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10.18632/oncotarget.6520 http://scihub22266oqcxt.onion/10.18632/oncotarget.6520 C4811302!4811302 !26657293     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 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 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 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 243.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 243.2 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\26657293 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Oncotarget 2016 ; 7 (2 ): 2054-69 Nephropedia Template TP {{tp|p=26657293 |t=2016. Human ?-defensin 3 contains an oncolytic motif that binds PI(4,5)P2 to mediate tumour cell permeabilisation |pdf=|usr=}}{{26657293 }} gab.com Text Human -defensin 3 contains an oncolytic motif that binds PI(4,5)P2 to mediate tumour cell permeabilisation JO: Oncotarget http://www.kidney.de/pget.php?&tw=1&pmid=26657293 #FOAvip Cationic antimicrobial peptides (CAPs), including taxonomically diverse defensins, are innate defense molecules that display potent antimicrobial and immunomodulatory activities. Specific CAPs have also been shown to possess anticancer activities; however, their mechanisms of action are not well defined. Recently, the plant defensin NaD1 was shown to induce tumour cell lysis by directly binding to the plasma membrane phosphoinositide, phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2). The NaD1-lipid interaction was structurally defined by X-ray crystallography, with the defensin forming a dimer that binds PI(4,5)P2 via its cationic ?2-?3 loops in a 'cationic grip' conformation. In this study, we show that human ?-defensin 3 (HBD-3) contains a homologous ?2-?3 loop that binds phosphoinositides. The binding of HBD-3 to PI(4,5)P2 was shown to be critical for mediating cytolysis of tumour cells, suggesting a conserved mechanism of action for defensins across diverse species. These data not only identify an evolutionary conservation of CAP structure and function for lipid binding, but also suggest that PIP-binding CAPs could be exploited for novel multifunction therapeutics. Twit Text FOAVip Human -defensin 3 contains an oncolytic motif that binds PI(4,5)P2 to mediate tumour cell permeabilisation ????Oncotarget http://www.kidney.de/pget.php?&tw=1&pmid=26657293 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26657293 #FOAvip English Wikipedia <ref>{{Cite pmid|26657293 }}</ref> Human ?-defensin 3 contains an oncolytic motif that binds PI(4,5)P2 to mediate tumour cell permeabilisation #MMPMID26657293 Phan TK ; Lay FT ; Poon IK ; Hinds MG ; Kvansakul M ; Hulett MD Oncotarget 2016[Jan]; 7 (2 ): 2054-69 PMID26657293 show ga Cationic antimicrobial peptides (CAPs), including taxonomically diverse defensins, are innate defense molecules that display potent antimicrobial and immunomodulatory activities. Specific CAPs have also been shown to possess anticancer activities; however, their mechanisms of action are not well defined. Recently, the plant defensin NaD1 was shown to induce tumour cell lysis by directly binding to the plasma membrane phosphoinositide, phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2). The NaD1-lipid interaction was structurally defined by X-ray crystallography, with the defensin forming a dimer that binds PI(4,5)P2 via its cationic ?2-?3 loops in a 'cationic grip' conformation. In this study, we show that human ?-defensin 3 (HBD-3) contains a homologous ?2-?3 loop that binds phosphoinositides. The binding of HBD-3 to PI(4,5)P2 was shown to be critical for mediating cytolysis of tumour cells, suggesting a conserved mechanism of action for defensins across diverse species. These data not only identify an evolutionary conservation of CAP structure and function for lipid binding, but also suggest that PIP-binding CAPs could be exploited for novel multifunction therapeutics. |Adenosine Triphosphate/metabolism [MESH] |Amino Acid Sequence [MESH] |Apoptosis [MESH] |Blotting, Western [MESH] |Cell Membrane Permeability [MESH] |Cell Membrane/*metabolism [MESH] |Cell Proliferation [MESH] |Flow Cytometry [MESH] |Humans [MESH] |Neoplasms/genetics/metabolism/*pathology [MESH] |Phosphatidylinositol 4,5-Diphosphate/*metabolism [MESH] |Phosphatidylinositols/*metabolism [MESH] |Sequence Homology, Amino Acid [MESH] |Tumor Cells, Cultured [MESH]Human ?-defensin 3 contains an oncolytic motif that binds PI(4,5)P2 to(epmc).pdf DeepDyve Pubget Overpricing