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10.4161/23723548.2014.965638 http://scihub22266oqcxt.onion/10.4161/23723548.2014.965638 C4905023!4905023 !27308415     free     free     free Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\27308415 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Mol+Cell+Oncol 2015 ; 2 (2 ): e965638 Nephropedia Template TP {{tp|p=27308415 |t=2015. Necroptosis: Fifty shades of RIPKs |pdf=|usr=}}{{27308415 }} gab.com Text Necroptosis: Fifty shades of RIPKs JO: Mol Cell Oncol http://www.kidney.de/pget.php?&tw=1&pmid=27308415 #FOAvip Apoptosis and necroptosis are 2 major, yet distinct, forms of regulated cell death. Whereas apoptosis requires caspase protease function, necroptosis requires activation of the receptor interacting protein kinases 1 (RIPK1) and RIPK3. Following activation, RIPK3 phosphorylates mixed-lineage kinase domain-like (MLKL), leading to cell death. Apoptosis and necroptosis are deeply intertwined such that a given death stimulus can often engage either form of cell death. Recent studies published in Cell Death and Differentiation by the Han, Oberst, and Vaux laboratories provide exciting new insights into necroptosis and how it interconnects with apoptosis. As we will discuss, their findings address key questions including: How does a cell choose between apoptosis or necroptosis? How can RIPK3 also induce apoptosis? What is the nature of the RIPK1-3 signaling cascade leading to necroptosis? Finally, data from the Oberst and Han groups strongly argue that RIPK1 is not only involved in executing necroptosis, but also protects against this process in some settings. Twit Text FOAVip Necroptosis: Fifty shades of RIPKs ????Mol Cell Oncol http://www.kidney.de/pget.php?&tw=1&pmid=27308415 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27308415 #FOAvip English Wikipedia <ref>{{Cite pmid|27308415 }}</ref> Necroptosis: Fifty shades of RIPKs #MMPMID27308415 Ichim G ; Tait SW Mol Cell Oncol 2015[Apr]; 2 (2 ): e965638 PMID27308415 show ga Apoptosis and necroptosis are 2 major, yet distinct, forms of regulated cell death. Whereas apoptosis requires caspase protease function, necroptosis requires activation of the receptor interacting protein kinases 1 (RIPK1) and RIPK3. Following activation, RIPK3 phosphorylates mixed-lineage kinase domain-like (MLKL), leading to cell death. Apoptosis and necroptosis are deeply intertwined such that a given death stimulus can often engage either form of cell death. Recent studies published in Cell Death and Differentiation by the Han, Oberst, and Vaux laboratories provide exciting new insights into necroptosis and how it interconnects with apoptosis. As we will discuss, their findings address key questions including: How does a cell choose between apoptosis or necroptosis? How can RIPK3 also induce apoptosis? What is the nature of the RIPK1-3 signaling cascade leading to necroptosis? Finally, data from the Oberst and Han groups strongly argue that RIPK1 is not only involved in executing necroptosis, but also protects against this process in some settings. äNecroptosis: Fifty shades of RIPKs (epmc).pdf DeepDyve Pubget Overpricing