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10.1021/acsnano.7b02755 http://scihub22266oqcxt.onion/10.1021/acsnano.7b02755 C5842356!5842356!28699736     free     free     free Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       ACS+Nano 2017 ; 11 (7): 7110-7 Nephropedia Template TP {{tp|p=28699736|t=2017. Detection of an Integrin-Binding Mechanoswitch within Fibronectin during Tissue Formation and Fibrosis |pdf=|usr=}}{{28699736}} gab.com Text Detection of an Integrin-Binding Mechanoswitch within Fibronectin during Tissue Formation and Fibrosis JO: ACS Nano http://www.kidney.de/pget.php?&tw=1&pmid=28699736 #FOAvip Fibronectin (Fn) is an extracellular matrix protein that orchestrates complex cell adhesion and signaling through cell surface integrin receptors during tissue development, remodeling, and disease, such as fibrosis. Fn is sensitive to mechanical forces in its tandem type III repeats, resulting in extensive molecular enlongation. As such, it has long been hypothesized that cell- and tissue-derived forces may activate an ?integrin switch? within the critical integrin-binding ninth and 10th type III repeats?conferring differential integrin-binding specificity, leading to differential cell responses. Yet, no direct evidence exists to prove the hypothesis nor demonstrate the physiological existence of the switch. We report direct experimental evidence for the Fn integrin switch both in vitro and ex vivo using a scFv engineered to detect the transient, force-induced conformational change, representing an opportunity for detection and targeting of early molecular signatures of cell contractile forces in tissue repair and disease. Twit Text FOAVip Detection of an Integrin-Binding Mechanoswitch within Fibronectin during Tissue Formation and Fibrosis ????ACS Nano http://www.kidney.de/pget.php?&tw=1&pmid=28699736 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28699736 #FOAvip English Wikipedia <ref>{{Cite pmid|28699736}}</ref> Detection of an Integrin-Binding Mechanoswitch within Fibronectin during Tissue Formation and Fibrosis #MMPMID28699736 Cao L; Nicosia J; Larouche J; Zhang Y; Bachman H; Brown AC; Holmgren L; Barker TH ACS Nano 2017[Jul]; 11 (7): 7110-7 PMID28699736show ga Fibronectin (Fn) is an extracellular matrix protein that orchestrates complex cell adhesion and signaling through cell surface integrin receptors during tissue development, remodeling, and disease, such as fibrosis. Fn is sensitive to mechanical forces in its tandem type III repeats, resulting in extensive molecular enlongation. As such, it has long been hypothesized that cell- and tissue-derived forces may activate an ?integrin switch? within the critical integrin-binding ninth and 10th type III repeats?conferring differential integrin-binding specificity, leading to differential cell responses. Yet, no direct evidence exists to prove the hypothesis nor demonstrate the physiological existence of the switch. We report direct experimental evidence for the Fn integrin switch both in vitro and ex vivo using a scFv engineered to detect the transient, force-induced conformational change, representing an opportunity for detection and targeting of early molecular signatures of cell contractile forces in tissue repair and disease. äDetection of an Integrin-Binding Mechanoswitch within Fibronectin duri(epmc).pdf DeepDyve Pubget Overpricing