Author

P. Munoz-Tello

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· 3 Research Focus:protein folding & dynamics· 3 Organism:human· 2 Assay:protein structure· 2 Approach:biophysical modeling· 1 Research Focus:cell type annotation· 1 Approach:mechanistic / dynamical model· 1 Assay:proteomics· 1

Frequent Co-Authors

D. J. Kojetin· 2 shared D. Kojetin· 2 shared H. Lin· 2 shared J. Bass· 2 shared J. Shang· 2 shared P. R. Griffin· 2 shared R. Brust· 2 shared S. A. Mosure· 2 shared

Activity by Year

2018-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 37 mutual co-author links

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2 shared papersBiochemistry

D. J. Kojetin

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4 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

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

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

Defining a canonical ligand-binding pocket in the orphan nuclear receptor Nurr1

I. M. S. de Vera, P. Munoz-Tello, V. Dharmarajan, D. P. Marciano, E. Matta-Camacho, P. K. Giri, J. Shang, T. S. Hughes, M. Rance, P. R. Griffin, D. J. Kojetin

This study shows the Nurr1 ligand-binding domain has a dynamic, solvent-accessible pocket that can bind unsaturated fatty acids, challenging the notion that it lacks a canonical ligand-binding pocket.

bioRxiv · Apr 17, 2018Biophysics