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10.1186/s12944-017-0473-y http://scihub22266oqcxt.onion/10.1186/s12944-017-0473-y C5410086!5410086!28454542     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       Lipids+Health+Dis 2017 ; 16 (ä): ä Nephropedia Template TP {{tp|p=28454542|t=2017. Perilipins: a diversity of intracellular lipid droplet proteins |pdf=|usr=}}{{28454542}} gab.com Text Perilipins: a diversity of intracellular lipid droplet proteins JO: Lipids Health Dis http://www.kidney.de/pget.php?&tw=1&pmid=28454542 #FOAvip Intracellular lipid droplets (LDs) are found in a wide variety of cell types and have been recognized as organelles with unique spherical structures. Although LDs are not stable lipid-depots, they are active sites of neutral lipid metabolism, and comprise neutral lipid or cholesterol cores surrounded by phospholipid monolayers containing specialized proteins. However, sizes and protein compositions vary between cell and tissue types. Proteins of the perilipin family have been associated with surfaces of LDs and all carry a conserved 11-mer repeat motif. Accumulating evidence indicates that all perilipins are involved in LD formation and that all play roles in LD function under differing conditions. In this brief review, we summarize current knowledge of the roles of perilipins and lipid metabolizing enzymes in a variety of mammalian cell types. Twit Text FOAVip Perilipins: a diversity of intracellular lipid droplet proteins ????Lipids Health Dis http://www.kidney.de/pget.php?&tw=1&pmid=28454542 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28454542 #FOAvip English Wikipedia <ref>{{Cite pmid|28454542}}</ref> Perilipins: a diversity of intracellular lipid droplet proteins #MMPMID28454542 Itabe H; Yamaguchi T; Nimura S; Sasabe N Lipids Health Dis 2017[]; 16 (ä): ä PMID28454542show ga Intracellular lipid droplets (LDs) are found in a wide variety of cell types and have been recognized as organelles with unique spherical structures. Although LDs are not stable lipid-depots, they are active sites of neutral lipid metabolism, and comprise neutral lipid or cholesterol cores surrounded by phospholipid monolayers containing specialized proteins. However, sizes and protein compositions vary between cell and tissue types. Proteins of the perilipin family have been associated with surfaces of LDs and all carry a conserved 11-mer repeat motif. Accumulating evidence indicates that all perilipins are involved in LD formation and that all play roles in LD function under differing conditions. In this brief review, we summarize current knowledge of the roles of perilipins and lipid metabolizing enzymes in a variety of mammalian cell types. äPerilipins: a diversity of intracellular lipid droplet proteins (epmc).pdf DeepDyve Pubget Overpricing