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10.1016/j.bbalip.2015.02.013 http://scihub22266oqcxt.onion/10.1016/j.bbalip.2015.02.013 C4380703!4380703!25732852     free     free     free Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Biochim+Biophys+Acta 2015 ; 1851 (6): 746-58 Nephropedia Template TP {{tp|p=25732852|t=2015. Polyphosphoinositide binding domains: key to inositol lipid biology |pdf=|usr=}}{{25732852}} gab.com Text Polyphosphoinositide binding domains: key to inositol lipid biology JO: Biochim Biophys Acta http://www.kidney.de/pget.php?&tw=1&pmid=25732852 #FOAvip Polyphosphoinositides (PPIn) are an important family of phospholipids located on the cytoplasmic leaflet of eukaryotic cell membranes. Collectively, they are critical for the regulation many aspects of membrane homeostasis and signaling, with notable relevance to human physiology and disease. This regulation is achieved through the selective interaction of these lipids with hundreds of cellular proteins, and thus the capability to study these localized interactions is crucial to understanding their functions. In this review, we discuss current knowledge of the principle types of PPIn-protein interactions, focusing on specific lipid-binding domains. We then discuss how these domains have been re-tasked by biologists as molecular probes for these lipids in living cells. Finally, we describe how the knowledge gained with these probes, when combined with other techniques, has led to the current view of the lipids? localization and function in eukaryotes, focusing mainly on animal cells. Twit Text FOAVip Polyphosphoinositide binding domains: key to inositol lipid biology ????Biochim Biophys Acta http://www.kidney.de/pget.php?&tw=1&pmid=25732852 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25732852 #FOAvip English Wikipedia <ref>{{Cite pmid|25732852}}</ref> Polyphosphoinositide binding domains: key to inositol lipid biology #MMPMID25732852 Hammond GRV; Balla T Biochim Biophys Acta 2015[Jun]; 1851 (6): 746-58 PMID25732852show ga Polyphosphoinositides (PPIn) are an important family of phospholipids located on the cytoplasmic leaflet of eukaryotic cell membranes. Collectively, they are critical for the regulation many aspects of membrane homeostasis and signaling, with notable relevance to human physiology and disease. This regulation is achieved through the selective interaction of these lipids with hundreds of cellular proteins, and thus the capability to study these localized interactions is crucial to understanding their functions. In this review, we discuss current knowledge of the principle types of PPIn-protein interactions, focusing on specific lipid-binding domains. We then discuss how these domains have been re-tasked by biologists as molecular probes for these lipids in living cells. Finally, we describe how the knowledge gained with these probes, when combined with other techniques, has led to the current view of the lipids? localization and function in eukaryotes, focusing mainly on animal cells. äPolyphosphoinositide binding domains: key to inositol lipid biology (epmc).pdf DeepDyve Pubget Overpricing