Use my Search Websuite to scan PubMed, PMCentral, Journal Hosts and Journal Archives, FullText. Kick-your-searchterm to multiple Engines kick-your-query now !>

A dictionary by aggregated review articles of nephrology, medicine and the life sciences Your one-stop-run pathway from word to the immediate pdf of peer-reviewed on-topic knowledge.

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 245.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Mitochondrion 2015 ; 21 (ä): 27-32 Nephropedia Template TP {{tp|p=25598000|t=2015. Tafazzinsfrom Drosophila and Mammalian Cells Assemble in Large Protein Complexes with a Short Half-Life |pdf=|usr=}}{{25598000}} gab.com Text Tafazzinsfrom 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?6 h, 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 Tafazzinsfrom 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> Tafazzinsfrom 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 PMID25598000show 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?6 h, 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. äTafazzinsfrom Drosophila and Mammalian Cells Assemble in Large Protein(epmc).pdf DeepDyve Pubget Overpricing