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of 4
pro vyhledávání: '"Justine Magnat"'
Autor:
Jody Pacalon, Guillaume Audic, Justine Magnat, Manon Philip, Jérôme Golebiowski, Christophe J. Moreau, Jérémie Topin
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-11 (2023)
Abstract In numerous insects, the olfactory receptor family forms a unique class of heteromeric cation channels. Recent progress in resolving the odorant receptor structures offers unprecedented opportunities for deciphering their molecular mechanism
Externí odkaz:
https://doaj.org/article/b16c6ce639bb4d078a61f12fc07040fb
Autor:
Jody Pacalon, Guillaume Audic, Justine Magnat, Manon Philip, Jérôme Golebiowski, Christophe J. Moreau, Jérémie Topin
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-1 (2024)
Externí odkaz:
https://doaj.org/article/a80750c91a5646799883b05b39867f03
Autor:
Jody Pacalon, Guillaume Audic, Justine Magnat, Manon Philip, Jérôme Golebiowski, Christophe J. Moreau, Jérémie Topin
In numerous insects, the olfactory receptor family forms a unique class of heteromeric cation channels. Recent progress in resolving the odorant receptor structures offers unprecedented opportunities for deciphering their molecular mechanisms of liga
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3b5fdafdba81e38b54d6a9f68c9c4328
https://doi.org/10.1101/2023.05.05.539596
https://doi.org/10.1101/2023.05.05.539596
Autor:
Anton Abyzov, Christophe Moreau, Nicola Salvi, Martin Blackledge, Wiktor Adamski, Malene Ringkjøbing Jensen, Justine Magnat, Damien Maurin, Sigrid Milles
Publikováno v:
Journal of the American Chemical Society
Journal of the American Chemical Society, American Chemical Society, 2019, 141 (44), pp.17817-17829. ⟨10.1021/jacs.9b09002⟩
Journal of the American Chemical Society, 2019, 141 (44), pp.17817-17829. ⟨10.1021/jacs.9b09002⟩
Journal of the American Chemical Society, American Chemical Society, 2019, 141 (44), pp.17817-17829. ⟨10.1021/jacs.9b09002⟩
Journal of the American Chemical Society, 2019, 141 (44), pp.17817-17829. ⟨10.1021/jacs.9b09002⟩
International audience; Intrinsically disordered proteins (IDPs) are flexible biomolecules whose essential functions are defined by their dynamic nature. Nuclear magnetic resonance (NMR) spectroscopy is ideally suited to the investigation of this beh