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10.1074/jbc.M114.582221 http://scihub22266oqcxt.onion/10.1074/jbc.M114.582221 C4215237!4215237 !25239624     free     free     free Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 265.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 265.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\25239624 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       J+Biol+Chem 2014 ; 289 (44 ): 30578-30589 Nephropedia Template TP {{tp|p=25239624 |t=2014. Identification of a point mutation impairing the binding between aquaporin-4 and neuromyelitis optica autoantibodies |pdf=|usr=}}{{25239624 }} gab.com Text Identification of a point mutation impairing the binding between aquaporin-4 and neuromyelitis optica autoantibodies JO: J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=25239624 #FOAvip Neuromyelitis optica (NMO) is characterized by the presence of pathogenic autoantibodies (NMO-IgGs) against supra-molecular assemblies of aquaporin-4 (AQP4), known as orthogonal array of particles (OAPs). NMO-IgGs have a polyclonal origin and recognize different conformational epitopes involving extracellular AQP4 loops A, C, and E. Here we hypothesize a pivotal role for AQP4 transmembrane regions (TMs) in epitope assembly. On the basis of multialignment analysis, mutagenesis, NMO-IgG binding, and cytotoxicity assay, we have disclosed the key role of aspartate 69 (Asp(69)) of TM2 for NMO-IgG epitope assembly. Mutation of Asp(69) to histidine severely impairs NMO-IgG binding for 85.7% of the NMO patient sera analyzed here. Although Blue Native-PAGE, total internal reflection fluorescence microscopy, and water transport assays indicate that the OAP Asp(69) mutant is similar in structure and function to the wild type, molecular dynamic simulations have revealed that the D(69)H mutation has the effect of altering the structural rearrangements of extracellular loop A. In conclusion, Asp(69) is crucial for the spatial control of loop A, the particular molecular conformation of which enables the assembly of NMO-IgG epitopes. These findings provide additional clues for new strategies for NMO treatment and a wealth of information to better approach NMO pathogenesis. Twit Text FOAVip Identification of a point mutation impairing the binding between aquaporin-4 and neuromyelitis optica autoantibodies ????J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=25239624 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25239624 #FOAvip English Wikipedia <ref>{{Cite pmid|25239624 }}</ref> Identification of a point mutation impairing the binding between aquaporin-4 and neuromyelitis optica autoantibodies #MMPMID25239624 Pisani F ; Mola MG ; Simone L ; Rosito S ; Alberga D ; Mangiatordi GF ; Lattanzi G ; Nicolotti O ; Frigeri A ; Svelto M ; Nicchia GP J Biol Chem 2014[Oct]; 289 (44 ): 30578-30589 PMID25239624 show ga Neuromyelitis optica (NMO) is characterized by the presence of pathogenic autoantibodies (NMO-IgGs) against supra-molecular assemblies of aquaporin-4 (AQP4), known as orthogonal array of particles (OAPs). NMO-IgGs have a polyclonal origin and recognize different conformational epitopes involving extracellular AQP4 loops A, C, and E. Here we hypothesize a pivotal role for AQP4 transmembrane regions (TMs) in epitope assembly. On the basis of multialignment analysis, mutagenesis, NMO-IgG binding, and cytotoxicity assay, we have disclosed the key role of aspartate 69 (Asp(69)) of TM2 for NMO-IgG epitope assembly. Mutation of Asp(69) to histidine severely impairs NMO-IgG binding for 85.7% of the NMO patient sera analyzed here. Although Blue Native-PAGE, total internal reflection fluorescence microscopy, and water transport assays indicate that the OAP Asp(69) mutant is similar in structure and function to the wild type, molecular dynamic simulations have revealed that the D(69)H mutation has the effect of altering the structural rearrangements of extracellular loop A. In conclusion, Asp(69) is crucial for the spatial control of loop A, the particular molecular conformation of which enables the assembly of NMO-IgG epitopes. These findings provide additional clues for new strategies for NMO treatment and a wealth of information to better approach NMO pathogenesis. |Amino Acid Sequence [MESH] |Animals [MESH] |Aquaporin 4/chemistry/*genetics/immunology [MESH] |Autoantibodies/*metabolism [MESH] |Biological Transport [MESH] |Epitopes/genetics [MESH] |HeLa Cells [MESH] |Humans [MESH] |Hydrogen-Ion Concentration [MESH] |Immunoglobulin G/metabolism [MESH] |Molecular Dynamics Simulation [MESH] |Molecular Sequence Data [MESH] |Mutation, Missense [MESH] |Neuromyelitis Optica/blood/*immunology [MESH] |Point Mutation [MESH] |Protein Binding [MESH] |Protein Structure, Tertiary [MESH] |Water/metabolism [MESH]Identification of a point mutation impairing the binding between aquap(epmc).pdf DeepDyve Pubget Overpricing