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10.1074/jbc.H118.003970 http://scihub22266oqcxt.onion/10.1074/jbc.H118.003970 C6036190!6036190 !29980653     free     free     free Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 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\29980653 .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 2018 ; 293 (27 ): 10841-10842 Nephropedia Template TP {{tp|p=29980653 |t=2018. The sulfation code for propagation of neurodegeneration |pdf=|usr=}}{{29980653 }} gab.com Text The sulfation code for propagation of neurodegeneration JO: J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=29980653 #FOAvip Prion-like propagation of protein aggregates is thought to be an essential feature in many neurodegenerative diseases, but the mechanisms underlying transcellular transfer of protein aggregates remain unclear. Stopschinski et al. now demonstrate that the cellular uptake of tau, A?, and ?-synuclein aggregates mediated by heparan sulfate proteoglycans (HSPGs) varies with distinct glycosaminoglycan chain length and sulfation patterns. The results help us to understand how different protein aggregates propagate, leading to distinct neurodegenerative pathologies. Twit Text FOAVip The sulfation code for propagation of neurodegeneration ????J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=29980653 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=29980653 #FOAvip English Wikipedia <ref>{{Cite pmid|29980653 }}</ref> The sulfation code for propagation of neurodegeneration #MMPMID29980653 Yamada M ; Hamaguchi T J Biol Chem 2018[Jul]; 293 (27 ): 10841-10842 PMID29980653 show ga Prion-like propagation of protein aggregates is thought to be an essential feature in many neurodegenerative diseases, but the mechanisms underlying transcellular transfer of protein aggregates remain unclear. Stopschinski et al. now demonstrate that the cellular uptake of tau, A?, and ?-synuclein aggregates mediated by heparan sulfate proteoglycans (HSPGs) varies with distinct glycosaminoglycan chain length and sulfation patterns. The results help us to understand how different protein aggregates propagate, leading to distinct neurodegenerative pathologies. |Amyloid beta-Peptides/*chemistry/metabolism [MESH] |Glycosaminoglycans/*chemistry/metabolism [MESH] |Heparan Sulfate Proteoglycans/*metabolism [MESH] |Humans [MESH] |Neurodegenerative Diseases/metabolism/*pathology [MESH] |Sulfur/*metabolism [MESH] |alpha-Synuclein/*metabolism [MESH]The sulfation code for propagation of neurodegeneration (epmc).pdf DeepDyve Pubget Overpricing