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10.1021/acs.biochem.6b00566 http://scihub22266oqcxt.onion/10.1021/acs.biochem.6b00566 C5551644!5551644!27951653     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 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 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 298.79999999999995 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Biochemistry 2016 ; 55 (49): 6880-96 Nephropedia Template TP {{tp|p=27951653|t=2016. Binding Properties of the Transforming Growth Factor-? Coreceptor Betaglycan: Proposed Mechanism for Potentiation of Receptor Complex Assembly and Signaling |pdf=|usr=}}{{27951653}} gab.com Text Binding Properties of the Transforming Growth Factor- Coreceptor Betaglycan: Proposed Mechanism for Potentiation of Receptor Complex Assembly and Signaling JO: Biochemistry http://www.kidney.de/pget.php?&tw=1&pmid=27951653 #FOAvip Transforming growth factor (TGF) ?1, ?2, and ?3 (TGF-?1?TGF-?3, respectively) are small secreted signaling proteins that each signal through the TGF-? type I and type II receptors (T?RI and T?RII, respectively). However, TGF-?2, which is well-known to bind T?RII several hundred-fold more weakly than TGF-?1 and TGF-?3, has an additional requirement for betaglycan, a membrane-anchored nonsignaling receptor. Betaglycan has two domains that bind TGF-?2 at independent sites, but how it binds TGF-?2 to potentiate T?RII binding and how the complex with TGF-?, T?RII, and betaglycan undergoes the transition to the signaling complex with TGF-?, T?RII, and T?RI are not understood. To investigate the mechanism, the binding of the TGF-?s to the betaglycan extracellular domain, as well as its two independent binding domains, either directly or in combination with the T?RI and T?RII ectodomains, was studied using surface plasmon resonance, isothermal titration calorimetry, and size-exclusion chromatography. These studies show that betaglycan binds TGF-? homodimers with a 1:1 stoichiometry in a manner that allows one molecule of T?RII to bind. These studies further show that betaglycan modestly potentiates the binding of T?RII and must be displaced to allow T?RI to bind. These findings suggest that betaglycan functions to bind and concentrate TGF-?2 on the cell surface and thus promote the binding of T?RII by both membrane-localization effects and allostery. These studies further suggest that the transition to the signaling complex is mediated by the recruitment of T?RI, which simultaneously displaces betaglycan and stabilizes the bound T?RII by direct receptor?receptor contact. Twit Text FOAVip Binding Properties of the Transforming Growth Factor- Coreceptor Betaglycan: Proposed Mechanism for Potentiation of Receptor Complex Assembly and Signaling ????Biochemistry http://www.kidney.de/pget.php?&tw=1&pmid=27951653 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27951653 #FOAvip English Wikipedia <ref>{{Cite pmid|27951653}}</ref> Binding Properties of the Transforming Growth Factor-? Coreceptor Betaglycan: Proposed Mechanism for Potentiation of Receptor Complex Assembly and Signaling #MMPMID27951653 Villarreal M; Kim SK; Barron L; Kodali R; Baardsnes J; Hinck CS; Krzysiak TC; Henen MA; Pakhomova O; Mendoza V; O?Connor-McCourt MD; Lafer EM; López-Casillas F; Hinck AP Biochemistry 2016[Dec]; 55 (49): 6880-96 PMID27951653show ga Transforming growth factor (TGF) ?1, ?2, and ?3 (TGF-?1?TGF-?3, respectively) are small secreted signaling proteins that each signal through the TGF-? type I and type II receptors (T?RI and T?RII, respectively). However, TGF-?2, which is well-known to bind T?RII several hundred-fold more weakly than TGF-?1 and TGF-?3, has an additional requirement for betaglycan, a membrane-anchored nonsignaling receptor. Betaglycan has two domains that bind TGF-?2 at independent sites, but how it binds TGF-?2 to potentiate T?RII binding and how the complex with TGF-?, T?RII, and betaglycan undergoes the transition to the signaling complex with TGF-?, T?RII, and T?RI are not understood. To investigate the mechanism, the binding of the TGF-?s to the betaglycan extracellular domain, as well as its two independent binding domains, either directly or in combination with the T?RI and T?RII ectodomains, was studied using surface plasmon resonance, isothermal titration calorimetry, and size-exclusion chromatography. These studies show that betaglycan binds TGF-? homodimers with a 1:1 stoichiometry in a manner that allows one molecule of T?RII to bind. These studies further show that betaglycan modestly potentiates the binding of T?RII and must be displaced to allow T?RI to bind. These findings suggest that betaglycan functions to bind and concentrate TGF-?2 on the cell surface and thus promote the binding of T?RII by both membrane-localization effects and allostery. These studies further suggest that the transition to the signaling complex is mediated by the recruitment of T?RI, which simultaneously displaces betaglycan and stabilizes the bound T?RII by direct receptor?receptor contact. äBinding Properties of the Transforming Growth Factor-? Coreceptor Beta(epmc).pdf DeepDyve Pubget Overpricing