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10.1074/jbc.R114.583492 http://scihub22266oqcxt.onion/10.1074/jbc.R114.583492 C4106303!4106303 !24860092     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=24860092 &cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\24860092 .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 (29 ): 19839-40 Nephropedia Template TP {{tp|p=24860092 |t=2014. Prions and prion-like proteins |pdf=|usr=}}{{24860092 }} gab.com Text Prions and prion-like proteins JO: J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=24860092 #FOAvip Prions are self-replicating protein aggregates and are the primary causative factor in a number of neurological diseases in mammals. The prion protein (PrP) undergoes a conformational transformation leading to aggregation into an infectious cellular pathogen. Prion-like protein spreading and transmission of aggregates between cells have also been demonstrated for other proteins associated with Alzheimer disease and Parkinson disease. This protein-only phenomenon may therefore have broader implications in neurodegenerative disorders. The minireviews in this thematic series highlight the recent advances in prion biology and the roles these unique proteins play in disease. Twit Text FOAVip Prions and prion-like proteins ????J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=24860092 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=24860092 #FOAvip English Wikipedia <ref>{{Cite pmid|24860092 }}</ref> Prions and prion-like proteins #MMPMID24860092 Fraser PE J Biol Chem 2014[Jul]; 289 (29 ): 19839-40 PMID24860092 show ga Prions are self-replicating protein aggregates and are the primary causative factor in a number of neurological diseases in mammals. The prion protein (PrP) undergoes a conformational transformation leading to aggregation into an infectious cellular pathogen. Prion-like protein spreading and transmission of aggregates between cells have also been demonstrated for other proteins associated with Alzheimer disease and Parkinson disease. This protein-only phenomenon may therefore have broader implications in neurodegenerative disorders. The minireviews in this thematic series highlight the recent advances in prion biology and the roles these unique proteins play in disease. |Alzheimer Disease/etiology [MESH] |Animals [MESH] |Humans [MESH] |Multiprotein Complexes/chemistry/metabolism [MESH] |Parkinson Disease/etiology [MESH] |Prion Diseases/*etiology/metabolism/transmission [MESH] |Prions/chemistry/*metabolism [MESH] |Protein Conformation [MESH] |Protein Multimerization [MESH]Prions and prion-like proteins (epmc).pdf DeepDyve Pubget Overpricing