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10.3390/pathogens7010027 http://scihub22266oqcxt.onion/10.3390/pathogens7010027 C5874753!5874753 !29518975     free     free     free Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 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\29518975 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Pathogens 2018 ; 7 (1 ): ä Nephropedia Template TP {{tp|p=29518975 |t=2018. Pharmacological Agents Targeting the Cellular Prion Protein |pdf=|usr=}}{{29518975 }} gab.com Text Pharmacological Agents Targeting the Cellular Prion Protein JO: Pathogens http://www.kidney.de/pget.php?&tw=1&pmid=29518975 #FOAvip Prion diseases are associated with the conversion of the cellular prion protein (PrP(C)), a glycoprotein expressed at the surface of a wide variety of cell types, into a misfolded conformer (the scrapie form of PrP, or PrP(Sc)) that accumulates in brain tissues of affected individuals. PrP(Sc) is a self-catalytic protein assembly capable of recruiting native conformers of PrP(C), and causing their rearrangement into new PrP(Sc) molecules. Several previous attempts to identify therapeutic agents against prion diseases have targeted PrP(Sc), and a number of compounds have shown potent anti-prion effects in experimental models. Unfortunately, so far, none of these molecules has successfully been translated into effective therapies for prion diseases. Moreover, mounting evidence suggests that PrP(Sc) might be a difficult pharmacological target because of its poorly defined structure, heterogeneous composition, and ability to generate different structural conformers (known as prion strains) that can elude pharmacological intervention. In the last decade, a less intuitive strategy to overcome all these problems has emerged: targeting PrP(C), the common substrate of any prion strain replication. This alternative approach possesses several technical and theoretical advantages, including the possibility of providing therapeutic effects also for other neurodegenerative disorders, based on recent observations indicating a role for PrP(C) in delivering neurotoxic signals of different misfolded proteins. Here, we provide an overview of compounds claimed to exert anti-prion effects by directly binding to PrP(C), discussing pharmacological properties and therapeutic potentials of each chemical class. Twit Text FOAVip Pharmacological Agents Targeting the Cellular Prion Protein ????Pathogens http://www.kidney.de/pget.php?&tw=1&pmid=29518975 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=29518975 #FOAvip English Wikipedia <ref>{{Cite pmid|29518975 }}</ref> Pharmacological Agents Targeting the Cellular Prion Protein #MMPMID29518975 Barreca ML ; Iraci N ; Biggi S ; Cecchetti V ; Biasini E Pathogens 2018[Mar]; 7 (1 ): ä PMID29518975 show ga Prion diseases are associated with the conversion of the cellular prion protein (PrP(C)), a glycoprotein expressed at the surface of a wide variety of cell types, into a misfolded conformer (the scrapie form of PrP, or PrP(Sc)) that accumulates in brain tissues of affected individuals. PrP(Sc) is a self-catalytic protein assembly capable of recruiting native conformers of PrP(C), and causing their rearrangement into new PrP(Sc) molecules. Several previous attempts to identify therapeutic agents against prion diseases have targeted PrP(Sc), and a number of compounds have shown potent anti-prion effects in experimental models. Unfortunately, so far, none of these molecules has successfully been translated into effective therapies for prion diseases. Moreover, mounting evidence suggests that PrP(Sc) might be a difficult pharmacological target because of its poorly defined structure, heterogeneous composition, and ability to generate different structural conformers (known as prion strains) that can elude pharmacological intervention. In the last decade, a less intuitive strategy to overcome all these problems has emerged: targeting PrP(C), the common substrate of any prion strain replication. This alternative approach possesses several technical and theoretical advantages, including the possibility of providing therapeutic effects also for other neurodegenerative disorders, based on recent observations indicating a role for PrP(C) in delivering neurotoxic signals of different misfolded proteins. Here, we provide an overview of compounds claimed to exert anti-prion effects by directly binding to PrP(C), discussing pharmacological properties and therapeutic potentials of each chemical class. äPharmacological Agents Targeting the Cellular Prion Protein (epmc).pdf DeepDyve Pubget Overpricing