Mario A. Moscarello mostly deals with Myelin basic protein, Biochemistry, Myelin, Citrullination and Multiple sclerosis. His biological study spans a wide range of topics, including Arginine, Protein-arginine deiminase, Citrulline and Gene isoform. The study incorporates disciplines such as Biophysics, Stereochemistry, Chromatography and Isolation in addition to Biochemistry.
His Myelin research includes elements of Cystine, Protein citrullination, Pathology, Molecular biology and Cell biology. His study looks at the relationship between Citrullination and topics such as Immunogold labelling, which overlap with Protein-Arginine Deiminases and Antigen. His Multiple sclerosis research is multidisciplinary, incorporating elements of Genetically modified mouse and Phosphorylation.
His primary scientific interests are in Biochemistry, Myelin basic protein, Myelin, Multiple sclerosis and Vesicle. His studies deal with areas such as Molecular biology and Citrullination, Arginine, Citrulline as well as Myelin basic protein. He interconnects Immunogold labelling and Cathepsin D in the investigation of issues within Citrullination.
His Myelin research includes themes of Sphingomyelin, Protein citrullination and Gene isoform. The Multiple sclerosis study combines topics in areas such as Genetically modified mouse and Pathogenesis, Pathology. His Vesicle study incorporates themes from Phospholipid, Phosphatidylserine, Phosphatidylcholine, Synthetic membrane and Bilayer.
Mario A. Moscarello spends much of his time researching Myelin basic protein, Myelin, Biochemistry, Multiple sclerosis and Citrullination. The concepts of his Myelin basic protein study are interwoven with issues in Arginine, Citrulline, Molecular biology, Protein structure and Gene isoform. His work carried out in the field of Myelin brings together such families of science as Pathology and Cell biology.
His Cell biology study combines topics in areas such as Membrane and Lipid bilayer. He has included themes like Genetically modified mouse, Remyelination and Pathogenesis in his Multiple sclerosis study. His studies in Citrullination integrate themes in fields like Biophysics, Lipid monolayer and Cathepsin D.
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Effects of proteins on the thermotropic phase transitions of phospholipid membranes
D. Papahadjopoulos;M. Moscarello;E.H. Eylar;T. Isac.
Biochimica et Biophysica Acta (1975)
Myelin in multiple sclerosis is developmentally immature.
M A Moscarello;D D Wood;C Ackerley;C Boulias.
Journal of Clinical Investigation (1994)
Acute multiple sclerosis (Marburg type) is associated with developmentally immature myelin basic protein.
D. D. Wood;M. A. Moscarello;J. M. Bilbao;P. O'Connors.
Annals of Neurology (1996)
Increased Citrullination of Histone H3 in Multiple Sclerosis Brain and Animal Models of Demyelination: A Role for Tumor Necrosis Factor-Induced Peptidylarginine Deiminase 4 Translocation
Fabrizio G. Mastronardi;D. Denise Wood;Jiang Mei;Reinout Raijmakers.
The Journal of Neuroscience (2006)
The role of citrullinated proteins suggests a novel mechanism in the pathogenesis of multiple sclerosis.
Mario A. Moscarello;Fabrizio G. Mastronardi;D. Denise Wood.
Neurochemical Research (2007)
Multiple Sclerosis An Important Role for Post-Translational Modifications of Myelin Basic Protein in Pathogenesis
J. K. Kim;F. G. Mastronardi;D. D. Wood;D. M. Lubman.
Molecular & Cellular Proteomics (2003)
The isolation, characterization, and lipid-aggregating properties of a citrulline containing myelin basic protein.
D D Wood;M A Moscarello.
Journal of Biological Chemistry (1989)
Deimination of myelin basic protein. 1. Effect of deimination of arginyl residues of myelin basic protein on its structure and susceptibility to digestion by cathepsin D.
Laura B. Pritzker;Shashikant Joshi;Jessica J. Gowan;George Harauz.
Biochemistry (2000)
Peptidyl argininedeiminase 2 CpG island in multiple sclerosis white matter is hypomethylated.
Fabrizio G. Mastronardi;Abdul Noor;Abdul Noor;D. Denise Wood;Tara Paton.
Journal of Neuroscience Research (2007)
Enzymic methods for the micro assay of D-mannose, D-glucose, D-galactose, and L-fucose from acid hydrolyzates of glycoproteins
P.R. Finch;R. Yuen;H. Schachter;M.A. Moscarello.
Analytical Biochemistry (1969)
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