Author

R. Brust

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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Biochemistry· 3 Biophysics· 2

Signature Assays, Organisms & Methods

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Approach:experimental assay· 5 Research Focus:chromatin & epigenetic regulation· 3 Organism:human· 3 Research Focus:protein folding & dynamics· 3 Assay:protein structure· 2 Assay:structural biology· 2 Approach:biophysical modeling· 1 Approach:statistical model· 1

Frequent Co-Authors

D. Kojetin· 4 shared J. Shang· 4 shared J. Bass· 3 shared P. Griffin· 3 shared P. Munoz-Tello· 2 shared S. A. Mosure· 2 shared T. Kamenecka· 2 shared A. A. Deniz· 1 shared

Activity by Year

2018-2022 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 32 mutual co-author links

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4 shared papersBiophysics

D. Kojetin

Mutual co-authors in cluster

Author profile →

5 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

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

Cooperative Cobinding of Synthetic and Natural Ligands to the Nuclear Receptor PPARγ

J. Shang, R. Brust, S. A. Mosure, J. Bass, P. Munoz-Tello, H. Lin, T. S. Hughes, M. Tang, Q. Ge, T. M. Kamekencka, D. J. Kojetin

The paper shows synthetic and natural ligands can bind cooperatively to PPARγ, altering its structure and function through a 'ligand link' to the omega loop.

bioRxiv · Nov 1, 2018Biochemistry

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