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10.15252/embr.201540229 http://scihub22266oqcxt.onion/10.15252/embr.201540229 C4515122!4515122 !26071602     free     free     free Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 267.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 267.2 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\26071602 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       EMBO+Rep 2015 ; 16 (7 ): 824-35 Nephropedia Template TP {{tp|p=26071602 |t=2015. Structural insight into the TRIAP1/PRELI-like domain family of mitochondrial phospholipid transfer complexes |pdf=|usr=}}{{26071602 }} gab.com Text Structural insight into the TRIAP1/PRELI-like domain family of mitochondrial phospholipid transfer complexes JO: EMBO Rep http://www.kidney.de/pget.php?&tw=1&pmid=26071602 #FOAvip The composition of the mitochondrial membrane is important for its architecture and proper function. Mitochondria depend on a tightly regulated supply of phospholipid via intra-mitochondrial synthesis and by direct import from the endoplasmic reticulum. The Ups1/PRELI-like family together with its mitochondrial chaperones (TRIAP1/Mdm35) represent a unique heterodimeric lipid transfer system that is evolutionary conserved from yeast to man. Work presented here provides new atomic resolution insight into the function of a human member of this system. Crystal structures of free TRIAP1 and the TRIAP1-SLMO1 complex reveal how the PRELI domain is chaperoned during import into the intermembrane mitochondrial space. The structural resemblance of PRELI-like domain of SLMO1 with that of mammalian phoshatidylinositol transfer proteins (PITPs) suggest that they share similar lipid transfer mechanisms, in which access to a buried phospholipid-binding cavity is regulated by conformationally adaptable loops. Twit Text FOAVip Structural insight into the TRIAP1/PRELI-like domain family of mitochondrial phospholipid transfer complexes ????EMBO Rep http://www.kidney.de/pget.php?&tw=1&pmid=26071602 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26071602 #FOAvip English Wikipedia <ref>{{Cite pmid|26071602 }}</ref> Structural insight into the TRIAP1/PRELI-like domain family of mitochondrial phospholipid transfer complexes #MMPMID26071602 Miliara X ; Garnett JA ; Tatsuta T ; Abid Ali F ; Baldie H ; Pérez-Dorado I ; Simpson P ; Yague E ; Langer T ; Matthews S EMBO Rep 2015[Jul]; 16 (7 ): 824-35 PMID26071602 show ga The composition of the mitochondrial membrane is important for its architecture and proper function. Mitochondria depend on a tightly regulated supply of phospholipid via intra-mitochondrial synthesis and by direct import from the endoplasmic reticulum. The Ups1/PRELI-like family together with its mitochondrial chaperones (TRIAP1/Mdm35) represent a unique heterodimeric lipid transfer system that is evolutionary conserved from yeast to man. Work presented here provides new atomic resolution insight into the function of a human member of this system. Crystal structures of free TRIAP1 and the TRIAP1-SLMO1 complex reveal how the PRELI domain is chaperoned during import into the intermembrane mitochondrial space. The structural resemblance of PRELI-like domain of SLMO1 with that of mammalian phoshatidylinositol transfer proteins (PITPs) suggest that they share similar lipid transfer mechanisms, in which access to a buried phospholipid-binding cavity is regulated by conformationally adaptable loops. |Adaptor Proteins, Signal Transducing/*chemistry/*metabolism [MESH] |Amino Acid Sequence [MESH] |Binding Sites [MESH] |Biological Transport [MESH] |Crystallography, X-Ray [MESH] |Endoplasmic Reticulum/metabolism [MESH] |Humans [MESH] |Hydrophobic and Hydrophilic Interactions [MESH] |Intracellular Signaling Peptides and Proteins/*chemistry/*metabolism [MESH] |Membrane Proteins/*chemistry/*metabolism [MESH] |Mitochondria/*metabolism [MESH] |Mitochondrial Membranes/*metabolism [MESH] |Mitochondrial Proteins/metabolism [MESH] |Molecular Chaperones/metabolism [MESH] |Molecular Sequence Data [MESH] |Phospholipids/chemistry/*metabolism [MESH] |Protein Structure, Secondary [MESH] |Protein Structure, Tertiary [MESH]Structural insight into the TRIAP1/PRELI-like domain family of mitocho(epmc).pdf DeepDyve Pubget Overpricing