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10.1007/s00294-017-0773-9 http://scihub22266oqcxt.onion/10.1007/s00294-017-0773-9 C5948289!5948289!29098365     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Curr+Genet 2018 ; 64 (3): 535-40 Nephropedia Template TP {{tp|p=29098365|t=2018. Mms1 is an assistant for regulating G-quadruplex DNA structures |pdf=|usr=}}{{29098365}} gab.com Text Mms1 is an assistant for regulating G-quadruplex DNA structures JO: Curr Genet http://www.kidney.de/pget.php?&tw=1&pmid=29098365 #FOAvip The preservation of genome stability is fundamental for every cell. Genomic integrity is constantly challenged. Among those challenges are also non-canonical nucleic acid structures. In recent years, scientists became aware of the impact of G-quadruplex (G4) structures on genome stability. It has been shown that folded G4-DNA structures cause changes in the cell, such as transcriptional up/down-regulation, replication stalling, or enhanced genome instability. Multiple helicases have been identified to regulate G4 structures and by this preserve genome stability. Interestingly, although these helicases are mostly ubiquitous expressed, they show specificity for G4 regulation in certain cellular processes (e.g., DNA replication). To this date, it is not clear how this process and target specificity of helicases are achieved. Recently, Mms1, an ubiquitin ligase complex protein, was identified as a novel G4-DNA-binding protein that supports genome stability by aiding Pif1 helicase binding to these regions. In this perspective review, we discuss the question if G4-DNA interacting proteins are fundamental for helicase function and specificity at G4-DNA structures. Twit Text FOAVip Mms1 is an assistant for regulating G-quadruplex DNA structures ????Curr Genet http://www.kidney.de/pget.php?&tw=1&pmid=29098365 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=29098365 #FOAvip English Wikipedia <ref>{{Cite pmid|29098365}}</ref> Mms1 is an assistant for regulating G-quadruplex DNA structures #MMPMID29098365 Schwindt E; Paeschke K Curr Genet 2018[]; 64 (3): 535-40 PMID29098365show ga The preservation of genome stability is fundamental for every cell. Genomic integrity is constantly challenged. Among those challenges are also non-canonical nucleic acid structures. In recent years, scientists became aware of the impact of G-quadruplex (G4) structures on genome stability. It has been shown that folded G4-DNA structures cause changes in the cell, such as transcriptional up/down-regulation, replication stalling, or enhanced genome instability. Multiple helicases have been identified to regulate G4 structures and by this preserve genome stability. Interestingly, although these helicases are mostly ubiquitous expressed, they show specificity for G4 regulation in certain cellular processes (e.g., DNA replication). To this date, it is not clear how this process and target specificity of helicases are achieved. Recently, Mms1, an ubiquitin ligase complex protein, was identified as a novel G4-DNA-binding protein that supports genome stability by aiding Pif1 helicase binding to these regions. In this perspective review, we discuss the question if G4-DNA interacting proteins are fundamental for helicase function and specificity at G4-DNA structures. äMms1 is an assistant for regulating G-quadruplex DNA structures (epmc).pdf DeepDyve Pubget Overpricing