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10.1098/rstb.2016.0212 http://scihub22266oqcxt.onion/10.1098/rstb.2016.0212 C5483515!5483515!28630152     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Philos+Trans+R+Soc+Lond+B+Biol+Sci 2017 ; 372 (1726): ä Nephropedia Template TP {{tp|p=28630152|t=2017. Repurposing a pore: highly conserved perforin-like proteins with alternative mechanisms |pdf=|usr=}}{{28630152}} gab.com Text Repurposing a pore: highly conserved perforin-like proteins with alternative mechanisms JO: Philos Trans R Soc Lond B Biol Sci http://www.kidney.de/pget.php?&tw=1&pmid=28630152 #FOAvip Pore-forming proteins play critical roles in pathogenic attack and immunological defence. The membrane attack complex/perforin (MACPF) group of homologues represents, with cholesterol-dependent cytolysins, the largest family of such proteins. In this review, we begin by describing briefly the structure of MACPF proteins, outlining their common mechanism of pore formation. We subsequently discuss some examples of MACPF proteins likely implicated in pore formation or other membrane-remodelling processes. Finally, we focus on astrotactin and bone morphogenetic protein and retinoic acid-induced neural-specific proteins, highly conserved MACPF family members involved in developmental processes, which have not been well studied to date or observed to form a pore?and which data suggest may act by alternative mechanisms.This article is part of the themed issue ?Membrane pores: from structure and assembly, to medicine and technology?. Twit Text FOAVip Repurposing a pore: highly conserved perforin-like proteins with alternative mechanisms ????Philos Trans R Soc Lond B Biol Sci http://www.kidney.de/pget.php?&tw=1&pmid=28630152 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28630152 #FOAvip English Wikipedia <ref>{{Cite pmid|28630152}}</ref> Repurposing a pore: highly conserved perforin-like proteins with alternative mechanisms #MMPMID28630152 Ni T; Gilbert RJC Philos Trans R Soc Lond B Biol Sci 2017[Aug]; 372 (1726): ä PMID28630152show ga Pore-forming proteins play critical roles in pathogenic attack and immunological defence. The membrane attack complex/perforin (MACPF) group of homologues represents, with cholesterol-dependent cytolysins, the largest family of such proteins. In this review, we begin by describing briefly the structure of MACPF proteins, outlining their common mechanism of pore formation. We subsequently discuss some examples of MACPF proteins likely implicated in pore formation or other membrane-remodelling processes. Finally, we focus on astrotactin and bone morphogenetic protein and retinoic acid-induced neural-specific proteins, highly conserved MACPF family members involved in developmental processes, which have not been well studied to date or observed to form a pore?and which data suggest may act by alternative mechanisms.This article is part of the themed issue ?Membrane pores: from structure and assembly, to medicine and technology?. äRepurposing a pore: highly conserved perforin-like proteins with alter(epmc).pdf DeepDyve Pubget Overpricing