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10.3389/fcimb.2015.00033 http://scihub22266oqcxt.onion/10.3389/fcimb.2015.00033 C4389571!4389571!25905048     free     free     free Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Front+Cell+Infect+Microbiol 2015 ; 5 (ä): ä Nephropedia Template TP {{tp|p=25905048|t=2015. New insight into the molecular control of bacterial functional amyloids |pdf=|usr=}}{{25905048}} gab.com Text New insight into the molecular control of bacterial functional amyloids JO: Front Cell Infect Microbiol http://www.kidney.de/pget.php?&tw=1&pmid=25905048 #FOAvip Amyloid protein structure has been discovered in a variety of functional or pathogenic contexts. What distinguishes the former from the latter is that functional amyloid systems possess dedicated molecular control systems that determine the timing, location, and structure of the fibers. Failure to guide this process can result in cytotoxicity, as observed in several pathologies like Alzheimer's and Parkinson's Disease. Many gram-negative bacteria produce an extracellular amyloid fiber known as curli via a multi-component secretion system. During this process, aggregation-prone, semi-folded curli subunits have to cross the periplasm and outer-membrane and self-assemble into surface-attached fibers. Two recent breakthroughs have provided molecular details regarding periplasmic chaperoning and subunit secretion. This review offers a combined perspective on these first mechanistic insights into the curli system. Twit Text FOAVip New insight into the molecular control of bacterial functional amyloids ????Front Cell Infect Microbiol http://www.kidney.de/pget.php?&tw=1&pmid=25905048 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25905048 #FOAvip English Wikipedia <ref>{{Cite pmid|25905048}}</ref> New insight into the molecular control of bacterial functional amyloids #MMPMID25905048 Taylor JD; Matthews SJ Front Cell Infect Microbiol 2015[]; 5 (ä): ä PMID25905048show ga Amyloid protein structure has been discovered in a variety of functional or pathogenic contexts. What distinguishes the former from the latter is that functional amyloid systems possess dedicated molecular control systems that determine the timing, location, and structure of the fibers. Failure to guide this process can result in cytotoxicity, as observed in several pathologies like Alzheimer's and Parkinson's Disease. Many gram-negative bacteria produce an extracellular amyloid fiber known as curli via a multi-component secretion system. During this process, aggregation-prone, semi-folded curli subunits have to cross the periplasm and outer-membrane and self-assemble into surface-attached fibers. Two recent breakthroughs have provided molecular details regarding periplasmic chaperoning and subunit secretion. This review offers a combined perspective on these first mechanistic insights into the curli system. äNew insight into the molecular control of bacterial functional amyloid(epmc).pdf DeepDyve Pubget Overpricing