Structural basis of synthetic agonist activation of the nuclear receptor REV-ERB

Autor: Meghan H. Murray, Aurore Cecile Valfort, Thomas Koelblen, Céline Ronin, Fabrice Ciesielski, Arindam Chatterjee, Giri Babu Veerakanellore, Bahaa Elgendy, John K. Walker, Lamees Hegazy, Thomas P. Burris

Publikováno v: Nature Communications, Vol 13, Iss 1, Pp 1-12 (2022)

The nuclear receptor REV-ERBα is a receptor for heme and plays a role in a range of physiological processes. Here, the authors provide the first structure of REV-ERB bound to a synthetic nonporphyrin ligand defining key mechanistic differences to ho

Externí odkaz: https://doaj.org/article/e9a3baa7b5fa4017822b58a19fb7301d

Antihyperlipidemic Activity of Gut-Restricted LXR Inverse Agonists

Autor: Kristine Griffett, Matthew Hayes, Gonzalo Bedia-Diaz, Kevin Appourchaux, Ryan Sanders, Michael P. Boeckman, Thomas Koelblen, Jinsong Zhang, Ira G. Schulman, Bahaa Elgendy, Thomas P. Burris

Publikováno v: ACS Chemical Biology. 17:1143-1154

Hyperlipidemia and increased circulating cholesterol levels are associated with increased cardiovascular disease risk. The liver X receptors (LXRs) are regulators of

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1a8cf044d8bb44c68f0d4e829ef7df91
https://doi.org/10.1021/acschembio.2c00057

The Orphan Nuclear Receptor TLX Is a Receptor for Synthetic and Natural Retinoids

Autor: Lamees Hegazy, McKenna L. Wilhelm, Ian Mitchelle S. de Vera, Thomas P. Burris, Thomas Koelblen, Gonzalo Bedia-Diaz, Cyrielle Billon, Kristine Griffett, Udayanga Wanninayake

Publikováno v: Cell chemical biology. 27(10)

TLX is an orphan nuclear receptor that plays a critical role in both embryonic and adult neurogenesis, as well in the pathogenesis of glioblastomas. TLX functions predominately as a transcriptional repressor, but no natural ligands or high-affinity s

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fb376325ea365488d753abae0e08f0e0
https://pubmed.ncbi.nlm.nih.gov/32763139

The Brucella TIR domain containing proteins BtpA and BtpB have a structural WxxxE motif important for protection against microtubule depolymerisation

Autor: David O'Callaghan, Thomas Koelblen, Laurent Terradot, Annette C. Vergunst, Christine Felix, Burcu Kaplan Türköz, Sebastien Ranaldi

Publikováno v: Cell Communication and Signaling
Cell Communication and Signaling, BioMed Central, 2013, 12, pp.53
Cell Communication and Signaling, 2013, 12, pp.53
Cell Communication and Signaling : CCS

PubMed ID: 25304327
Background: The TIR domain-containing proteins BtpA/Btp1/TcpB and BtpB are translocated into host cells by the facultative intracellular bacterial pathogen Brucella. Here, they interfere with Toll like receptor signalling to

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::321ad3d22aa5efb3f223f39e9dfa181f
https://www.hal.inserm.fr/inserm-01205296/file/s12964-014-0053-y.pdf

Molecular dissection of protein-protein interactions between integrin α5β1 and the Helicobacter pylori Cag type IV secretion system.

Autor: Koelblen, Thomas¹, Bergé, Célia¹, Cherrier, Mickaël V.¹, Brillet, Karl¹, Jimenez‐Soto, Luisa², Ballut, Lionel¹, Takagi, Junichi³, Montserret, Roland¹, Rousselle, Patricia⁴, Fischer, Wolfgang², Haas, Rainer^2,5, Fronzes, Rémi⁶, Terradot, Laurent¹ laurent.terradot@ibcp.fr

Publikováno v: FEBS Journal. Dec2017, Vol. 284 Issue 23, p4143-4157. 15p.