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10.1016/j.tim.2015.07.010 http://scihub22266oqcxt.onion/10.1016/j.tim.2015.07.010 C4636965!4636965 !26439293     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=26439293 &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 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 Deprecated: Implicit conversion from float 209.6 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\26439293 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Trends+Microbiol 2015 ; 23 (11 ): 693-706 Nephropedia Template TP {{tp|p=26439293 |t=2015. Bacterial amyloid formation: structural insights into curli biogensis |pdf=|usr=}}{{26439293 }} gab.com Text Bacterial amyloid formation: structural insights into curli biogensis JO: Trends Microbiol http://www.kidney.de/pget.php?&tw=1&pmid=26439293 #FOAvip Curli are functional amyloid fibers assembled by many Gram-negative bacteria as part of an extracellular matrix that encapsulates the bacteria within a biofilm. A multicomponent secretion system ensures the safe transport of the aggregation-prone curli subunits across the periplasm and outer membrane, and coordinates subunit self-assembly into surface-attached fibers. To avoid the build-up of potentially toxic intracellular protein aggregates, the timing and location of the interactions of the different curli proteins are of paramount importance. Here we review the structural and molecular biology of curli biogenesis, with a focus on the recent breakthroughs in our understanding of subunit chaperoning and secretion. The mechanistic insight into the curli assembly pathway will provide tools for new biotechnological applications and inform the design of targeted inhibitors of amyloid polymerization and biofilm formation. Twit Text FOAVip Bacterial amyloid formation: structural insights into curli biogensis ????Trends Microbiol http://www.kidney.de/pget.php?&tw=1&pmid=26439293 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26439293 #FOAvip English Wikipedia <ref>{{Cite pmid|26439293 }}</ref> Bacterial amyloid formation: structural insights into curli biogensis #MMPMID26439293 Van Gerven N ; Klein RD ; Hultgren SJ ; Remaut H Trends Microbiol 2015[Nov]; 23 (11 ): 693-706 PMID26439293 show ga Curli are functional amyloid fibers assembled by many Gram-negative bacteria as part of an extracellular matrix that encapsulates the bacteria within a biofilm. A multicomponent secretion system ensures the safe transport of the aggregation-prone curli subunits across the periplasm and outer membrane, and coordinates subunit self-assembly into surface-attached fibers. To avoid the build-up of potentially toxic intracellular protein aggregates, the timing and location of the interactions of the different curli proteins are of paramount importance. Here we review the structural and molecular biology of curli biogenesis, with a focus on the recent breakthroughs in our understanding of subunit chaperoning and secretion. The mechanistic insight into the curli assembly pathway will provide tools for new biotechnological applications and inform the design of targeted inhibitors of amyloid polymerization and biofilm formation. |Amyloid/antagonists & inhibitors/*biosynthesis/metabolism [MESH] |Bacterial Proteins/*biosynthesis/metabolism [MESH] |Biofilms/*growth & development [MESH] |Escherichia coli Proteins/metabolism [MESH] |Escherichia coli/metabolism [MESH]Bacterial amyloid formation: structural insights into curli biogensis (epmc).pdf DeepDyve Pubget Overpricing