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10.1182/blood-2015-04-641688 http://scihub22266oqcxt.onion/10.1182/blood-2015-04-641688 C4543227!4543227 !26065652     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 245.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 245.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\26065652 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Blood 2015 ; 126 (8 ): 935-8 Nephropedia Template TP {{tp|p=26065652 |t=2015. Mapping the interaction between factor VIII and von Willebrand factor by electron microscopy and mass spectrometry |pdf=|usr=}}{{26065652 }} gab.com Text Mapping the interaction between factor VIII and von Willebrand factor by electron microscopy and mass spectrometry JO: Blood http://www.kidney.de/pget.php?&tw=1&pmid=26065652 #FOAvip Association with the D'D3 domain of von Willebrand factor (VWF) stabilizes factor VIII (FVIII) in the circulation and maintains it at a level sufficient to prevent spontaneous bleeding. We used negative-stain electron microscopy (EM) to visualize complexes of FVIII with dimeric and monomeric forms of the D'D3 domain. The EM averages show that FVIII interacts with the D'D3 domain primarily through its C1 domain, with the C2 domain providing a secondary attachment site. Hydrogen-deuterium exchange mass spectrometry corroborated the importance of the C1 domain in D'D3 binding and implicates additional surface regions on FVIII in the interaction. Together, our results establish that the C1 domain is the major binding site on FVIII for VWF, reiterate the importance of the a3 acidic peptide in VWF binding, and suggest that the A3 and C2 domains play ancillary roles in this interaction. Twit Text FOAVip Mapping the interaction between factor VIII and von Willebrand factor by electron microscopy and mass spectrometry ????Blood http://www.kidney.de/pget.php?&tw=1&pmid=26065652 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26065652 #FOAvip English Wikipedia <ref>{{Cite pmid|26065652 }}</ref> Mapping the interaction between factor VIII and von Willebrand factor by electron microscopy and mass spectrometry #MMPMID26065652 Chiu PL ; Bou-Assaf GM ; Chhabra ES ; Chambers MG ; Peters RT ; Kulman JD ; Walz T Blood 2015[Aug]; 126 (8 ): 935-8 PMID26065652 show ga Association with the D'D3 domain of von Willebrand factor (VWF) stabilizes factor VIII (FVIII) in the circulation and maintains it at a level sufficient to prevent spontaneous bleeding. We used negative-stain electron microscopy (EM) to visualize complexes of FVIII with dimeric and monomeric forms of the D'D3 domain. The EM averages show that FVIII interacts with the D'D3 domain primarily through its C1 domain, with the C2 domain providing a secondary attachment site. Hydrogen-deuterium exchange mass spectrometry corroborated the importance of the C1 domain in D'D3 binding and implicates additional surface regions on FVIII in the interaction. Together, our results establish that the C1 domain is the major binding site on FVIII for VWF, reiterate the importance of the a3 acidic peptide in VWF binding, and suggest that the A3 and C2 domains play ancillary roles in this interaction. |Binding Sites [MESH] |Factor VIII/*chemistry/*metabolism/ultrastructure [MESH] |HEK293 Cells [MESH] |Humans [MESH] |Mass Spectrometry [MESH] |Microscopy, Electron [MESH] |Protein Structure, Tertiary [MESH]Mapping the interaction between factor VIII and von Willebrand factor (epmc).pdf DeepDyve Pubget Overpricing