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10.1074/jbc.M117.777839 http://scihub22266oqcxt.onion/10.1074/jbc.M117.777839 C5535044!5535044!28623233     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 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 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       J+Biol+Chem 2017 ; 292 (30): 12713-24 Nephropedia Template TP {{tp|p=28623233|t=2017. Structural and functional analyses of pyroglutamate-amyloid-?-specific antibodies as a basis for Alzheimer immunotherapy |pdf=|usr=}}{{28623233}} gab.com Text Structural and functional analyses of pyroglutamate-amyloid- -specific antibodies as a basis for Alzheimer immunotherapy JO: J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=28623233 #FOAvip Alzheimer disease is associated with deposition of the amyloidogenic peptide A? in the brain. Passive immunization using A?-specific antibodies has been demonstrated to reduce amyloid deposition both in vitro and in vivo. Because N-terminally truncated pyroglutamate (pE)-modified A? species (A?pE3) exhibit enhanced aggregation potential and propensity to form toxic oligomers, they represent particularly attractive targets for antibody therapy. Here we present three separate monoclonal antibodies that specifically recognize A?pE3 with affinities of 1?10 nm and inhibit A?pE3 fibril formation in vitro. In vivo application of one of these resulted in improved memory in A?pE3 oligomer-treated mice. Crystal structures of Fab-A?pE3 complexes revealed two distinct binding modes for the peptide. Juxtaposition of pyroglutamate pE3 and the F4 side chain (the ?pEF head?) confers a pronounced bulky hydrophobic nature to the A?pE3 N terminus that might explain the enhanced aggregation properties of the modified peptide. The deep burial of the pEF head by two of the antibodies explains their high target specificity and low cross-reactivity, making them promising candidates for the development of clinical antibodies. Twit Text FOAVip Structural and functional analyses of pyroglutamate-amyloid- -specific antibodies as a basis for Alzheimer immunotherapy ????J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=28623233 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28623233 #FOAvip English Wikipedia <ref>{{Cite pmid|28623233}}</ref> Structural and functional analyses of pyroglutamate-amyloid-?-specific antibodies as a basis for Alzheimer immunotherapy #MMPMID28623233 Piechotta A; Parthier C; Kleinschmidt M; Gnoth K; Pillot T; Lues I; Demuth HU; Schilling S; Rahfeld JU; Stubbs MT J Biol Chem 2017[Jul]; 292 (30): 12713-24 PMID28623233show ga Alzheimer disease is associated with deposition of the amyloidogenic peptide A? in the brain. Passive immunization using A?-specific antibodies has been demonstrated to reduce amyloid deposition both in vitro and in vivo. Because N-terminally truncated pyroglutamate (pE)-modified A? species (A?pE3) exhibit enhanced aggregation potential and propensity to form toxic oligomers, they represent particularly attractive targets for antibody therapy. Here we present three separate monoclonal antibodies that specifically recognize A?pE3 with affinities of 1?10 nm and inhibit A?pE3 fibril formation in vitro. In vivo application of one of these resulted in improved memory in A?pE3 oligomer-treated mice. Crystal structures of Fab-A?pE3 complexes revealed two distinct binding modes for the peptide. Juxtaposition of pyroglutamate pE3 and the F4 side chain (the ?pEF head?) confers a pronounced bulky hydrophobic nature to the A?pE3 N terminus that might explain the enhanced aggregation properties of the modified peptide. The deep burial of the pEF head by two of the antibodies explains their high target specificity and low cross-reactivity, making them promising candidates for the development of clinical antibodies. äStructural and functional analyses of pyroglutamate-amyloid-?-specific(epmc).pdf DeepDyve Pubget Overpricing