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Molecular Genetics and Metabolism|April 20, 2006
Structural and phylogenetic approaches to assess the significance of human Apolipoprotein E variationRosa Maria Corbo, Martine Prévost, Vincent Raussens, et al.
ACS Chemical Neuroscience|March 16, 2017
Distinct Mechanisms Determine α-Synuclein Fibril Morphology during Growth and MaturationArshdeep Sidhu, Ine Segers-Nolten, Vincent Raussens, et al.
The Biochemical Journal|February 10, 2012
Toxic prefibrillar α-synuclein amyloid oligomers adopt a distinctive antiparallel β-sheet structureMaría Soledad Celej, Rabia Sarroukh, Erik Goormaghtigh, et al.
The Journal of Biological Chemistry|July 22, 2010
Mutational and cysteine scanning analysis of the glucagon receptor N-terminal domainMartine Prévost, Pascale Vertongen, Vincent Raussens, et al.
Molecules (Basel, Switzerland)|July 1, 2020
Characterization by Nano-Infrared Spectroscopy of Individual Aggregated Species of Amyloid ProteinsJehan Waeytens, Vincent Van Hemelryck, Ariane Deniset-Besseau, et al.
Biochemistry|September 7, 2006
Calcium-triggered membrane interaction of the alpha-synuclein acidic tailShiori Tamamizu-Kato, Malathi G Kosaraju, Hiroyuki Kato, et al.
The Biochemical Journal|August 15, 2015
Amyloid fibrils are the molecular trigger of inflammation in Parkinson's diseaseAdelin Gustot, José Ignacio Gallea, Rabia Sarroukh, et al.
Biochimica Et Biophysica Acta|February 5, 2016
Structural remodeling during amyloidogenesis of physiological Nα-acetylated α-synucleinJ Ignacio Gallea, Rabia Sarroukh, Pablo Yunes-Quartino, et al.
Cellular and Molecular Life Sciences : CMLS|September 21, 2010
Transformation of amyloid β(1-40) oligomers into fibrils is characterized by a major change in secondary structureRabia Sarroukh, Emilie Cerf, Sylvie Derclaye, et al.
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