Zobrazeno 1 - 10
of 31
pro vyhledávání: '"Richard Brust"'
Autor:
Jinsai Shang, Sarah A. Mosure, Jie Zheng, Richard Brust, Jared Bass, Ashley Nichols, Laura A. Solt, Patrick R. Griffin, Douglas J. Kojetin
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-14 (2020)
Structural studies of nuclear receptor transcription factors revealed that nearly all nuclear receptors share a conserved helix 12 dependent transcriptional activation mechanism. Here the authors present two crystal structures of peroxisome prolifera
Externí odkaz:
https://doaj.org/article/9d32e7db99b24a56b787934b31a56130
Autor:
Richard Brust, Jinsai Shang, Jakob Fuhrmann, Sarah A. Mosure, Jared Bass, Andrew Cano, Zahra Heidari, Ian M. Chrisman, Michelle D. Nemetchek, Anne-Laure Blayo, Patrick R. Griffin, Theodore M. Kamenecka, Travis S. Hughes, Douglas J. Kojetin
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-14 (2018)
Peroxisome proliferator-activated receptor gamma (PPARγ) is a target for insulin sensitizing drugs. Here the authors combine NMR, X-ray crystallography and MD simulations and report a structural mechanism for eliciting PPARγ inverse agonism, where
Externí odkaz:
https://doaj.org/article/83045b413545471dafc949ec4db32b64
Autor:
Jinsai Shang, Richard Brust, Sarah A Mosure, Jared Bass, Paola Munoz-Tello, Hua Lin, Travis S Hughes, Miru Tang, Qingfeng Ge, Theodore M Kamenekca, Douglas J Kojetin
Publikováno v:
eLife, Vol 7 (2018)
Crystal structures of peroxisome proliferator-activated receptor gamma (PPARγ) have revealed overlapping binding modes for synthetic and natural/endogenous ligands, indicating competition for the orthosteric pocket. Here we show that cobinding of a
Externí odkaz:
https://doaj.org/article/a02167cd994848e18bdd02c3743d1314
Autor:
Sarah A. Mosure, Paola Munoz-Tello, Kuang-Ting Kuo, Brian MacTavish, Xiaoyu Yu, Daniel Scholl, Christopher C. Williams, Timothy S. Strutzenberg, Jared Bass, Richard Brust, Ashok A. Deniz, Patrick R. Griffin, Douglas J. Kojetin
PPARγ is a nuclear receptor transcription factor that regulates adipogenic and insulin sensitizing gene programs via two activation function (AF) regulatory domains: a ligand-dependent AF-2 coregulator interaction surface within the C-terminal ligan
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d1391d8be19b46ea8fd2251bbc5a88fd
https://doi.org/10.1101/2022.07.13.499031
https://doi.org/10.1101/2022.07.13.499031
Autor:
Stefano Forli, Richard Brust, Jerome Eberhardt, Jinsai Shang, Jie Zheng, Patrick R. Griffin, Sarah A. Mosure, Douglas J. Kojetin
Publikováno v:
Journal of Medicinal Chemistry. 62:2008-2023
Pioglitazone (Pio) is a Food and Drug Administration-approved drug for type-2 diabetes that binds and activates the nuclear receptor peroxisome proliferator-activated receptor γ (PPARγ), yet it remains unclear how in vivo Pio metabolites affect PPA
Autor:
Jared Bass, Jinsai Shang, Jie Zheng, Laura A. Solt, Patrick R. Griffin, Richard Brust, Douglas J. Kojetin, Sarah A. Mosure, Ashley Nichols
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-14 (2020)
Nature Communications
Nature Communications
Nuclear receptor (NR) transcription factors use a conserved activation function-2 (AF-2) helix 12 mechanism for agonist-induced coactivator interaction and NR transcriptional activation. In contrast, ligand-induced corepressor-dependent NR repression
Autor:
Alice Asteian, Jakob Fuhrmann, Richard Brust, Hua Lin, Douglas J. Kojetin, Theodore M. Kamenecka
Publikováno v:
ACS Chemical Biology. 12:969-978
GW9662 and T0070907 are widely used commercially available irreversible antagonists of peroxisome proliferator-activated receptor gamma (PPARγ). These antagonists covalently modify Cys285 located in an orthosteric ligand-binding pocket embedded in t
Publikováno v:
The FASEB Journal. 33
Autor:
Travis S. Hughes, Miru Tang, Qingfeng Ge, Theodore M Kamenekca, Paola Munoz-Tello, Jared Bass, Douglas J. Kojetin, Richard Brust, Hua Lin, Jinsai Shang, Sarah A. Mosure
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9f72f591dab4f8e1094100f37265f6db
https://doi.org/10.7554/elife.43320.077
https://doi.org/10.7554/elife.43320.077
Autor:
Ian M. Chrisman, Jakob Fuhrmann, Travis S. Hughes, Zahra Heidari, Richard Brust, Andrew Cano, Sarah A. Mosure, Anne-Laure Blayo, Jinsai Shang, Theodore M. Kamenecka, Michelle D. Nemetchek, Patrick R. Griffin, Jared Bass, Douglas J. Kojetin
Publikováno v:
Nature Communications
Nature Communications, Vol 9, Iss 1, Pp 1-14 (2018)
Nature Communications, Vol 9, Iss 1, Pp 1-14 (2018)
Small chemical modifications can have significant effects on ligand efficacy and receptor activity, but the underlying structural mechanisms can be difficult to predict from static crystal structures alone. Here we show how a simple phenyl-to-pyridyl