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10.1099/vir.0.062083-0 http://scihub22266oqcxt.onion/10.1099/vir.0.062083-0 C4059271!4059271!24769839     free     free     free Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 243.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 243.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 243.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 243.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 243.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 276.79999999999995 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 276.79999999999995 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 276.79999999999995 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       J+Gen+Virol 2014 ; 95 (Pt 7): 1612-8 Nephropedia Template TP {{tp|p=24769839|t=2014. Complex proteinopathy with accumulations of prion protein, hyperphosphorylated tau, ?-synuclein and ubiquitin in experimental bovine spongiform encephalopathy of monkeys |pdf=|usr=}}{{24769839}} gab.com Text Complex proteinopathy with accumulations of prion protein, hyperphosphorylated tau, -synuclein and ubiquitin in experimental bovine spongiform encephalopathy of monkeys JO: J Gen Virol http://www.kidney.de/pget.php?&tw=1&pmid=24769839 #FOAvip Proteins aggregate in several slowly progressive neurodegenerative diseases called ?proteinopathies?. Studies with cell cultures and transgenic mice overexpressing mutated proteins suggested that aggregates of one protein induced misfolding and aggregation of other proteins as well ? a possible common mechanism for some neurodegenerative diseases. However, most proteinopathies are ?sporadic?, without gene mutation or overexpression. Thus, proteinopathies in WT animals genetically close to humans might be informative. Squirrel monkeys infected with the classical bovine spongiform encephalopathy agent developed an encephalopathy resembling variant Creutzfeldt?Jakob disease with accumulations not only of abnormal prion protein (PrPTSE), but also three other proteins: hyperphosphorylated tau (p-tau), ?-synuclein and ubiquitin; ?-amyloid protein (A?) did not accumulate. Severity of brain lesions correlated with spongiform degeneration. No amyloid was detected. These results suggested that PrPTSE enhanced formation of p-tau and aggregation of ?-synuclein and ubiquitin, but not A?, providing a new experimental model for neurodegenerative diseases associated with complex proteinopathies. Twit Text FOAVip Complex proteinopathy with accumulations of prion protein, hyperphosphorylated tau, -synuclein and ubiquitin in experimental bovine spongiform encephalopathy of monkeys ????J Gen Virol http://www.kidney.de/pget.php?&tw=1&pmid=24769839 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=24769839 #FOAvip English Wikipedia <ref>{{Cite pmid|24769839}}</ref> Complex proteinopathy with accumulations of prion protein, hyperphosphorylated tau, ?-synuclein and ubiquitin in experimental bovine spongiform encephalopathy of monkeys #MMPMID24769839 Piccardo P; Cervenak J; Bu M; Miller L; Asher DM J Gen Virol 2014[Jul]; 95 (Pt 7): 1612-8 PMID24769839show ga Proteins aggregate in several slowly progressive neurodegenerative diseases called ?proteinopathies?. Studies with cell cultures and transgenic mice overexpressing mutated proteins suggested that aggregates of one protein induced misfolding and aggregation of other proteins as well ? a possible common mechanism for some neurodegenerative diseases. However, most proteinopathies are ?sporadic?, without gene mutation or overexpression. Thus, proteinopathies in WT animals genetically close to humans might be informative. Squirrel monkeys infected with the classical bovine spongiform encephalopathy agent developed an encephalopathy resembling variant Creutzfeldt?Jakob disease with accumulations not only of abnormal prion protein (PrPTSE), but also three other proteins: hyperphosphorylated tau (p-tau), ?-synuclein and ubiquitin; ?-amyloid protein (A?) did not accumulate. Severity of brain lesions correlated with spongiform degeneration. No amyloid was detected. These results suggested that PrPTSE enhanced formation of p-tau and aggregation of ?-synuclein and ubiquitin, but not A?, providing a new experimental model for neurodegenerative diseases associated with complex proteinopathies. äComplex proteinopathy with accumulations of prion protein, hyperphosph(epmc).pdf DeepDyve Pubget Overpricing