Author

D. J. 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

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Biochemistry· 1 Biophysics· 1 Immunology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Research Focus:protein folding & dynamics· 2 Approach:biophysical modeling· 1 Assay:bulk RNA-seq· 1 Research Focus:cell signaling & trafficking· 1 Research Focus:differential expression· 1 Research Focus:host-pathogen & immune response· 1 Approach:mechanistic / dynamical model· 1

Frequent Co-Authors

J. Shang· 3 shared P. Munoz-Tello· 2 shared T. S. Hughes· 2 shared A. Eliason· 1 shared B. Frey· 1 shared C. Hegner· 1 shared C. T. Weaver· 1 shared D. D. Moore· 1 shared

Activity by Year

2018-2020 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 25 mutual co-author links

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3 shared papersImmunology

J. Shang

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

CAR/Nr1i3 directs T cell adaptation to bile acids in the small intestine

M. L. Chen, X. Huang, H. Wang, Y. Liu, J. Shang, A. Eliason, C. Hegner, H. Park, B. Frey, G. Wang, D. J. Kojetin, C. T. Weaver, M. E. Pipkin, D. D. Moore, M. S. Sundrud

This study identifies CAR/Nr1i3 as a regulator of T cell adaptation to bile acids in the small intestine, showing its role in detoxification and inflammation resolution.

bioRxiv · Jul 30, 2020 · PreprintImmunology

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