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10.1007/s12195-016-0432-0 http://scihub22266oqcxt.onion/10.1007/s12195-016-0432-0 C4974015!4974015 !27499815     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=27499815 &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 Deprecated: Implicit conversion from float 211.6 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\27499815 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Cell+Mol+Bioeng 2016 ; 9 (2 ): 207-216 Nephropedia Template TP {{tp|p=27499815 |t=2016. LINCing defective nuclear-cytoskeletal coupling and DYT1 dystonia |pdf=|usr=}}{{27499815 }} gab.com Text LINCing defective nuclear-cytoskeletal coupling and DYT1 dystonia JO: Cell Mol Bioeng http://www.kidney.de/pget.php?&tw=1&pmid=27499815 #FOAvip Mechanical forces generated by nuclear-cytoskeletal coupling through the LINC (linker of nucleoskeleton and cytoskeleton) complex, an evolutionarily conserved molecular bridge in the nuclear envelope (NE), are critical for the execution of wholesale nuclear positioning events in migrating and dividing cells, chromosome dynamics during meiosis, and mechanotransduction. LINC complexes consist of outer (KASH (Klarsicht, ANC-1, and Syne homology)) and inner (SUN (Sad1, UNC-84)) nuclear membrane proteins. KASH proteins interact with the cytoskeleton in the cytoplasm and SUN proteins in the perinuclear space of the NE. In the nucleoplasm, SUN proteins interact with A-type nuclear lamins and chromatin-binding proteins. Recent structural insights into the KASH-SUN interaction have generated several questions regarding how LINC complex assembly and function might be regulated within the perinuclear space. Here we discuss potential LINC regulatory mechanisms and focus on the potential role of AAA+ (ATPases associated with various cellular activities) protein, torsinA, as a LINC complex regulator within the NE. We also examine how defects in LINC complex regulation by torsinA may contribute to the pathogenesis of the human neurological movement disorder, DYT1 dystonia. Twit Text FOAVip LINCing defective nuclear-cytoskeletal coupling and DYT1 dystonia ????Cell Mol Bioeng http://www.kidney.de/pget.php?&tw=1&pmid=27499815 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27499815 #FOAvip English Wikipedia <ref>{{Cite pmid|27499815 }}</ref> LINCing defective nuclear-cytoskeletal coupling and DYT1 dystonia #MMPMID27499815 Saunders CA ; Luxton GW Cell Mol Bioeng 2016[Jun]; 9 (2 ): 207-216 PMID27499815 show ga Mechanical forces generated by nuclear-cytoskeletal coupling through the LINC (linker of nucleoskeleton and cytoskeleton) complex, an evolutionarily conserved molecular bridge in the nuclear envelope (NE), are critical for the execution of wholesale nuclear positioning events in migrating and dividing cells, chromosome dynamics during meiosis, and mechanotransduction. LINC complexes consist of outer (KASH (Klarsicht, ANC-1, and Syne homology)) and inner (SUN (Sad1, UNC-84)) nuclear membrane proteins. KASH proteins interact with the cytoskeleton in the cytoplasm and SUN proteins in the perinuclear space of the NE. In the nucleoplasm, SUN proteins interact with A-type nuclear lamins and chromatin-binding proteins. Recent structural insights into the KASH-SUN interaction have generated several questions regarding how LINC complex assembly and function might be regulated within the perinuclear space. Here we discuss potential LINC regulatory mechanisms and focus on the potential role of AAA+ (ATPases associated with various cellular activities) protein, torsinA, as a LINC complex regulator within the NE. We also examine how defects in LINC complex regulation by torsinA may contribute to the pathogenesis of the human neurological movement disorder, DYT1 dystonia. äLINCing defective nuclear-cytoskeletal coupling and DYT1 dystonia (epmc).pdf DeepDyve Pubget Overpricing