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10.1016/j.molcel.2014.09.022 http://scihub22266oqcxt.onion/10.1016/j.molcel.2014.09.022 C4869853!4869853 !25458844     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=25458844 &cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215       Mol+Cell 2014 ; 56 (4 ): 496-505 Nephropedia Template TP {{tp|p=25458844 |t=2014. Structural model of active Bax at the membrane |pdf=|usr=}}{{25458844 }} gab.com Text Structural model of active Bax at the membrane JO: Mol Cell http://www.kidney.de/pget.php?&tw=1&pmid=25458844 #FOAvip Bax plays a central role in the mitochondrial pathway of apoptosis. Upon activation, cytosolic Bax monomers oligomerize on the surface of mitochondria and change conformation concertedly to punch holes into the outer membrane. The subsequent release of cytochrome c initiates cell death. However, the structure of membrane-inserted Bax and its mechanism of action remain largely unknown. Here, we propose a 3D model of active Bax at the membrane based on double electron-electron resonance (DEER) spectroscopy in liposomes and isolated mitochondria. We show that active Bax is organized at the membrane as assemblies of dimers. In addition to a stable dimerization domain, each monomer contains a more flexible piercing domain involved in interdimer interactions and pore formation. The most important structural change during Bax activation is the opening of the hairpin formed by helices 5 and 6, which adopts a clamp-like conformation central to the mechanism of mitochondrial permeabilization. Twit Text FOAVip Structural model of active Bax at the membrane ????Mol Cell http://www.kidney.de/pget.php?&tw=1&pmid=25458844 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25458844 #FOAvip English Wikipedia <ref>{{Cite pmid|25458844 }}</ref> Structural model of active Bax at the membrane #MMPMID25458844 Bleicken S ; Jeschke G ; Stegmueller C ; Salvador-Gallego R ; García-Sáez AJ ; Bordignon E Mol Cell 2014[Nov]; 56 (4 ): 496-505 PMID25458844 show ga Bax plays a central role in the mitochondrial pathway of apoptosis. Upon activation, cytosolic Bax monomers oligomerize on the surface of mitochondria and change conformation concertedly to punch holes into the outer membrane. The subsequent release of cytochrome c initiates cell death. However, the structure of membrane-inserted Bax and its mechanism of action remain largely unknown. Here, we propose a 3D model of active Bax at the membrane based on double electron-electron resonance (DEER) spectroscopy in liposomes and isolated mitochondria. We show that active Bax is organized at the membrane as assemblies of dimers. In addition to a stable dimerization domain, each monomer contains a more flexible piercing domain involved in interdimer interactions and pore formation. The most important structural change during Bax activation is the opening of the hairpin formed by helices 5 and 6, which adopts a clamp-like conformation central to the mechanism of mitochondrial permeabilization. |Animals [MESH] |Cell Membrane/*chemistry [MESH] |Mice [MESH] |Models, Molecular [MESH] |Protein Multimerization [MESH] |Protein Structure, Quaternary [MESH] |Protein Structure, Secondary [MESH] |Protein Structure, Tertiary [MESH]Structural model of active Bax at the membrane (epmc).pdf DeepDyve Pubget Overpricing