Zobrazeno 1 - 10
of 32
pro vyhledávání: '"Mark G.H. Scott"'
Autor:
Nawal Maïssa, Valentina Covarelli, Sébastien Janel, Beatrice Durel, Nandi Simpson, Sandra C. Bernard, Liliana Pardo-Lopez, Haniaa Bouzinba-Ségard, Camille Faure, Mark G.H. Scott, Mathieu Coureuil, Philippe C. Morand, Frank Lafont, Xavier Nassif, Stefano Marullo, Sandrine Bourdoulous
Publikováno v:
Nature Communications, Vol 8, Iss 1, Pp 1-15 (2017)
Neisseria meningitidis bacteria bind to host proteins CD147 and β2-adrenergic receptor on the surface of endothelial cells. Here, Maïssa et al. show that the two proteins interact with each other forming clusters that increase the binding strength
Externí odkaz:
https://doaj.org/article/812ccd1878054e24ab2fafea122fa20e
Publikováno v:
Oncotarget
Oncotarget, 2021, 12 (26), pp.2543-2545. ⟨10.18632/oncotarget.28065⟩
Oncotarget, 2021, ⟨10.18632/oncotarget.28065⟩
Oncotarget, 2021, 12 (26), pp.2543-2545. ⟨10.18632/oncotarget.28065⟩
Oncotarget, 2021, ⟨10.18632/oncotarget.28065⟩
International audience; No abstract available
Autor:
Stephane Angers, Kusumika Saha, Jane E. Findlay, Evelyne Lima-Fernandes, Michel Bouvier, Justine S. Paradis, Stefano Marullo, Cédric Auffray, George S. Baillie, Hervé Enslen, Mark G.H. Scott, Alessia Zamborlini, Anne Poupon, Elodie Blondel-Tepaz, Badr Sokrat, Milena Kosic, Louis Gaboury, Marie Leverve
Publikováno v:
Oncogene
Oncogene, Nature Publishing Group, 2021, 40 (12), pp.2243-2257. ⟨10.1038/s41388-021-01704-w⟩
Oncogene, 2021, 40 (12), pp.2243-2257. ⟨10.1038/s41388-021-01704-w⟩
Oncogene, Nature Publishing Group, 2021, 40 (12), pp.2243-2257. ⟨10.1038/s41388-021-01704-w⟩
Oncogene, 2021, 40 (12), pp.2243-2257. ⟨10.1038/s41388-021-01704-w⟩
International audience; Mdm2 antagonizes the tumor suppressor p53. Targeting the Mdm2-p53 interaction represents an attractive approach for the treatment of cancers with functional p53. Investigating mechanisms underlying Mdm2-p53 regulation is there
Autor:
Robyn Flynn, Daniel Young, Manon Defaye, Mircea Iftinca, Christophe Altier, Mark G.H. Scott, Nasser Abdullah, Antoine Dufour, Ahmed Hassan, Francina Agosti
Publikováno v:
International Journal of Molecular Sciences
International Journal of Molecular Sciences, MDPI, 2021, 22 (5), pp.2280. ⟨10.3390/ijms22052280⟩
International Journal of Molecular Sciences, 2021, 22 (5), pp.2280. ⟨10.3390/ijms22052280⟩
International Journal of Molecular Sciences, Vol 22, Iss 2280, p 2280 (2021)
Volume 22
Issue 5
International Journal of Molecular Sciences, MDPI, 2021, 22 (5), pp.2280. ⟨10.3390/ijms22052280⟩
International Journal of Molecular Sciences, 2021, 22 (5), pp.2280. ⟨10.3390/ijms22052280⟩
International Journal of Molecular Sciences, Vol 22, Iss 2280, p 2280 (2021)
Volume 22
Issue 5
International audience; Transient receptor potential vanilloids (TRPV1) are non-selective cation channels that sense and transduce inflammatory pain signals. We previously reported that activation of TRPV1 induced the translocation of β-arrestin2 (A
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d599e69a05565ff7c9fc6e481bd723d7
https://hal.archives-ouvertes.fr/hal-03414911/document
https://hal.archives-ouvertes.fr/hal-03414911/document
Autor:
Stefano Marullo, Aurélie Borrull, Mireille Lambert, Isaure Lot, Alexandre Beautrait, Michel Bouvier, Revu Ann Alexander, Kusumika Saha, Eleonore Decosta, Mark G.H. Scott, Atef Asnacios, Hervé Enslen, Guillaume Abadie, Hiroyuki Kobayashi
Publikováno v:
Cellular and Molecular Life Sciences
Cellular and Molecular Life Sciences, Springer Verlag, 2020, 77 (24), pp.5259-5279. ⟨10.1007/s00018-020-03471-5⟩
Cellular and Molecular Life Sciences, Springer Verlag, 2020, Epub ahead of print. ⟨10.1007/s00018-020-03471-5⟩
Cellular and Molecular Life Sciences, 2020, Epub ahead of print. ⟨10.1007/s00018-020-03471-5⟩
Cellular and Molecular Life Sciences, Springer Verlag, 2020, 77 (24), pp.5259-5279. ⟨10.1007/s00018-020-03471-5⟩
Cellular and Molecular Life Sciences, Springer Verlag, 2020, Epub ahead of print. ⟨10.1007/s00018-020-03471-5⟩
Cellular and Molecular Life Sciences, 2020, Epub ahead of print. ⟨10.1007/s00018-020-03471-5⟩
International audience; Focal adhesion kinase (FAK) regulates key biological processes downstream of G protein-coupled receptors (GPCRs) in normal and cancer cells, but the modes of kinase activation by these receptors remain unclear. We report that
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::343d1ead466b69d230fa38200280fb6a
https://hal.archives-ouvertes.fr/hal-03031947
https://hal.archives-ouvertes.fr/hal-03031947
Publikováno v:
Cold Spring Harb Perspect Med
Phosphatase and tensin homolog deleted on chromosome 10 (PTEN) is a tumor suppressor that is frequently down-modulated in human cancer. PTEN inhibits the phosphatidylinositol 3-phosphate kinase (PI3K)/AKT pathway through its lipid phosphatase activit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f22e7290ff63fb0a4090b3c712805c27
https://europepmc.org/articles/PMC7328454/
https://europepmc.org/articles/PMC7328454/
Publikováno v:
Beta-arrestins: Methods and Protocols
Beta-arrestins: Methods and Protocols, pp.251-269, 2019, ⟨10.1007/978-1-4939-9158-7_16⟩
Beta-Arrestins ISBN: 9781493991570
Beta-arrestins: Methods and Protocols, pp.251-269, 2019, ⟨10.1007/978-1-4939-9158-7_16⟩
Beta-Arrestins ISBN: 9781493991570
β-Arrestins (β-arrs) were originally appreciated for the roles they play in the desensitization and internalization of G protein-coupled receptors (GPCRs). They are also now known to act as molecular scaffolds, providing control in multiple signall
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bf8384553f11d4172440af482d6c3a94
https://hal.archives-ouvertes.fr/hal-02349003
https://hal.archives-ouvertes.fr/hal-02349003
Autor:
Frederick Charles Campbell, Arman Javadi, Mark G.H. Scott, Ravi K. Deevi, Emma Evergren, George S. Baillie, Elodie Blondel-Tepaz
Publikováno v:
eLife, Vol 6 (2017)
eLife
eLife
PTEN controls three-dimensional (3D) glandular morphogenesis by coupling juxtamembrane signaling to mitotic spindle machinery. While molecular mechanisms remain unclear, PTEN interacts through its C2 membrane-binding domain with the scaffold protein
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a05dafaf6d036388b0211d1d7da31a96
https://eprints.gla.ac.uk/144649/1/144649.pdf
https://eprints.gla.ac.uk/144649/1/144649.pdf
Autor:
Mark G.H. Scott, Stefano Marullo, Marie-Caroline Le Bousse-Kerdilès, Laetitia Boutin, Bernadette Guerton, Denis Clay, Aurélie Chabanon, Adrienne Anginot, Frédéric Torossian, Christophe Desterke, Jean-Jacques Lataillade
Publikováno v:
Blood. 123:191-202
In addition to its well-known effect on migration and homing of hematopoietic stem/progenitor cells (HSPCs), CXCL12 chemokine also exhibits a cell cycle and survival-promoting factor for human CD34(+) HSPCs. CXCR4 was suggested to be responsible for