Výsledky vyhledávání - "G. Poncet-Montange"

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Regulation of kinase activity by combined action of juxtamembrane and C-terminal regions of receptors

Autor: Stefan T. Arold, Kin Man Suen, G. Poncet-Montange, Chi-Chuan Lin, John E. Ladbury, Lukasz Wieteska, Zamal Ahmed

Despite the kinetically-favorable, ATP-rich intracellular environment, the mechanism by which receptor tyrosine kinases (RTKs) repress activation prior to extracellular stimulation is poorly understood. RTKs are activated through a precise sequence o

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::f27d1f4be57609d4e661f777b57c8d7c
https://doi.org/10.1101/2020.10.01.322123

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Prion Protein-Antibody Complexes Characterized by Chromatography-Coupled Small-Angle X-Ray Scattering

Autor: Stanley B. Prusiner, Lester G. Carter, G. Poncet-Montange, Thomas M. Weiss, Seung Joong Kim, Hiro Tsuruta, Andrej Sali, Dina Schneidman-Duhovny, Jan Stöhr

Publikováno v: Biophysical journal, vol 109, iss 4

Aberrant self-assembly, induced by structural misfolding of the prion proteins, leads to a number of neurodegenerative disorders. In particular, misfolding of the mostly α-helical cellular prion protein (PrP(C)) into a β-sheet-rich disease-causing

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::df76dbcf5c695a46b8269b081d6ed3a7
https://escholarship.org/uc/item/896342mv

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Structure-Guided Design of IACS-9571, a Selective High-Affinity Dual TRIM24-BRPF1 Bromodomain Inhibitor

Publikováno v: Palmer, W S; Poncet-Montange, G; Liu, G; Petrocchi, A; Reyna, N; Subramanian, G; et al.(2015). Structure-Guided Design of IACS-9571, a Selective High-Affinity Dual TRIM24-BRPF1 Bromodomain Inhibitor. J Med Chem. UC Office of the President: Multicampus Research Programs and Initiatives (MRPI); a funding opportunity through UC Research Initiatives (UCRI). Retrieved from: http://www.escholarship.org/uc/item/2997633w

The bromodomain containing proteins TRIM24 (tripartite motif containing protein 24) and BRPF1 (bromodomain and PHD finger containing protein 1) are involved in the epigenetic regulation of gene expression and have been implicated in human cancer. Ove

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::88d2274e44993fac4ed4392dfab37921
http://www.escholarship.org/uc/item/2997633w

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Observed bromodomain flexibility reveals histone peptide- and small molecule ligand-compatible forms of ATAD2

Autor: Gilbert R. Lee, Mario Cardozo, Xi Shi, Jennifer Bardenhagen, Philip Jones, Alessia Petrocchi, Paul G. Leonard, Wylie S. Palmer, Yanai Zhan, John E. Ladbury, G. Poncet-Montange, Mary K. Geck Do, Jannik N. Andersen, Elisabetta Leo

Publikováno v: The Biochemical journal. 466(2)

Preventing histone recognition by bromodomains emerges as an attractive therapeutic approach in cancer. Overexpression of ATAD2 (ATPase family AAA domain-containing 2 isoform A) in cancer cells is associated with poor prognosis making the bromodomain

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::26c2b89543d804087a82e5650be05e4d
https://pubmed.ncbi.nlm.nih.gov/25486442

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The Human Orphan Nuclear Receptor Tailless (TLX, NR2E1) Is Druggable

Autor: G. Poncet-Montange, Senapathy Rajagopalan, Robert J. Fletterick, Jan-Åke Gustafsson, Cindy Benod, Carly S. Filgueira, Paul Webb, Paul G. Leonard, Peter K. Hwang, Rosa Villagomez

Publikováno v: PLoS ONE
PLoS ONE, Vol 9, Iss 6, p e99440 (2014)

Nuclear receptors (NRs) are an important group of ligand-dependent transcriptional factors. Presently, no natural or synthetic ligand has been identified for a large group of orphan NRs. Small molecules to target these orphan NRs will provide unique

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::df1e75b0245911e69331e9ad6a7c4267
http://europepmc.org/articles/PMC4060991

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Oligomeric-induced activity by thienyl pyrimidine compounds traps prion infectivity

Autor: Jean-Michel Verdier, G. Poncet-Montange, Ilia V. Baskakov, Thibaut Imberdis, Karine Toupet, Adeline Ayrolles-Torro, Catherine Grégoire, Véronique Perrier, Françoise Roquet-Baneres, Joan Torrent, Sylvain Lehmann, Martine Pugnière, Didier Rognan

Publikováno v: Journal of Neuroscience
Journal of Neuroscience, Society for Neuroscience, 2011, 31 (42), pp.14882-14892. ⟨10.1523/JNEUROSCI.0547-11.2011⟩

Accumulation of PrPSc, an abnormal form of cellular prion protein (PrP), in the brain of animals and humans leads to fatal neurodegenerative disorders known as prion diseases. Limited protease digestion of PrPScproduces a truncated form called PrP(27

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::57752a35df279589e31f3fe3be03071a
https://pubmed.ncbi.nlm.nih.gov/22016521

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NAD kinases use substrate-assisted catalysis for specific recognition of NAD

Autor: Gilles Labesse, Stefan T. Arold, G. Poncet-Montange, Liliane Assairi, Sylvie Pochet

Publikováno v: Journal of Biological Chemistry
Journal of Biological Chemistry, 2007, 282 (47), pp.33925-34. ⟨10.1074/jbc.M701394200⟩
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2007, 282 (47), pp.33925-34. ⟨10.1074/jbc.M701394200⟩

International audience; Here we describe the crystal structures of the NAD kinase (LmNADK1) from Listeria monocytogenes in complex with its substrate NAD, its product NADP, or two synthesized NAD mimics. We identified one of the NAD mimics, di-adenos

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4f0934f836605fb6bfdadfc462bcb073
https://hal-pasteur.archives-ouvertes.fr/pasteur-00202295/document

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Lack of dynamics in the MabA active site kills the enzyme activity: practical consequences for drug-design studies

Autor: Annaïck Quemard, Martin Cohen-Gonsaud, Stéphanie Ducasse-Cabanot, Gilles Labesse, G. Poncet-Montange

Publikováno v: Acta crystallographica. Section D, Biological crystallography. 63(Pt 8)

The MabA protein from Mycobacterium tuberculosis is a validated drug target. Previous structural studies of this protein showed dynamic behaviour in the catalytic site and described motion between an open `active' holo form (with NADP) and a closed `

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::be61e8bf652735b222a89418442a8a3d
https://pubmed.ncbi.nlm.nih.gov/17642518

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