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10.1074/jbc.M115.678177 http://scihub22266oqcxt.onion/10.1074/jbc.M115.678177 C4777860!4777860!26742841     free     free     free Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       J+Biol+Chem 2016 ; 291 (10): 5278-98 Nephropedia Template TP {{tp|p=26742841|t=2016. Cell Adhesion on Amyloid Fibrils Lacking Integrin Recognition Motif* |pdf=|usr=}}{{26742841}} gab.com Text Cell Adhesion on Amyloid Fibrils Lacking Integrin Recognition Motif* JO: J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=26742841 #FOAvip Amyloids are highly ordered, cross-?-sheet-rich protein/peptide aggregates associated with both human diseases and native functions. Given the well established ability of amyloids in interacting with cell membranes, we hypothesize that amyloids can serve as universal cell-adhesive substrates. Here, we show that, similar to the extracellular matrix protein collagen, amyloids of various proteins/peptides support attachment and spreading of cells via robust stimulation of integrin expression and formation of integrin-based focal adhesions. Additionally, amyloid fibrils are also capable of immobilizing non-adherent red blood cells through charge-based interactions. Together, our results indicate that both active and passive mechanisms contribute to adhesion on amyloid fibrils. The present data may delineate the functional aspect of cell adhesion on amyloids by various organisms and its involvement in human diseases. Our results also raise the exciting possibility that cell adhesivity might be a generic property of amyloids. Twit Text FOAVip Cell Adhesion on Amyloid Fibrils Lacking Integrin Recognition Motif* ????J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=26742841 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26742841 #FOAvip English Wikipedia <ref>{{Cite pmid|26742841}}</ref> Cell Adhesion on Amyloid Fibrils Lacking Integrin Recognition Motif* #MMPMID26742841 Jacob RS; George E; Singh PK; Salot S; Anoop A; Jha NN; Sen S; Maji SK J Biol Chem 2016[Mar]; 291 (10): 5278-98 PMID26742841show ga Amyloids are highly ordered, cross-?-sheet-rich protein/peptide aggregates associated with both human diseases and native functions. Given the well established ability of amyloids in interacting with cell membranes, we hypothesize that amyloids can serve as universal cell-adhesive substrates. Here, we show that, similar to the extracellular matrix protein collagen, amyloids of various proteins/peptides support attachment and spreading of cells via robust stimulation of integrin expression and formation of integrin-based focal adhesions. Additionally, amyloid fibrils are also capable of immobilizing non-adherent red blood cells through charge-based interactions. Together, our results indicate that both active and passive mechanisms contribute to adhesion on amyloid fibrils. The present data may delineate the functional aspect of cell adhesion on amyloids by various organisms and its involvement in human diseases. Our results also raise the exciting possibility that cell adhesivity might be a generic property of amyloids. äCell Adhesion on Amyloid Fibrils Lacking Integrin Recognition Motif* (epmc).pdf DeepDyve Pubget Overpricing