Zobrazeno 1 - 10 of 24 pro vyhledávání: '"Angélique Chéron"'
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Akademický článek
Microsatellite Analysis Using a Two-Step Procedure for Fluorescence Labeling of PCR Products
Autor: Sophie Jouquand, Angélique Chéron, Francis Galibert
Publikováno v: BioTechniques, Vol 26, Iss 5, Pp 902-905 (1999)
A method for fluorescent labeling of PCR products has been developed. This method consists in a two-step procedure in which a first exponential classical PCR is followed by a “linear amplification”. This second step relies on incorporation of flu
Externí odkaz: https://doaj.org/article/e2d8cf4e556947f99d13be30d002f54c
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2
The LC3B FRET biosensor monitors the modes of action of ATG4B during autophagy in living cells
Autor: Elif Begüm Gökerküçük, Angélique Chéron, Marc Tramier, Giulia Bertolin
Publikováno v: Autophagy
Autophagy, In press, pp.1-21. ⟨10.1080/15548627.2023.2179845⟩
Although several mechanisms of autophagy have been dissected in the last decade, following this pathway in real time remains challenging. Among the early events leading to its activation, the ATG4B protease primes the key autophagy player LC3B. Given
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::25e27eabd1715febf13608222686c560
https://doi.org/10.1080/15548627.2023.2179845
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3
Fine mapping of hydrophobic contacts reassesses the organization of the first three dystrophin coiled-coil repeats
Autor: Olivier Delalande, Jean-François Hubert, Angélique Chéron, Dominique Mias-Lucquin, Elisabeth Le Rumeur
Publikováno v: Protein Science. 28:561-570
Coiled-coil domain is a structural motif found in proteins crucial for achievement of central biological processes, such as cellular cohesion or neuro-transmission. The coiled-coil fold consists of alpha-helices bundle that can be repeated to form la
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::f594ba69fe34c8bc35a9a3891a9df489
https://doi.org/10.1002/pro.3557
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4
Mitochondrial Aurora kinase A induces mitophagy by interacting with MAP1LC3 and Prohibitin 2
Autor: Agnès Burel, Angélique Chéron, Claude Prigent, Marie-Clotilde Alves-Guerra, Marc Tramier, Roland Le Borgne, Giulia Bertolin
Publikováno v: Life Science Alliance
Life Science Alliance, Life Science Alliance LLC, 2021, 4 (6), pp.e202000806. ⟨10.26508/lsa.202000806⟩
Life Science Alliance, 2021, 4 (6), pp.e202000806. ⟨10.26508/lsa.202000806⟩
The multifunctional Ser/Thr kinase AURKA uses the Inner Mitochondrial Membrane receptor PHB2 and MAP1LC3 as a signalling platform to orchestrate the elimination of dysfunctional mitochondria.
Epithelial and haematologic tumours often show the ov
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::83c52ff923b76bc1092ac477d2eb7011
https://pubmed.ncbi.nlm.nih.gov/33820826
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5
How the central domain of dystrophin acts to bridge F-actin to sarcolemmal lipids
Autor: Marie-Sousai Appavou, Olivier Delalande, Dominique Mias-Lucquin, Steve J. Winder, Javier Pérez, Thomas Chenuel, Angélique Chéron, Mélanie Lagarrigue, Elisabeth Le Rumeur, Raphael Dos Santos Morais, Anne L. Martel, Jean-François Hubert, Sophie Combet, Guillaume Alviset
Publikováno v: Journal of Structural Biology
Journal of Structural Biology, Elsevier, 2020, 209 (1), pp.107411. ⟨10.1016/j.jsb.2019.107411⟩
Journal of Structural Biology, 2020, 209 (1), pp.107411. ⟨10.1016/j.jsb.2019.107411⟩
'Journal of Structural Biology ', vol: 209, pages: 107411-1-107411-12 (2020)
Journal of structural biology 209, 107411-(2020). doi:10.1016/j.jsb.2019.107411
International audience; Dystrophin is a large intracellular protein that prevents sarcolemmal ruptures by providing a mechanical link between the intracellular actin cytoskeleton and the transmembrane dystroglycan complex. Dystrophin deficiency leads
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::757bc5d94ee51647f86661ed8a2b8081
https://pubmed.ncbi.nlm.nih.gov/31689503
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6
Dystrophin's central domain forms a complex filament that becomes disorganized by in-frame deletions
Autor: Olivier Delalande, Angélique Chéron, Céline Raguénès-Nicol, Mirjam Czjzek, Arnaud Bondon, Christophe Tascon, Jean-François Hubert, Nicolas Ferey, Elisabeth Le Rumeur, Emmanuel Giudice, Aurélie Nicolas, Émeline Pollet, Marc Baaden, Javier Pérez, Raphael Dos Santos Morais, Marine Guilbaud, Pierre Roblin, Anne-Elisabeth Molza
Publikováno v: Journal of Biological Chemistry
Journal of Biological Chemistry, 2018, 293 (18), pp.6637-6646. ⟨10.1074/jbc.M117.809798⟩
BASE-Bielefeld Academic Search Engine
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2018, 293 (18), pp.6637-6646. ⟨10.1074/jbc.M117.809798⟩
Journal of Biological Chemistry 18 (293), 6637-6646. (2018)
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2018, 293 (18), pp.6637-6646. ⟨10.1074/jbc.m117.809798⟩
International audience; Dystrophin, encoded by the DMD gene, is critical for maintaining plasma membrane integrity during muscle contraction events. Mutations in the DMD gene disrupting the reading frame prevent dystrophin production and result in se
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f9ccc3e07c52f1fe9cdf14f6f392151d
https://univ-rennes.hal.science/hal-01795395v2/document
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7
Human Dystrophin Structural Changes upon Binding to Anionic Membrane Lipids
Autor: Mélanie Lagarrigue, Olivier Delalande, Thomas Chenuel, Raphael Dos Santos Morais, Sophie Combet, Elisabeth Le Rumeur, Jean-François Hubert, Anne-Elisabeth Molza, Dominique Mias-Lucquin, Angélique Chéron, Céline Raguénès-Nicol, Arnaud Bondon, Anne L. Martel, Marie-Sousai Appavou, Javier Pérez
Publikováno v: Biophysical Journal
Biophysical Journal, Biophysical Society, 2018, 115 (7), pp.1231-1239. ⟨10.1016/j.bpj.2018.07.039⟩
Biophysical Journal, 2018, 115 (7), pp.1231-1239. ⟨10.1016/j.bpj.2018.07.039⟩
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International audience; Scaffolding proteins play important roles in supporting the plasma membrane (sarcolemma) of muscle cells. Among them, dystrophin strengthens the sarcolemma through protein-lipid interactions, and its absence due to gene mutati
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::53e5f81f06011530b53f3c5717f6bb69
https://hal-univ-rennes1.archives-ouvertes.fr/hal-01880131
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8
Transcarboxylase mRNA: A marker which evidences P. freudenreichii survival and metabolic activity during its transit in the human gut
Autor: Christophe Hervé, Gwénaël Jan, Frédérique Barloy-Hubler, Marc Fondrevez, Angélique Chéron
Publikováno v: International Journal of Food Microbiology
International Journal of Food Microbiology, Elsevier, 2007, 113 (3), pp.303-314. ⟨10.1016/j.ijfoodmicro.2006.08.013⟩
International Journal of Food Microbiology, 2007, 113 (3), pp.303-314. ⟨10.1016/j.ijfoodmicro.2006.08.013⟩
Dairy propionibacteria have recently been considered as probiotics which may beneficially modulate the intestinal ecosystem. However, appropriate vectors (food matrices containing the probiotic) which preserve their viability and offer good tolerance
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::421d73f0c416e111a7b03e9fa6ef3580
https://doi.org/10.1016/j.ijfoodmicro.2006.08.013
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9
Becker muscular dystrophy severity is linked to the structure of dystrophin
Autor: Aurélie Nicolas, Céline Raguénès-Nicol, Rabah Ben Yaou, Sarah Ameziane-Le Hir, Angélique Chéron, Véronique Vié, Mireille Claustres, France Leturcq, Olivier Delalande, Jean-François Hubert, Sylvie Tuffery-Giraud, Emmanuel Giudice, Elisabeth Le Rumeur
Publikováno v: Human Molecular Genetics
Human Molecular Genetics, 2015, 24 (5), pp.1267-79. ⟨10.1093/hmg/ddu537⟩
Human Molecular Genetics, Oxford University Press (OUP), 2015, 24 (5), pp.1267-79. ⟨10.1093/hmg/ddu537⟩
International audience; In-frame exon deletions of the Duchenne muscular dystrophy (DMD) gene produce internally truncated proteins that typically lead to Becker muscular dystrophy (BMD), a milder allelic disorder of DMD. We hypothesized that differe
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::147f56bd3cb6ecdce3a9af5d9bcddf82
https://univ-rennes.hal.science/hal-01117005
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10
Smc01944, a secreted peroxidase induced by oxidative stresses in Sinorhizobium meliloti 1021
Autor: Francis Galibert, Adeline Hellégouarch, Angélique Chéron, Frédérique Barloy-Hubler
Publikováno v: Microbiology. 150:657-664
Sequencing of the Sinorhizobium meliloti strain 1021 genome led to the detection of 6204 open reading frames, 41 % of which have no hypothetical function. To help annotate this genome, a transcriptome analysis was carried out with a dedicated microar
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aeeab997ebff6696f0ef45792e93ecf6
https://doi.org/10.1099/mic.0.26764-0
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