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10.1007/978-3-642-41199-1_16 http://scihub22266oqcxt.onion/10.1007/978-3-642-41199-1_16 C4516163!4516163 !24292837     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=24292837 &cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\24292837 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Handb+Exp+Pharmacol 2014 ; 219 (ä): 309-39 Nephropedia Template TP {{tp|p=24292837 |t=2014. Arrestins in apoptosis |pdf=|usr=}}{{24292837 }} gab.com Text Arrestins in apoptosis JO: Handb Exp Pharmacol http://www.kidney.de/pget.php?&tw=1&pmid=24292837 #FOAvip Programmed cell death (apoptosis) is a coordinated set of events eventually leading to the massive activation of specialized proteases (caspases) that cleave numerous substrates, orchestrating fairly uniform biochemical changes than culminate in cellular suicide. Apoptosis can be triggered by a variety of stimuli, from external signals or growth factor withdrawal to intracellular conditions, such as DNA damage or ER stress. Arrestins regulate many signaling cascades involved in life-or-death decisions in the cell, so it is hardly surprising that numerous reports document the effects of ubiquitous nonvisual arrestins on apoptosis under various conditions. Although these findings hardly constitute a coherent picture, with the same arrestin subtypes, sometimes via the same signaling pathways, reported to promote or inhibit cell death, this might reflect real differences in pro- and antiapoptotic signaling in different cells under a variety of conditions. Recent finding suggests that one of the nonvisual subtypes, arrestin-2, is specifically cleaved by caspases. Generated fragment actively participates in the core mechanism of apoptosis: it assists another product of caspase activity, tBID, in releasing cytochrome C from mitochondria. This is the point of no return in committing vertebrate cells to death, and the aspartate where caspases cleave arrestin-2 is evolutionary conserved in vertebrate, but not in invertebrate arrestins. In contrast to wild-type arrestin-2, its caspase-resistant mutant does not facilitate cell death. Twit Text FOAVip Arrestins in apoptosis ????Handb Exp Pharmacol http://www.kidney.de/pget.php?&tw=1&pmid=24292837 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=24292837 #FOAvip English Wikipedia <ref>{{Cite pmid|24292837 }}</ref> Arrestins in apoptosis #MMPMID24292837 Kook S ; Gurevich VV ; Gurevich EV Handb Exp Pharmacol 2014[]; 219 (ä): 309-39 PMID24292837 show ga Programmed cell death (apoptosis) is a coordinated set of events eventually leading to the massive activation of specialized proteases (caspases) that cleave numerous substrates, orchestrating fairly uniform biochemical changes than culminate in cellular suicide. Apoptosis can be triggered by a variety of stimuli, from external signals or growth factor withdrawal to intracellular conditions, such as DNA damage or ER stress. Arrestins regulate many signaling cascades involved in life-or-death decisions in the cell, so it is hardly surprising that numerous reports document the effects of ubiquitous nonvisual arrestins on apoptosis under various conditions. Although these findings hardly constitute a coherent picture, with the same arrestin subtypes, sometimes via the same signaling pathways, reported to promote or inhibit cell death, this might reflect real differences in pro- and antiapoptotic signaling in different cells under a variety of conditions. Recent finding suggests that one of the nonvisual subtypes, arrestin-2, is specifically cleaved by caspases. Generated fragment actively participates in the core mechanism of apoptosis: it assists another product of caspase activity, tBID, in releasing cytochrome C from mitochondria. This is the point of no return in committing vertebrate cells to death, and the aspartate where caspases cleave arrestin-2 is evolutionary conserved in vertebrate, but not in invertebrate arrestins. In contrast to wild-type arrestin-2, its caspase-resistant mutant does not facilitate cell death. |Animals [MESH] |Apoptosis/*physiology [MESH] |Arrestins/*metabolism [MESH] |Caspases/metabolism [MESH] |DNA Damage/physiology [MESH] |Endoplasmic Reticulum Stress/physiology [MESH] |Humans [MESH] |MAP Kinase Signaling System/physiology [MESH] |Signal Transduction/*physiology [MESH] |Tumor Suppressor Protein p53/physiology [MESH]Arrestins in apoptosis (epmc).pdf DeepDyve Pubget Overpricing