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10.1016/j.mito.2015.01.002 http://scihub22266oqcxt.onion/10.1016/j.mito.2015.01.002 C4693151!4693151 !25598000     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 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\25598000 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Mitochondrion 2015 ; 21 (ä): 27-32 Nephropedia Template TP {{tp|p=25598000 |t=2015. Tafazzins from Drosophila and mammalian cells assemble in large protein complexes with a short half-life |pdf=|usr=}}{{25598000 }} gab.com Text Tafazzins from Drosophila and mammalian cells assemble in large protein complexes with a short half-life JO: Mitochondrion http://www.kidney.de/pget.php?&tw=1&pmid=25598000 #FOAvip Tafazzin is a transacylase that affects cardiolipin fatty acid composition and mitochondrial function. Mutations in human tafazzin cause Barth syndrome yet the enzyme has mostly been characterized in yeast. To study tafazzin in higher organisms, we isolated mitochondria from Drosophila and mammalian cell cultures. Our data indicate that tafazzin binds to multiple protein complexes in these organisms, and that the interactions of tafazzin lack strong specificity. Very large tafazzin complexes could only be detected in the presence of cardiolipin, but smaller complexes remained intact even upon treatment with phospholipase A2. In mammalian cells, tafazzin had a half-life of only 3-6h, which was much shorter than the half-life of other mitochondrial proteins. The data suggest that tafazzin is a transient resident of multiple protein complexes. Twit Text FOAVip Tafazzins from Drosophila and mammalian cells assemble in large protein complexes with a short half-life ????Mitochondrion http://www.kidney.de/pget.php?&tw=1&pmid=25598000 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25598000 #FOAvip English Wikipedia <ref>{{Cite pmid|25598000 }}</ref> Tafazzins from Drosophila and mammalian cells assemble in large protein complexes with a short half-life #MMPMID25598000 Xu Y ; Malhotra A ; Claypool SM ; Ren M ; Schlame M Mitochondrion 2015[Mar]; 21 (ä): 27-32 PMID25598000 show ga Tafazzin is a transacylase that affects cardiolipin fatty acid composition and mitochondrial function. Mutations in human tafazzin cause Barth syndrome yet the enzyme has mostly been characterized in yeast. To study tafazzin in higher organisms, we isolated mitochondria from Drosophila and mammalian cell cultures. Our data indicate that tafazzin binds to multiple protein complexes in these organisms, and that the interactions of tafazzin lack strong specificity. Very large tafazzin complexes could only be detected in the presence of cardiolipin, but smaller complexes remained intact even upon treatment with phospholipase A2. In mammalian cells, tafazzin had a half-life of only 3-6h, which was much shorter than the half-life of other mitochondrial proteins. The data suggest that tafazzin is a transient resident of multiple protein complexes. |*Protein Multimerization [MESH] |1-Acylglycerophosphocholine O-Acyltransferase/isolation & purification/*metabolism [MESH] |Acyltransferases [MESH] |Animals [MESH] |Cell Line [MESH] |Drosophila [MESH] |Drosophila Proteins/isolation & purification/*metabolism [MESH] |Humans [MESH] |Protein Binding [MESH]Tafazzins from Drosophila and mammalian cells assemble in large protei(epmc).pdf DeepDyve Pubget Overpricing