Zobrazeno 1 - 10
of 16
pro vyhledávání: '"Morgane Callon"'
Autor:
Lauriane Lecoq, Louis Brigandat, Rebecca Huber, Marie-Laure Fogeron, Shishan Wang, Marie Dujardin, Mathilde Briday, Thomas Wiegand, Morgane Callon, Alexander Malär, David Durantel, Dara Burdette, Jan Martin Berke, Beat H. Meier, Michael Nassal, Anja Böckmann
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-14 (2023)
Hepatitis B virus (HBV) capsid assembly modulators (CAM) represent a recent class of anti-HBV antivirals. Structural approaches provide limited conformational information on the CAM-induced off-path assemblies. Here, authors use solid-state NMR to es
Externí odkaz:
https://doaj.org/article/f91900044dae4b51a0f7e494c6893cce
Autor:
Alexander A. Malär, Morgane Callon, Albert A. Smith, Shishan Wang, Lauriane Lecoq, Carolina Pérez-Segura, Jodi A. Hadden-Perilla, Anja Böckmann, Beat H. Meier
Publikováno v:
Frontiers in Molecular Biosciences, Vol 8 (2022)
Protein plasticity and dynamics are important aspects of their function. Here we use solid-state NMR to experimentally characterize the dynamics of the 3.5 MDa hepatitis B virus (HBV) capsid, assembled from 240 copies of the Cp149 core protein. We me
Externí odkaz:
https://doaj.org/article/045695b8c91b412abf8c30d4732030fd
Autor:
Lauriane Lecoq, Maarten Schledorn, Shishan Wang, Susanne Smith-Penzel, Alexander A. Malär, Morgane Callon, Michael Nassal, Beat H. Meier, Anja Böckmann
Publikováno v:
Frontiers in Molecular Biosciences, Vol 6 (2019)
We sequentially assigned the fully-protonated capsids made from core proteins of the Hepatitis B virus using proton detection at 100 kHz magic-angle spinning (MAS) in 0.7 mm rotors and compare sensitivity and assignment completeness to previously obt
Externí odkaz:
https://doaj.org/article/71b16c6dac574f3db8ac6f6dac83d843
Autor:
Thomas Wiegand, Anja Böckmann, Alexander A. Malär, Anahit Torosyan, Václav Římal, Beat H. Meier, Morgane Callon, Riccardo Cadalbert, Matthias Ernst
Publikováno v:
Magnetic Resonance, Vol 3, Pp 15-26 (2022)
Magnetic Resonance, 3 (1)
Magnetic resonance : MR 3(1), 15-26 (2022). doi:10.5194/mr-3-15-2022
Magnetic Resonance, 3 (1)
Magnetic resonance : MR 3(1), 15-26 (2022). doi:10.5194/mr-3-15-2022
With the advent of faster magic-angle spinning (MAS) and higher magnetic fields, the resolution of biomolecular solid-state nuclear magnetic resonance (NMR) spectra has been continuously increasing. As a direct consequence, the always narrower spectr
Autor:
Lauriane Lecoq, Louis Brigandat, Rebecca Huber, Marie-Laure Fogeron, Shishan Wang, Marie Dujardin, Mathilde Briday, Thomas Wiegand, Morgane Callon, Alexander Malär, David Durantel, Dara Burdette, Jan Martin Berke, Beat H. Meier, Michael Nassal, Anja Böckmann
Publikováno v:
Nature Communications, 14 (1)
Hepatitis B virus (HBV) capsid assembly modulators (CAMs) represent a recent class of anti-HBV antivirals. CAMs disturb proper nucleocapsid assembly, by inducing formation of either aberrant assemblies (CAM-A) or of apparently normal but genome-less
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ebbd116831a9401bf67b6009921d9fca
https://doi.org/10.1101/2022.09.14.507909
https://doi.org/10.1101/2022.09.14.507909
Autor:
Morgane Callon, Alexander A. Malär, Lauriane Lecoq, Marie Dujardin, Marie‐Laure Fogeron, Shishan Wang, Maarten Schledorn, Thomas Bauer, Michael Nassal, Anja Böckmann, Beat H. Meier
Publikováno v:
Angewandte Chemie. 134
Experimentally determined protein structures often feature missing domains. One example is the C-terminal domain (CTD) of the hepatitis B virus capsid protein, a functionally central part of this assembly, crucial in regulating nucleic-acid interacti
Autor:
Morgane Callon, Alexander A Malär, Lauriane Lecoq, Marie Dujardin, Marie-Laure Fogeron, Shishan Wang, Maarten Schledorn, Thomas Bauer, Michael Nassal, Anja Böckmann, Beat H Meier
Experimentally determined protein structures often feature missing domains. One example is the C terminal domain (CTD) of the hepatitis B virus capsid protein, a functionally central part of this assembly, crucial in regulated nucleic-acid interactio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::dad41305e2d42d055d4459d2c267b159
https://doi.org/10.26434/chemrxiv-2022-lr0q1
https://doi.org/10.26434/chemrxiv-2022-lr0q1
Autor:
Václav Římal, Morgane Callon, Alexander A. Malär, Riccardo Cadalbert, Anahit Torosyan, Thomas Wiegand, Matthias Ernst, Anja Böckmann, Beat H. Meier
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::fea5bcd2ffe42cec27d8ceb3a9c2107a
https://doi.org/10.5194/mr-2021-64-supplement
https://doi.org/10.5194/mr-2021-64-supplement
Autor:
Marie-Laure Fogeron, Stefanie Jonas, Rajdeep Deb, Anja Böckmann, Dawid Zyla, Václav Rímal, Beat H. Meier, Matías Chávez, Rudolf Glockshuber, Marco E. Weber, Matthias Ernst, Johannes Zehnder, Andreas Hunkeler, Anahit Torosyan, Lauriane Lecoq, Michael Nassal, Alexander Däpp, Thomas Wiegand, Sara Pfister, Alexander A. Malär, Morgane Callon, Riccardo Cadalbert
Progress in NMR in general and in biomolecular applications in particular is driven by increasing magnetic-field strengths leading to improved resolution and sensitivity of the NMR spectra. Recently, persistent superconducting magnets at a magnetic f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8664f57bf7ed65dd4ced762983b325ed
https://doi.org/10.1101/2021.03.31.437892
https://doi.org/10.1101/2021.03.31.437892
Autor:
Anja Böckmann, Lauriane Lecoq, Riccardo Cadalbert, Andreas Hunkeler, Morgane Callon, Matías Chávez, Matthias Ernst, Beat H. Meier, Marco E. Weber, Thomas Wiegand, Alexander A. Malär, Marie-Laure Fogeron, Dawid Zyla, Michael Nassal, Alexander Däpp, Rajdeep Deb, Stefanie Jonas, Rudolf Glockshuber, Johannes Zehnder, Anahit Torosyan, Sara Pfister, Václav Římal
Publikováno v:
Journal of biomolecular NMR 75(6/7), 255-272 (2021). doi:10.1007/s10858-021-00373-x
Journal of Biomolecular NMR, 75 (6)
Journal of Biomolecular NMR
Journal of Biomolecular NMR, Springer Verlag, 2021, 75, pp.255-272. ⟨10.1007/s10858-021-00373-x⟩
Journal of Biomolecular Nmr
Journal of Biomolecular NMR, Springer Verlag, 2021, 75 (6-7), pp.255-272. ⟨10.1007/s10858-021-00373-x⟩
Journal of biomolecular NMR
Journal of Biomolecular NMR, 75 (6)
Journal of Biomolecular NMR
Journal of Biomolecular NMR, Springer Verlag, 2021, 75, pp.255-272. ⟨10.1007/s10858-021-00373-x⟩
Journal of Biomolecular Nmr
Journal of Biomolecular NMR, Springer Verlag, 2021, 75 (6-7), pp.255-272. ⟨10.1007/s10858-021-00373-x⟩
Journal of biomolecular NMR
Journal of biomolecular NMR 75(6/7), 255-272 (2021). doi:10.1007/s10858-021-00373-x
Published by Springer Science + Business Media B.V, Dordrecht [u.a.]
Published by Springer Science + Business Media B.V, Dordrecht [u.a.]
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::67d9ceebb70648ca080d4b72a4af90bf