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pro vyhledávání: '"F. Briki"'
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Autor:
Ahmet Dogan, S. Valleix, Gilles Grateau, Nathalie Rioux-Leclercq, Franck Bridoux, Renan Goude, Jean Doucet, Cyrille Garnier, F. Briki, Philippe Derreumaux, Marc Delpech, Patrick Le Pogamp, Brigitte Nedelec, Laurent Martin, Caroline Beugnet
Publikováno v:
Blood
Blood, American Society of Hematology, 2017, 130 (25), pp.2799-2807. 〈10.1182/blood-2017-07-796185〉
Blood, American Society of Hematology, 2017, 130 (25), pp.2799-2807. ⟨10.1182/blood-2017-07-796185⟩
Blood, 2017, 130 (25), pp.2799-2807. ⟨10.1182/blood-2017-07-796185⟩
Blood, American Society of Hematology, 2017, 130 (25), pp.2799-2807. 〈10.1182/blood-2017-07-796185〉
Blood, American Society of Hematology, 2017, 130 (25), pp.2799-2807. ⟨10.1182/blood-2017-07-796185⟩
Blood, 2017, 130 (25), pp.2799-2807. ⟨10.1182/blood-2017-07-796185⟩
International audience; The first case of hereditary fibrinogen A alpha-chain amyloidosis was recognized >20 years ago, but disease mechanisms still remain unknown. Here we report detailed clinical and proteomics studies of a French kindred with a no
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::78719ea460bf43d3e88b8fc9e51145d6
https://hal-univ-rennes1.archives-ouvertes.fr/hal-01688181/document
https://hal-univ-rennes1.archives-ouvertes.fr/hal-01688181/document
Autor:
Jean-François Sadoc, Laurie Gumez, Aurélien Gourrier, Chantal Pichon, Jean Doucet, F. Briki, Sabine F. Bensamoun
Publikováno v:
Journal of Structural Biology
Journal of Structural Biology, Elsevier, 2010, 173 (2), pp.197-201. ⟨10.1016/j.jsb.2010.11.018⟩
Journal of Structural Biology, Elsevier, 2010, 173 (2), pp.197-201. ⟨10.1016/j.jsb.2010.11.018⟩
International audience; A characteristic feature of the dense phases formed by fiber-shaped molecules is their organization into parallel rods packed in a hexagonal or pseudo-hexagonal lateral network. This is typically the case for the collagen trip
Publikováno v:
Journal of Structural Biology
Journal of Structural Biology, Elsevier, 2009, 170 (1), pp.69-75. ⟨10.1016/j.jsb.2009.11.006⟩
Journal of Structural Biology, Elsevier, 2009, 170 (1), pp.69-75. ⟨10.1016/j.jsb.2009.11.006⟩
International audience; X-rays interact strongly with biological organisms. Synchrotron radiation sources deliver very intense X-ray photon fluxes within micro- or submicro cross-section beams, resulting in doses larger than the MGy. The relevance of
The Intermediate Filament Architecture as Determined by X-Ray Diffraction Modeling of Hard α-Keratin
Publikováno v:
Biophysical Journal. 86(6):3893-3904
Despite investigation since the 1950s, the molecular architecture of intermediate filaments has not yet been fully elucidated. Reliable information about the longitudinal organization of the molecules within the filaments and about the lateral interf
Publikováno v:
Journal of Structural Biology. 141:132-142
The [URE3] phenotype in the yeast Saccharomyces cerevisiae is inherited by a prion mechanism involving self-propagating Ure2p aggregates. It is believed that assembly of intact Ure2p into fibrillar polymers that bind Congo Red and show yellow-green b
Autor:
Yolanda Duvault, F. Briki, Gwyn P. Williams, Jean-Luc Leveque, C. Mérigoux, Jean Doucet, Paul Dumas, Laurent Kreplak, Lisa M. Miller, Frederic Leroy, G. L. Carr
Publikováno v:
International Journal of Cosmetic Science. 23:369-374
Synopsis Synchrotron-based infrared microscopic measurements have been performed on various hair transverse sections, sampled either from the heads of Caucasian or Afro-American subjects. Lipid content of various virgin hair transverse sections was e
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1547:268-274
The cuticle of mammalian hair fibres protects the core of the fibre against physical and chemical stress. The structure and some of the properties of the cuticle have been extensively studied by electron microscopy. However, there is still a need for
Publikováno v:
Biopolymers. 58:526-533
Transformations of proteins secondary and tertiary structures are generally studied in globular proteins in solution. In fibrous proteins, such as hard alpha-keratin, that contain long and well-defined double stranded alpha-helical coiled coil domain
Autor:
Daniel Genest, F. Briki
Publikováno v:
Biophysical Chemistry. 52:35-43
We report a method for analyzing atomic correlated motions in biopolymers from trajectories obtained by molecular dynamics simulation. A correlation coefficient based on the canonical analysis of data is defined which is independent on the relative o