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10.1016/j.stemcr.2017.03.023 http://scihub22266oqcxt.onion/10.1016/j.stemcr.2017.03.023 C5425684!5425684!28457890     free     free     free Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Stem+Cell+Reports 2017 ; 8 (5): 1115-23 Nephropedia Template TP {{tp|p=28457890|t=2017. Context-Dependent Functions of NANOG Phosphorylation in Pluripotency and Reprogramming |pdf=|usr=}}{{28457890}} gab.com Text Context-Dependent Functions of NANOG Phosphorylation in Pluripotency and Reprogramming JO: Stem Cell Reports http://www.kidney.de/pget.php?&tw=1&pmid=28457890 #FOAvip The core pluripotency transcription factor NANOG is critical for embryonic stem cell (ESC) self-renewal and somatic cell reprogramming. Although NANOG is phosphorylated at multiple residues, the role of NANOG phosphorylation in ESC self-renewal is incompletely understood, and no information exists regarding its functions during reprogramming. Here we report our findings that NANOG phosphorylation is beneficial, although nonessential, for ESC self-renewal, and that loss of phosphorylation enhances NANOG activity in reprogramming. Mutation of serine 65 in NANOG to alanine (S65A) alone has the most significant impact on increasing NANOG reprogramming capacity. Mechanistically, we find that pluripotency regulators (ESRRB, OCT4, SALL4, DAX1, and TET1) are transcriptionally primed and preferentially associated with NANOG S65A at the protein level due to presumed structural alterations in the N-terminal domain of NANOG. These results demonstrate that a single phosphorylation site serves as a critical interface for controlling context-dependent NANOG functions in pluripotency and reprogramming. Twit Text FOAVip Context-Dependent Functions of NANOG Phosphorylation in Pluripotency and Reprogramming ????Stem Cell Reports http://www.kidney.de/pget.php?&tw=1&pmid=28457890 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28457890 #FOAvip English Wikipedia <ref>{{Cite pmid|28457890}}</ref> Context-Dependent Functions of NANOG Phosphorylation in Pluripotency and Reprogramming #MMPMID28457890 Saunders A; Li D; Faiola F; Huang X; Fidalgo M; Guallar D; Ding J; Yang F; Xu Y; Zhou H; Wang J Stem Cell Reports 2017[May]; 8 (5): 1115-23 PMID28457890show ga The core pluripotency transcription factor NANOG is critical for embryonic stem cell (ESC) self-renewal and somatic cell reprogramming. Although NANOG is phosphorylated at multiple residues, the role of NANOG phosphorylation in ESC self-renewal is incompletely understood, and no information exists regarding its functions during reprogramming. Here we report our findings that NANOG phosphorylation is beneficial, although nonessential, for ESC self-renewal, and that loss of phosphorylation enhances NANOG activity in reprogramming. Mutation of serine 65 in NANOG to alanine (S65A) alone has the most significant impact on increasing NANOG reprogramming capacity. Mechanistically, we find that pluripotency regulators (ESRRB, OCT4, SALL4, DAX1, and TET1) are transcriptionally primed and preferentially associated with NANOG S65A at the protein level due to presumed structural alterations in the N-terminal domain of NANOG. These results demonstrate that a single phosphorylation site serves as a critical interface for controlling context-dependent NANOG functions in pluripotency and reprogramming. äContext-Dependent Functions of NANOG Phosphorylation in Pluripotency a(epmc).pdf DeepDyve Pubget Overpricing