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10.4161/19491034.2014.970104 http://scihub22266oqcxt.onion/10.4161/19491034.2014.970104 C4615786!4615786!25482067     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=25482067&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 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Nucleus 2014 ; 5 (6): 499-507 Nephropedia Template TP {{tp|p=25482067|t=2014. PML nuclear bodies: Assembly and oxidative stress-sensitive sumoylation |pdf=|usr=}}{{25482067}} gab.com Text PML nuclear bodies: Assembly and oxidative stress-sensitive sumoylation JO: Nucleus http://www.kidney.de/pget.php?&tw=1&pmid=25482067 #FOAvip PML Nuclear Bodies (NBs) have fascinated cell biologists due to their exquisitely dynamic nature and their involvement in human diseases, notably acute promyelocytic leukemia. NBs, as well as their master organizer - the PML protein - exhibit multiple connections with stress responses. Initially viewed as a tumor suppressor, PML recently re-emerged as a multifaceted protein, capable of controlling numerous aspects of cellular homeostasis. NBs recruit many functionally diverse proteins and function as stress-regulated sumoylation factories. SUMO-initiated partner retention can subsequently facilitate a variety of other post-translational modifications, as well as partner degradation. With this newly elucidated central role of stress-enhanced sumoylation, it should now be possible to build a working model for the different NB-regulated cellular activities. Moreover, pharmacological manipulation of NB formation by interferons or oxidants holds the promise of clearing many undesirable proteins for clinical management of malignant, viral or neurodegenerative diseases. Twit Text FOAVip PML nuclear bodies: Assembly and oxidative stress-sensitive sumoylation ????Nucleus http://www.kidney.de/pget.php?&tw=1&pmid=25482067 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25482067 #FOAvip English Wikipedia <ref>{{Cite pmid|25482067}}</ref> PML nuclear bodies: Assembly and oxidative stress-sensitive sumoylation #MMPMID25482067 Sahin U; de Thé H; Lallemand-Breitenbach V Nucleus 2014[]; 5 (6): 499-507 PMID25482067show ga PML Nuclear Bodies (NBs) have fascinated cell biologists due to their exquisitely dynamic nature and their involvement in human diseases, notably acute promyelocytic leukemia. NBs, as well as their master organizer - the PML protein - exhibit multiple connections with stress responses. Initially viewed as a tumor suppressor, PML recently re-emerged as a multifaceted protein, capable of controlling numerous aspects of cellular homeostasis. NBs recruit many functionally diverse proteins and function as stress-regulated sumoylation factories. SUMO-initiated partner retention can subsequently facilitate a variety of other post-translational modifications, as well as partner degradation. With this newly elucidated central role of stress-enhanced sumoylation, it should now be possible to build a working model for the different NB-regulated cellular activities. Moreover, pharmacological manipulation of NB formation by interferons or oxidants holds the promise of clearing many undesirable proteins for clinical management of malignant, viral or neurodegenerative diseases. äPML nuclear bodies: Assembly and oxidative stress-sensitive sumoylatio(epmc).pdf DeepDyve Pubget Overpricing