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10.3389/fchem.2021.626059 http://scihub22266oqcxt.onion/10.3389/fchem.2021.626059 33681145!7930612!33681145     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       Front+Chem 2021 ; 9 (ä): 626059 Nephropedia Template TP {{tp|p=33681145|t=2021. Viroporins vs Other Pore-Forming Proteins: What Lessons Can We Take?|pdf=|usr=}}{{33681145}} gab.com Text Viroporins vs Other Pore-Forming Proteins: What Lessons Can We Take JO: Front Chem http://www.kidney.de/pget.php?&tw=1&pmid=33681145 #FOAvip Pore-forming proteins (PFPs) exist in virtually all domains of life, and by disrupting cellular membranes, depending on the pore size, they cause ion dis-balance, small substances, or even protein efflux/influx, influencing cell's signaling routes and fate. Such pore-forming proteins exist from bacteria to viruses and also shape host defense systems, including innate immunity. There is strong evidence that amyloid toxicity is also caused by prefibrillar oligomers making "amyloid pores" into cellular membranes. For most of the PFPs, a 2-step mechanism of protein-membrane interaction takes place on the "lipid rafts," membrane microdomains rich in gangliosides and cholesterol. In this mini-review paper, common traits of different PFPs are looked at. Possible ways for therapy of channelopathies and/or modulating immunity relevant to the new threat of SARS-CoV-2 infections could be learnt from such comparisons. Twit Text FOAVip Viroporins vs Other Pore-Forming Proteins: What Lessons Can We Take ????Front Chem http://www.kidney.de/pget.php?&tw=1&pmid=33681145 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33681145 #FOAvip English Wikipedia <ref>{{Cite pmid|33681145}}</ref> Viroporins vs Other Pore-Forming Proteins: What Lessons Can We Take? #MMPMID33681145 Zerovnik E Front Chem 2021[]; 9 (ä): 626059 PMID33681145show ga Pore-forming proteins (PFPs) exist in virtually all domains of life, and by disrupting cellular membranes, depending on the pore size, they cause ion dis-balance, small substances, or even protein efflux/influx, influencing cell's signaling routes and fate. Such pore-forming proteins exist from bacteria to viruses and also shape host defense systems, including innate immunity. There is strong evidence that amyloid toxicity is also caused by prefibrillar oligomers making "amyloid pores" into cellular membranes. For most of the PFPs, a 2-step mechanism of protein-membrane interaction takes place on the "lipid rafts," membrane microdomains rich in gangliosides and cholesterol. In this mini-review paper, common traits of different PFPs are looked at. Possible ways for therapy of channelopathies and/or modulating immunity relevant to the new threat of SARS-CoV-2 infections could be learnt from such comparisons. äViroporins vs Other Pore-Forming Proteins: What Lessons Can We Take?(epmc).pdf DeepDyve Pubget Overpricing