Zobrazeno 1 - 10
of 15
pro vyhledávání: '"Andrée E. Gravel"'
Autor:
Philip Wiredu Addo, Philip Ossowski, Sarah MacPherson, Andrée E. Gravel, Rajvinder Kaur, Valerio Hoyos-Villegas, Jaswinder Singh, Valérie Orsat, Marie-Josée Dumont, Mark Lefsrud
Publikováno v:
Molecules, Vol 27, Iss 5, p 1642 (2022)
Pisum sativum is a leguminous crop suitable for cultivation worldwide. It is used as a forage or dried seed supplement in animal feed and, more recently, as a potential non-traditional oilseed. This study aimed to develop a low-cost, rapid, and non-d
Externí odkaz:
https://doaj.org/article/1a1a5998fe9d43f480922bf85684b8c8
Autor:
Dror E. Warschawski, Alexandre A. Arnold, Matthieu Fillion, Isabelle Marcotte, Michèle Auger, Andrée E. Gravel
Publikováno v:
Biochimica et Biophysica Acta:Biomembranes
Biochimica et Biophysica Acta:Biomembranes, Elsevier, 2020, 1862 (10), pp.183379. ⟨10.1016/j.bbamem.2020.183379⟩
Biochimica et Biophysica Acta:Biomembranes, Elsevier, 2020, 1862 (10), pp.183379. ⟨10.1016/j.bbamem.2020.183379⟩
International audience; We present a new membrane mimetic system using a membrane softening detergent commonly known as Tween 80 (TW80), to form oriented systems for solid-state NMR applications. TW80 is a fatty acid ester (oleate) of sorbitan polyet
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3699c74f93929ec10840dc406bc55617
https://hal.archives-ouvertes.fr/hal-02861563
https://hal.archives-ouvertes.fr/hal-02861563
Autor:
Michèle Auger, Alexandre A. Arnold, Matthieu Fillion, Dror E. Warschawski, Isabelle Marcotte, Andrée E. Gravel
Publikováno v:
Biophysical Journal. 120:140a-141a
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. 1858:2959-2964
Nuclear magnetic resonance (NMR) is commonly used to probe the effect of antimicrobial agents on bacterial membranes using model membrane systems. Ideally, considering the complexity of membranes, the interaction of molecules with membranes should be
Autor:
Alexandre A. Arnold, Isabelle Marcotte, Chai Ann Ng, Matthew D. Perry, Jamie I. Vandenberg, Andrée E. Gravel
Slow deactivation of Kv11.1 channels is critical for its function in the heart. The S4-S5 linker, which joins the voltage sensor and pore domains, plays a critical role in this slow deactivation gating. Here, we use NMR spectroscopy to identify the m
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d1328d5a1bdce78764a7fa09f0954d72
https://europepmc.org/articles/PMC5016128/
https://europepmc.org/articles/PMC5016128/
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. 1798:1651-1662
The human ether-à-go-go related gene (hERG) potassium channels are located in the myocardium cell membrane where they ensure normal cardiac activity. The binding of drugs to this channel, a side effect known as drug-induced (acquired) long QT syndro
Publikováno v:
Biophysical Journal. 114:95a
Publikováno v:
Biophysical Journal. 112:23a
Antimicrobial peptides (AMPs) are promising candidates to act against drug-resistant bacteria since they can disrupt the bacterial lipid barrier, leading to cell death. 2H solid-state NMR is a valuable tool to study at a molecular level the action of
Publikováno v:
Biochimica et Biophysica Acta:Biomembranes
Biochimica et Biophysica Acta:Biomembranes, Elsevier, 2013, 1828 (6), pp.1494-1502. ⟨10.1016/j.bbamem.2013.02.012⟩
Biochimica et Biophysica Acta:Biomembranes, Elsevier, 2013, 1828 (6), pp.1494-1502. ⟨10.1016/j.bbamem.2013.02.012⟩
The human ether-a-go-go-related gene (hERG) voltage-gated K(+) channels are located in heart cell membranes and hold a unique selectivity filter (SF) amino acid sequence (SVGFG) as compared to other K(+) channels (TVGYG). The hERG provokes the acquir
Autor:
Alexandre A. Arnold, Étienne Chartrand, Andrée E. Gravel, Maïwenn Beaugrand, Dror E. Warschawski, Isabelle Marcotte
Publikováno v:
Biochimica et Biophysica Acta:Biomembranes
Biochimica et Biophysica Acta:Biomembranes, Elsevier, 2011, 1808 (8), pp.1957-1974. ⟨10.1016/j.bbamem.2011.03.016⟩
Biochimica et Biophysica Acta:Biomembranes, Elsevier, 2011, 1808 (8), pp.1957-1974. ⟨10.1016/j.bbamem.2011.03.016⟩
The native environment of membrane proteins is complex and scientists have felt the need to simplify it to reduce the number of varying parameters. However, experimental problems can also arise from oversimplification which contributes to why membran
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0cd52181202278863110d597949ed817
https://hal.archives-ouvertes.fr/hal-02567622
https://hal.archives-ouvertes.fr/hal-02567622