Author

T. Kamenecka

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biophysics· 2 Biochemistry· 1 Pharmacology & Toxicology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Organism:human· 3 Research Focus:chromatin & epigenetic regulation· 2 Research Focus:protein folding & dynamics· 2 Assay:proteomics· 2 Approach:statistical model· 2 Research Focus:cell type annotation· 1 Research Focus:drug response / drug discovery· 1

Frequent Co-Authors

D. Kojetin· 3 shared J. Shang· 2 shared P. Griffin· 2 shared R. Brust· 2 shared A. Cano· 1 shared A.-L. Blayo· 1 shared C. Doebellin· 1 shared H. Lin· 1 shared

Activity by Year

2018-2020 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 23 mutual co-author links

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3 shared papersPharmacology & Toxicology

D. Kojetin

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

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

HDX-MS reveals structural determinants for RORγ hyperactivation by synthetic agonists

T. S. Strutzenberg, R. Garcia-Ordonez, S. Novick, H. Park, M. R. Chang, C. Doebellin, Y. He, R. Patouret, T. Kamenecka, P. R. Griffin

This study uses HDX-MS to identify structural determinants of RORγ hyperactivation by synthetic agonists, showing correlations between receptor dynamics and activity.

bioRxiv · Mar 26, 2019Biophysics

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