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10.1091/mbc.E16-06-0390 http://scihub22266oqcxt.onion/10.1091/mbc.E16-06-0390 C5385934!5385934 !28148651     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 245.2 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 Deprecated: Implicit conversion from float 245.2 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 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\28148651 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Mol+Biol+Cell 2017 ; 28 (7 ): 858-864 Nephropedia Template TP {{tp|p=28148651 |t=2017. An intramolecular interaction within the lipid kinase Fab1 regulates cellular phosphatidylinositol 3,5-bisphosphate lipid levels |pdf=|usr=}}{{28148651 }} gab.com Text An intramolecular interaction within the lipid kinase Fab1 regulates cellular phosphatidylinositol 3,5-bisphosphate lipid levels JO: Mol Biol Cell http://www.kidney.de/pget.php?&tw=1&pmid=28148651 #FOAvip Phosphorylated phosphoinositide lipids (PPIs) are low-abundance signaling molecules that control signal transduction pathways and are necessary for cellular homeostasis. The PPI phosphatidylinositol (3,5)-bisphosphate (PI(3,5)P(2)) is essential in multiple organ systems. PI(3,5)P(2) is generated from PI3P by the conserved lipid kinase Fab1/PIKfyve. Defects in the dynamic regulation of PI(3,5)P(2) are linked to human diseases. However, few mechanisms that regulate PI(3,5)P(2) have been identified. Here we report an intramolecular interaction between the yeast Fab1 kinase region and an upstream conserved cysteine-rich (CCR) domain. We identify mutations in the kinase domain that lead to elevated levels of PI(3,5)P(2) and impair the interaction between the kinase and CCR domain. We also identify mutations in the CCR domain that lead to elevated levels of PI(3,5)P(2) Together these findings reveal a regulatory mechanism that involves the CCR domain of Fab1 and contributes to dynamic control of cellular PI(3,5)P(2) synthesis. Twit Text FOAVip An intramolecular interaction within the lipid kinase Fab1 regulates cellular phosphatidylinositol 3,5-bisphosphate lipid levels ????Mol Biol Cell http://www.kidney.de/pget.php?&tw=1&pmid=28148651 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28148651 #FOAvip English Wikipedia <ref>{{Cite pmid|28148651 }}</ref> An intramolecular interaction within the lipid kinase Fab1 regulates cellular phosphatidylinositol 3,5-bisphosphate lipid levels #MMPMID28148651 Lang MJ ; Strunk BS ; Azad N ; Petersen JL ; Weisman LS Mol Biol Cell 2017[Apr]; 28 (7 ): 858-864 PMID28148651 show ga Phosphorylated phosphoinositide lipids (PPIs) are low-abundance signaling molecules that control signal transduction pathways and are necessary for cellular homeostasis. The PPI phosphatidylinositol (3,5)-bisphosphate (PI(3,5)P(2)) is essential in multiple organ systems. PI(3,5)P(2) is generated from PI3P by the conserved lipid kinase Fab1/PIKfyve. Defects in the dynamic regulation of PI(3,5)P(2) are linked to human diseases. However, few mechanisms that regulate PI(3,5)P(2) have been identified. Here we report an intramolecular interaction between the yeast Fab1 kinase region and an upstream conserved cysteine-rich (CCR) domain. We identify mutations in the kinase domain that lead to elevated levels of PI(3,5)P(2) and impair the interaction between the kinase and CCR domain. We also identify mutations in the CCR domain that lead to elevated levels of PI(3,5)P(2) Together these findings reveal a regulatory mechanism that involves the CCR domain of Fab1 and contributes to dynamic control of cellular PI(3,5)P(2) synthesis. |Cystine [MESH] |Homeostasis [MESH] |Lipids/physiology [MESH] |Phosphatidylinositol 3-Kinases/metabolism [MESH] |Phosphatidylinositol 4,5-Diphosphate/metabolism [MESH] |Phosphatidylinositol Phosphates/*metabolism/physiology [MESH] |Phosphatidylinositols [MESH] |Phosphorylation [MESH] |Phosphotransferases (Alcohol Group Acceptor)/*metabolism/physiology [MESH] |Protein Domains [MESH] |Saccharomyces cerevisiae Proteins/*metabolism/physiology [MESH] |Saccharomyces cerevisiae/metabolism [MESH]An intramolecular interaction within the lipid kinase Fab1 regulates c(epmc).pdf DeepDyve Pubget Overpricing