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10.1083/jcb.201609081 http://scihub22266oqcxt.onion/10.1083/jcb.201609081 C5100297!5100297 !27821493     free     free     free Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 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\27821493 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       J+Cell+Biol 2016 ; 215 (3 ): 313-323 Nephropedia Template TP {{tp|p=27821493 |t=2016. Mechanistic insights into mammalian stress granule dynamics |pdf=|usr=}}{{27821493 }} gab.com Text Mechanistic insights into mammalian stress granule dynamics JO: J Cell Biol http://www.kidney.de/pget.php?&tw=1&pmid=27821493 #FOAvip The accumulation of stalled translation preinitiation complexes (PICs) mediates the condensation of stress granules (SGs). Interactions between prion-related domains and intrinsically disordered protein regions found in SG-nucleating proteins promote the condensation of ribonucleoproteins into SGs. We propose that PIC components, especially 40S ribosomes and mRNA, recruit nucleators that trigger SG condensation. With resolution of stress, translation reinitiation reverses this process and SGs disassemble. By cooperatively modulating the assembly and disassembly of SGs, ribonucleoprotein condensation can influence the survival and recovery of cells exposed to unfavorable environmental conditions. Twit Text FOAVip Mechanistic insights into mammalian stress granule dynamics ????J Cell Biol http://www.kidney.de/pget.php?&tw=1&pmid=27821493 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27821493 #FOAvip English Wikipedia <ref>{{Cite pmid|27821493 }}</ref> Mechanistic insights into mammalian stress granule dynamics #MMPMID27821493 Panas MD ; Ivanov P ; Anderson P J Cell Biol 2016[Nov]; 215 (3 ): 313-323 PMID27821493 show ga The accumulation of stalled translation preinitiation complexes (PICs) mediates the condensation of stress granules (SGs). Interactions between prion-related domains and intrinsically disordered protein regions found in SG-nucleating proteins promote the condensation of ribonucleoproteins into SGs. We propose that PIC components, especially 40S ribosomes and mRNA, recruit nucleators that trigger SG condensation. With resolution of stress, translation reinitiation reverses this process and SGs disassemble. By cooperatively modulating the assembly and disassembly of SGs, ribonucleoprotein condensation can influence the survival and recovery of cells exposed to unfavorable environmental conditions. |*Stress, Physiological [MESH] |Animals [MESH] |Cytoplasmic Granules/*metabolism [MESH] |Humans [MESH] |Intrinsically Disordered Proteins/metabolism [MESH] |Mammals/*metabolism [MESH] |Models, Biological [MESH]Mechanistic insights into mammalian stress granule dynamics (epmc).pdf DeepDyve Pubget Overpricing