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10.1038/s41598-017-01264-8 http://scihub22266oqcxt.onion/10.1038/s41598-017-01264-8 C5430790!5430790!28446792     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 265.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 265.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 265.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 265.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Sci+Rep 2017 ; 7 (ä): ä Nephropedia Template TP {{tp|p=28446792|t=2017. Sulfated Hyaluronan Derivatives Modulate TGF-?1:Receptor Complex Formation: Possible Consequences for TGF-?1 Signaling |pdf=|usr=}}{{28446792}} gab.com Text Sulfated Hyaluronan Derivatives Modulate TGF- 1:Receptor Complex Formation: Possible Consequences for TGF- 1 Signaling JO: Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=28446792 #FOAvip Glycosaminoglycans are known to bind biological mediators thereby modulating their biological activity. Sulfated hyaluronans (sHA) were reported to strongly interact with transforming growth factor (TGF)-?1 leading to impaired bioactivity in fibroblasts. The underlying mechanism is not fully elucidated yet. Examining the interaction of all components of the TGF-?1:receptor complex with sHA by surface plasmon resonance, we could show that highly sulfated HA (sHA3) blocks binding of TGF-?1 to its TGF-? receptor-I (T?R-I) and -II (T?R-II). However, sequential addition of sHA3 to the T?R-II/TGF-?1 complex led to a significantly stronger recruitment of T?R-I compared to a complex lacking sHA3, indicating that the order of binding events is very important. Molecular modeling suggested a possible molecular mechanism in which sHA3 could potentially favor the association of T?R-I when added sequentially. For the first time bioactivity of TGF-?1 in conjunction with sHA was investigated at the receptor level. T?R-I and, furthermore, Smad2 phosphorylation were decreased in the presence of sHA3 indicating the formation of an inactive signaling complex. The results contribute to an improved understanding of the interference of sHA3 with TGF-?1:receptor complex formation and will help to further improve the design of functional biomaterials that interfere with TGF-?1-driven skin fibrosis. Twit Text FOAVip Sulfated Hyaluronan Derivatives Modulate TGF- 1:Receptor Complex Formation: Possible Consequences for TGF- 1 Signaling ????Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=28446792 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28446792 #FOAvip English Wikipedia <ref>{{Cite pmid|28446792}}</ref> Sulfated Hyaluronan Derivatives Modulate TGF-?1:Receptor Complex Formation: Possible Consequences for TGF-?1 Signaling #MMPMID28446792 Koehler L; Samsonov S; Rother S; Vogel S; Köhling S; Moeller S; Schnabelrauch M; Rademann J; Hempel U; Pisabarro MT; Scharnweber D; Hintze V Sci Rep 2017[]; 7 (ä): ä PMID28446792show ga Glycosaminoglycans are known to bind biological mediators thereby modulating their biological activity. Sulfated hyaluronans (sHA) were reported to strongly interact with transforming growth factor (TGF)-?1 leading to impaired bioactivity in fibroblasts. The underlying mechanism is not fully elucidated yet. Examining the interaction of all components of the TGF-?1:receptor complex with sHA by surface plasmon resonance, we could show that highly sulfated HA (sHA3) blocks binding of TGF-?1 to its TGF-? receptor-I (T?R-I) and -II (T?R-II). However, sequential addition of sHA3 to the T?R-II/TGF-?1 complex led to a significantly stronger recruitment of T?R-I compared to a complex lacking sHA3, indicating that the order of binding events is very important. Molecular modeling suggested a possible molecular mechanism in which sHA3 could potentially favor the association of T?R-I when added sequentially. For the first time bioactivity of TGF-?1 in conjunction with sHA was investigated at the receptor level. T?R-I and, furthermore, Smad2 phosphorylation were decreased in the presence of sHA3 indicating the formation of an inactive signaling complex. The results contribute to an improved understanding of the interference of sHA3 with TGF-?1:receptor complex formation and will help to further improve the design of functional biomaterials that interfere with TGF-?1-driven skin fibrosis. äSulfated Hyaluronan Derivatives Modulate TGF-?1:Receptor Complex Forma(epmc).pdf DeepDyve Pubget Overpricing