling
N. Bruno, J. C. Nwachukwu, S. Srinivasan, C. C. Nettles, T. Izard, z. Jin, S. Boregowda, D. Phinney, O. Elemento, X. Liu, E. A. Ortlund, R. Houtman, D. Stavreva, G. Hager, T. Kamencka, , K. W. Nettles
The paper uses Ligand Class Analysis to identify target genes and coregulator interactions of glucocorticoid receptor ligands, revealing mechanisms linking ligand structure to physiological outcomes.
bioRxiv · Jun 15, 2020Pharmacology & Toxicology
Assessment of NR4A Ligands that Directly Bind and Modulate the Orphan Nuclear Receptor Nurr1
P. Munoz-Tello, H. Lin, P. Khan, I. de Vera, T. Kamenecka, D. Kojetin
The paper assesses twelve NR4A ligands to determine if they directly bind and modulate Nurr1 or act through effector proteins, finding some bind directly while others do not.
bioRxiv · May 22, 2020Pharmacology & Toxicology
Quantitative Structural Assessment of Graded Receptor Agonism
J. Shang, R. Brust, P. Griffin, T. Kamenecka, D. Kojetin
The paper quantifies how agonist structure affects PPARγ conformational changes, showing efficacy correlates with shifts toward active states detected by NMR.
bioRxiv · Apr 29, 2019Biophysics
Structural basis of altered potency and efficacy displayed by a major in vivo metabolite of the anti-diabetic PPARγ drug pioglitazone
S. Mosure, J. Shang, R. Brust, J. Zheng, P. Griffin, D. Kojetin
This study compares the structure and function of pioglitazone and its metabolite 1-hydroxypioglitazone bound to PPARγ, showing reduced potency and efficacy of the metabolite.
bioRxiv · Aug 13, 2018Biochemistry
A structural mechanism for directing inverse agonism of PPARγ
R. Brust, J. Shang, J. Fuhrmann, J. Bass, A. Cano, Z. Heidari, I. Chrisman, A.-L. Blayo, P. Griffin, T. Kamenecka, T. Hughes, D. Kojetin
The paper shows how a phenyl-to-pyridyl substitution in PPARγ ligands converts an antagonist to an inverse agonist through a water-mediated hydrogen bond network involving Arg288.
bioRxiv · Jan 17, 2018Biochemistry