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10.1016/j.str.2014.07.014 http://scihub22266oqcxt.onion/10.1016/j.str.2014.07.014 C4192069!4192069!25220470     free     free     free Deprecated: Implicit conversion from float 215.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 215.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Structure 2014 ; 22 (10): 1489-500 Nephropedia Template TP {{tp|p=25220470|t=2014. A Plug Release Mechanism for Membrane Permeation by MLKL |pdf=|usr=}}{{25220470}} gab.com Text A Plug Release Mechanism for Membrane Permeation by MLKL JO: Structure http://www.kidney.de/pget.php?&tw=1&pmid=25220470 #FOAvip MLKL is crucial for necroptosis, permeabilizing membranes through its N-terminal region upon phosphorylation of its kinase-like domain by RIP3. However, the mechanism underlying membrane permeabilization is unknown. The solution structure of the MLKL N-terminal region determined by NMR spectroscopy reveals a four-helix bundle with an additional helix at the top that is likely key for MLKL function, and a sixth, C-terminal helix that interacts with the top helix and with a poorly packed interface within the four-helix bundle. Fluorescence spectroscopy measurements indicate that much of the four-helix bundle inserts into membranes, but not the C-terminal helix. Moreover, we find that the four-helix bundle is sufficient to induce liposome leakage and that the C-terminal helix inhibits this activity. These results suggest that the four-helix bundle mediates membrane breakdown during necroptosis and that the sixth helix acts as a plug that prevents opening of the bundle and is released upon RIP3 phosphorylation. Twit Text FOAVip A Plug Release Mechanism for Membrane Permeation by MLKL ????Structure http://www.kidney.de/pget.php?&tw=1&pmid=25220470 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25220470 #FOAvip English Wikipedia <ref>{{Cite pmid|25220470}}</ref> A Plug Release Mechanism for Membrane Permeation by MLKL #MMPMID25220470 Su L; Quade B; Wang H; Sun L; Wang X; Rizo J Structure 2014[Oct]; 22 (10): 1489-500 PMID25220470show ga MLKL is crucial for necroptosis, permeabilizing membranes through its N-terminal region upon phosphorylation of its kinase-like domain by RIP3. However, the mechanism underlying membrane permeabilization is unknown. The solution structure of the MLKL N-terminal region determined by NMR spectroscopy reveals a four-helix bundle with an additional helix at the top that is likely key for MLKL function, and a sixth, C-terminal helix that interacts with the top helix and with a poorly packed interface within the four-helix bundle. Fluorescence spectroscopy measurements indicate that much of the four-helix bundle inserts into membranes, but not the C-terminal helix. Moreover, we find that the four-helix bundle is sufficient to induce liposome leakage and that the C-terminal helix inhibits this activity. These results suggest that the four-helix bundle mediates membrane breakdown during necroptosis and that the sixth helix acts as a plug that prevents opening of the bundle and is released upon RIP3 phosphorylation. äA Plug Release Mechanism for Membrane Permeation by MLKL (epmc).pdf DeepDyve Pubget Overpricing