Compounds > 1-palmitoyl-2-oleoylphosphatidylcholine

1-palmitoyl-2-oleoylphosphatidylcholine and Neuromyelitis-Optica

1-palmitoyl-2-oleoylphosphatidylcholine has been researched along with Neuromyelitis-Optica* in 1 studies

Other Studies

1 other study(ies) available for 1-palmitoyl-2-oleoylphosphatidylcholine and Neuromyelitis-Optica

Article	Year
Comparative molecular dynamics study of neuromyelitis optica-immunoglobulin G binding to aquaporin-4 extracellular domains. Biochimica et biophysica acta. Biomembranes, 2017, Volume: 1859, Issue:8 Neuromyelitis optica (NMO) is an inflammatory demyelinating disease of the central nervous system in which most patients have serum autoantibodies (called NMO-IgG) that bind to astrocyte water channel aquaporin-4 (AQP4). A potential therapeutic strategy in NMO is to block the interaction of NMO-IgG with AQP4. Building on recent observation that some single-point and compound mutations of the AQP4 extracellular loop C prevent NMO-IgG binding, we carried out comparative Molecular Dynamics (MD) investigations on three AQP4 mutants, TP Topics: Amino Acid Motifs; Aquaporin 4; Autoantibodies; Binding Sites; Epitopes; Humans; Hydrogen Bonding; Immunoglobulin G; Lipid Bilayers; Models, Molecular; Molecular Dynamics Simulation; Mutation; Neuromyelitis Optica; Phosphatidylcholines; Protein Binding; Protein Conformation, alpha-Helical; Protein Interaction Domains and Motifs; Protein Multimerization; Thermodynamics	2017

Article

Year

Comparative molecular dynamics study of neuromyelitis optica-immunoglobulin G binding to aquaporin-4 extracellular domains.

Biochimica et biophysica acta. Biomembranes, 2017, Volume: 1859, Issue:8

Neuromyelitis optica (NMO) is an inflammatory demyelinating disease of the central nervous system in which most patients have serum autoantibodies (called NMO-IgG) that bind to astrocyte water channel aquaporin-4 (AQP4). A potential therapeutic strategy in NMO is to block the interaction of NMO-IgG with AQP4. Building on recent observation that some single-point and compound mutations of the AQP4 extracellular loop C prevent NMO-IgG binding, we carried out comparative Molecular Dynamics (MD) investigations on three AQP4 mutants, TP

Topics: Amino Acid Motifs; Aquaporin 4; Autoantibodies; Binding Sites; Epitopes; Humans; Hydrogen Bonding; Immunoglobulin G; Lipid Bilayers; Models, Molecular; Molecular Dynamics Simulation; Mutation; Neuromyelitis Optica; Phosphatidylcholines; Protein Binding; Protein Conformation, alpha-Helical; Protein Interaction Domains and Motifs; Protein Multimerization; Thermodynamics

2017