Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Marion Sevajol"'
Autor:
Rida Awad, Marion Sévajol, Isabel Ayala, Anne Chouquet, Philippe Frachet, Pierre Gans, Jean-Baptiste Reiser, Jean-Philippe Kleman
Publikováno v:
FEBS Open Bio, Vol 5, Iss 1, Pp 99-106 (2015)
Eukaryotic EnguLfment and cell MOtility (ELMO) proteins form an evolutionary conserved family of regulators involved in small GTPase dependent actin remodeling processes that regulates the guanine exchange factor activity of some of the Downstream Of
Externí odkaz:
https://doaj.org/article/6c904176dc4841e890c5d8273930a7ba
Publikováno v:
Virus Research
Virus Research, 2014, 194, pp.90-99. ⟨10.1016/j.virusres.2014.10.008⟩
Virus Research, 2014, 194, pp.90-99. ⟨10.1016/j.virusres.2014.10.008⟩
Highlights • This review summarizes coronavirus RNA biochemistry mechanisms. • A processivity factor for the viral RNA-dependent RNA polymerase. • RNA proofreading through a viral 3′–5′ exonuclease. • Viral capping regulator factors.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e515c7aa187be15b83f95e871bbc6034
https://doi.org/10.1016/j.virusres.2014.10.008
https://doi.org/10.1016/j.virusres.2014.10.008
Autor:
David Blocquel, François Ferron, Johnny Habchi, Marion Sevajol, Eric Durand, Nicolas Papageorgiou, Sonia Longhi, Jenny Erales
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 70:1589-1603
The structures of two constructs of themeasles virus(MeV) phosphoprotein (P) multimerization domain (PMD) are reported and are compared with a third structure published recently by another group [Communieet al.(2013),J. Virol.87, 7166–7169]. Althou
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::67da2a133623478725b0c54ac92f7c2d
https://doi.org/10.1107/s139900471400234x
https://doi.org/10.1107/s139900471400234x
Autor:
Bruno Canard, Bruno Coutard, Nicolas Papageorgiou, Julie Lichière, Amal Baklouti, Marion Sevajol, François Ferron
Publikováno v:
Acta crystallographica. Section D, Structural biology
Acta crystallographica. Section D, Structural biology, International Union of Crystallography, 2016, 72 (2), pp.192-202. ⟨10.1107/S2059798315024328⟩
Acta crystallographica Section D : Structural biology [1993-...]
Acta crystallographica Section D : Structural biology [1993-..], 2016, 72 (2), pp.192-202. ⟨10.1107/S2059798315024328⟩
Acta Crystallographica. Section D, Structural Biology
Acta crystallographica. Section D, Structural biology, International Union of Crystallography, 2016, 72 (2), pp.192-202. ⟨10.1107/S2059798315024328⟩
Acta crystallographica Section D : Structural biology [1993-...]
Acta crystallographica Section D : Structural biology [1993-..], 2016, 72 (2), pp.192-202. ⟨10.1107/S2059798315024328⟩
Acta Crystallographica. Section D, Structural Biology
The N protein of coronaviruses is a multifunctional protein that is organized into several domains. The N‐terminal part is composed of an intrinsically disordered region (IDR) followed by a structured domain called the N‐terminal domain (NTD). In
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::463f49d834e1ebef00543bf4ab2ba4b0
https://hal.archives-ouvertes.fr/hal-01439080
https://hal.archives-ouvertes.fr/hal-01439080
Autor:
David Blocquel, Nicolas Papageorgiou, Eric Durand, Marion Sevajol, François Ferron, Johnny Habchi, Jenny Erales, Sonia Longhi
Publikováno v:
Acta Crystallographica Section A Foundations and Advances. 70:C1599-C1599
The structural characterization of various constructs of the Measles virus (MeV) Phosphoprotein (P) multimerization domain (PMD) has brought to light significant discrepancies in the quaternary structure due to both crystal constraints and the flexib
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5a3b3e5df15cabd3aa66ab40ceaddfa8
https://doi.org/10.1107/s2053273314084009
https://doi.org/10.1107/s2053273314084009