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10.1038/cddiscovery.2017.16 http://scihub22266oqcxt.onion/10.1038/cddiscovery.2017.16 C5357670!5357670!28386457     free     free     free Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Cell+Death+Discov 2017 ; 3 (ä): 17016- Nephropedia Template TP {{tp|p=28386457|t=2017. Clearing the outer mitochondrial membrane from harmful proteins via lipid droplets |pdf=|usr=}}{{28386457}} gab.com Text Clearing the outer mitochondrial membrane from harmful proteins via lipid droplets JO: Cell Death Discov http://www.kidney.de/pget.php?&tw=1&pmid=28386457 #FOAvip In recent years it turned out that there is not only extensive communication between the nucleus and mitochondria but also between mitochondria and lipid droplets (LDs) as well. We were able to demonstrate that a number of proteins shuttle between LDs and mitochondria and it depends on the metabolic state of the cell on which organelle these proteins are predominantly localized. Responsible for the localization of the particular proteins is a protein domain consisting of two ?-helices, which we termed V-domain according to the predicted structure. So far we have detected this domain in the following proteins: mammalian BAX, BCL-XL, TCTP and yeast Mmi1p and Erg6p. According to our experiments there are two functions of this domain: (1) shuttling of proteins to mitochondria in times of stress and apoptosis; (2) clearing the outer mitochondrial membrane from pro- as well as anti-apoptotic proteins by moving them to LDs after the stress ceases. In this way the LDs are used by the cell to modulate stress response. Twit Text FOAVip Clearing the outer mitochondrial membrane from harmful proteins via lipid droplets ????Cell Death Discov http://www.kidney.de/pget.php?&tw=1&pmid=28386457 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28386457 #FOAvip English Wikipedia <ref>{{Cite pmid|28386457}}</ref> Clearing the outer mitochondrial membrane from harmful proteins via lipid droplets #MMPMID28386457 Bischof J; Salzmann M; Streubel MK; Hasek J; Geltinger F; Duschl J; Bresgen N; Briza P; Haskova D; Lejskova R; Sopjani M; Richter K; Rinnerthaler M Cell Death Discov 2017[]; 3 (ä): 17016- PMID28386457show ga In recent years it turned out that there is not only extensive communication between the nucleus and mitochondria but also between mitochondria and lipid droplets (LDs) as well. We were able to demonstrate that a number of proteins shuttle between LDs and mitochondria and it depends on the metabolic state of the cell on which organelle these proteins are predominantly localized. Responsible for the localization of the particular proteins is a protein domain consisting of two ?-helices, which we termed V-domain according to the predicted structure. So far we have detected this domain in the following proteins: mammalian BAX, BCL-XL, TCTP and yeast Mmi1p and Erg6p. According to our experiments there are two functions of this domain: (1) shuttling of proteins to mitochondria in times of stress and apoptosis; (2) clearing the outer mitochondrial membrane from pro- as well as anti-apoptotic proteins by moving them to LDs after the stress ceases. In this way the LDs are used by the cell to modulate stress response. äClearing the outer mitochondrial membrane from harmful proteins via li(epmc).pdf DeepDyve Pubget Overpricing