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10.1080/15384101.2015.1049778 http://scihub22266oqcxt.onion/10.1080/15384101.2015.1049778 C4613835!4613835!26017022     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       Cell+Cycle 2015 ; 14 (13): 2160-70 Nephropedia Template TP {{tp|p=26017022|t=2015. A novel role for the condensin II complex in cellular senescence |pdf=|usr=}}{{26017022}} gab.com Text A novel role for the condensin II complex in cellular senescence JO: Cell Cycle http://www.kidney.de/pget.php?&tw=1&pmid=26017022 #FOAvip Although cellular senescence is accompanied by global alterations in genome architecture, how the genome is restructured during the senescent processes is not well understood. Here, we show that the hCAP-H2 subunit of the condensin II complex exists as either a full-length protein or an N-terminus truncated variant (?N). While the full-length hCAP-H2 associates with mitotic chromosomes, the ?N variant exists as an insoluble nuclear structure. When overexpressed, both hCAP-H2 isoforms assemble this nuclear architecture and induce senescence-associated heterochromatic foci (SAHF). The hCAP-H2?N protein accumulates as cells approach senescence, and hCAP-H2 knockdown inhibits oncogene-induced senescence. This study identifies a novel mechanism whereby condensin drives senescence via nuclear/genomic reorganization. Twit Text FOAVip A novel role for the condensin II complex in cellular senescence ????Cell Cycle http://www.kidney.de/pget.php?&tw=1&pmid=26017022 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26017022 #FOAvip English Wikipedia <ref>{{Cite pmid|26017022}}</ref> A novel role for the condensin II complex in cellular senescence #MMPMID26017022 Yokoyama Y; Zhu H; Zhang R; Noma Ki Cell Cycle 2015[Jul]; 14 (13): 2160-70 PMID26017022show ga Although cellular senescence is accompanied by global alterations in genome architecture, how the genome is restructured during the senescent processes is not well understood. Here, we show that the hCAP-H2 subunit of the condensin II complex exists as either a full-length protein or an N-terminus truncated variant (?N). While the full-length hCAP-H2 associates with mitotic chromosomes, the ?N variant exists as an insoluble nuclear structure. When overexpressed, both hCAP-H2 isoforms assemble this nuclear architecture and induce senescence-associated heterochromatic foci (SAHF). The hCAP-H2?N protein accumulates as cells approach senescence, and hCAP-H2 knockdown inhibits oncogene-induced senescence. This study identifies a novel mechanism whereby condensin drives senescence via nuclear/genomic reorganization. äA novel role for the condensin II complex in cellular senescence (epmc).pdf DeepDyve Pubget Overpricing