Author response: Unanticipated mechanisms of covalent inhibitor and synthetic ligand cobinding to PPARγ

Year: 2024

Type: peer-review

Abstract: Commonly used covalent PPARγ inhibitors weaken, but do not block, binding of other ligands via an allosteric mechanism where ligands clash with a covalent ligand-induced transcriptionally repressive structural conformation.

DOI: 10.7554/elife.99782.3.sa3

Authors: Jinsai Shang, Douglas J Kojetin

Institutions: Guangzhou Regenerative Medicine and Health Guangdong Laboratory, Vanderbilt University

Language: English

Topic: Peroxisome Proliferator-Activated Receptors

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

SDG: Good health and well-being

Open Access status: gold

Funders: U.S. Department of Energy, National Institutes of Health, Office of Science, National Institute of General Medical Sciences, National Institute of Diabetes and Digestive and Kidney Diseases, Basic Energy Sciences, Biological and Environmental Research, SLAC National Accelerator Laboratory

OpenAlex ID: W4404483106