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10.1016/j.bpj.2014.08.038 http://scihub22266oqcxt.onion/10.1016/j.bpj.2014.08.038 C4213724!4213724!25418161     free     free     free Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Biophys+J 2014 ; 107 (8): 1802-9 Nephropedia Template TP {{tp|p=25418161|t=2014. The Talin Dimer Structure Orientation Is Mechanically Regulated |pdf=|usr=}}{{25418161}} gab.com Text The Talin Dimer Structure Orientation Is Mechanically Regulated JO: Biophys J http://www.kidney.de/pget.php?&tw=1&pmid=25418161 #FOAvip Formation of a stable cell-substrate contact can be regulated by mechanical force, especially at the focal adhesion. Individual proteins that make up the focal adhesions, such as talin, can exhibit mechanosensing. We previously described one mode of talin mechanosensing in which the vinculin-binding site of talin is exposed after force-induced stretch of a single talin rod domain. Here, we describe a second mode of talin mechanosensing in which the talin dimer itself can adopt different orientations in response to mechanical stimulation. Using molecular dynamics models, we demonstrate that the C-terminus region of the talin dimer is flexible mainly at the linker between the dimerization helices and the nearby actin-binding helical bundle. Our molecular dynamics simulations reveal two possible orientations of the talin dimer at its C-terminus. The extracellular matrix (ECM)-bound integrins cross-linked by talin can be forced apart leading to an elongated orientation of the talin dimer, and the ECM-bound integrins can be forced together by the ECM producing a collapsed orientation of the talin dimer. Formation of the elongated orientation is shown to be more favorable. Switching between the two talin dimer orientations constitutes a mode of mechanosensing. Twit Text FOAVip The Talin Dimer Structure Orientation Is Mechanically Regulated ????Biophys J http://www.kidney.de/pget.php?&tw=1&pmid=25418161 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25418161 #FOAvip English Wikipedia <ref>{{Cite pmid|25418161}}</ref> The Talin Dimer Structure Orientation Is Mechanically Regulated #MMPMID25418161 Golji J; Mofrad M Biophys J 2014[Oct]; 107 (8): 1802-9 PMID25418161show ga Formation of a stable cell-substrate contact can be regulated by mechanical force, especially at the focal adhesion. Individual proteins that make up the focal adhesions, such as talin, can exhibit mechanosensing. We previously described one mode of talin mechanosensing in which the vinculin-binding site of talin is exposed after force-induced stretch of a single talin rod domain. Here, we describe a second mode of talin mechanosensing in which the talin dimer itself can adopt different orientations in response to mechanical stimulation. Using molecular dynamics models, we demonstrate that the C-terminus region of the talin dimer is flexible mainly at the linker between the dimerization helices and the nearby actin-binding helical bundle. Our molecular dynamics simulations reveal two possible orientations of the talin dimer at its C-terminus. The extracellular matrix (ECM)-bound integrins cross-linked by talin can be forced apart leading to an elongated orientation of the talin dimer, and the ECM-bound integrins can be forced together by the ECM producing a collapsed orientation of the talin dimer. Formation of the elongated orientation is shown to be more favorable. Switching between the two talin dimer orientations constitutes a mode of mechanosensing. äThe Talin Dimer Structure Orientation Is Mechanically Regulated (epmc).pdf DeepDyve Pubget Overpricing