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10.4161/idp.26204 http://scihub22266oqcxt.onion/10.4161/idp.26204 C5424802!5424802!28516021     free     free     free Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Intrinsically+Disord+Proteins 2013 ; 1 (1): ä Nephropedia Template TP {{tp|p=28516021|t=2013. Multiple fuzzy interactions in the moonlighting function of thymosin-?4 |pdf=|usr=}}{{28516021}} gab.com Text Multiple fuzzy interactions in the moonlighting function of thymosin- 4 JO: Intrinsically Disord Proteins http://www.kidney.de/pget.php?&tw=1&pmid=28516021 #FOAvip Thymosine ?4 (Tß4) is a 43 amino acid long intrinsically disordered protein (IDP), which was initially identified as an actin-binding and sequestering molecule. Later it was described to have multiple other functions, such as regulation of endothelial cell differentiation, blood vessel formation, wound repair, cardiac cell migration, and survival.1 The various functions of T?4 are mediated by interactions with distinct and structurally unrelated partners, such as PINCH, ILK, and stabilin-2, besides the originally identified G-actin. Although the cellular readout of these interactions and the formation of these complexes have been thoroughly described, no attempt was made to study these interactions in detail, and to elucidate the thermodynamic, kinetic, and structural underpinning of this range of moonlighting functions. Because T?4 is mostly disordered, and its 4 described partners are structurally unrelated (the CTD of stabilin-2 is actually fully disordered), it occurred to us that this system might be ideal to characterize the structural adaptability and ensuing moonlighting functions of IDPs. Unexpectedly, we found that T?4 engages in multiple weak, transient, and fuzzy interactions, i.e., it is capable of mediating distinct yet specific interactions without adapting stable folded structures. Twit Text FOAVip Multiple fuzzy interactions in the moonlighting function of thymosin- 4 ????Intrinsically Disord Proteins http://www.kidney.de/pget.php?&tw=1&pmid=28516021 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28516021 #FOAvip English Wikipedia <ref>{{Cite pmid|28516021}}</ref> Multiple fuzzy interactions in the moonlighting function of thymosin-?4 #MMPMID28516021 Tantos A; Szabo B; Lang A; Varga Z; Tsylonok M; Bokor M; Verebelyi T; Kamasa P; Tompa K; Perczel A; Buday L; Lee SH; Choo Y; Han KH; Tompa P Intrinsically Disord Proteins 2013[Jan]; 1 (1): ä PMID28516021show ga Thymosine ?4 (Tß4) is a 43 amino acid long intrinsically disordered protein (IDP), which was initially identified as an actin-binding and sequestering molecule. Later it was described to have multiple other functions, such as regulation of endothelial cell differentiation, blood vessel formation, wound repair, cardiac cell migration, and survival.1 The various functions of T?4 are mediated by interactions with distinct and structurally unrelated partners, such as PINCH, ILK, and stabilin-2, besides the originally identified G-actin. Although the cellular readout of these interactions and the formation of these complexes have been thoroughly described, no attempt was made to study these interactions in detail, and to elucidate the thermodynamic, kinetic, and structural underpinning of this range of moonlighting functions. Because T?4 is mostly disordered, and its 4 described partners are structurally unrelated (the CTD of stabilin-2 is actually fully disordered), it occurred to us that this system might be ideal to characterize the structural adaptability and ensuing moonlighting functions of IDPs. Unexpectedly, we found that T?4 engages in multiple weak, transient, and fuzzy interactions, i.e., it is capable of mediating distinct yet specific interactions without adapting stable folded structures. äMultiple fuzzy interactions in the moonlighting function of thymosin-?(epmc).pdf DeepDyve Pubget Overpricing