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10.1267/ahc.17011 http://scihub22266oqcxt.onion/10.1267/ahc.17011 28522883/?report=reader!5433938!28522883     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 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 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 245.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 245.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Acta+Histochem+Cytochem 2017 ; 50 (2): 85-93 Nephropedia Template TP {{tp|p=28522883|t=2017. In Situ Evaluation of Estrogen Receptor Dimers in Breast Carcinoma Cells: Visualization of Protein-Protein Interactions |pdf=|usr=}}{{28522883}} gab.com Text In Situ Evaluation of Estrogen Receptor Dimers in Breast Carcinoma Cells: Visualization of Protein-Protein Interactions JO: Acta Histochem Cytochem http://www.kidney.de/pget.php?&tw=1&pmid=28522883 #FOAvip The estrogen receptor (ER) functions as a dimer and is involved in several different biological functions. However ER dimeric proteins have not been identified by in situ methodologies. Structured illumination microscopy (SIM) has been recently developed, which enabled the localization of protein and protein interaction. Therefore, in this study, we firstly demonstrated that ERs formed both homodimers and heterodimers in breast carcinoma cell lines using Nikon's SIM (N-SIM). ERalpha/alpha homodimers were detected in the nuclei of both ERalpha-positive MCF-7 and T-47D cells; 23.0% and 13.4% of ERalpha proteins formed ERalpha/alpha homodimers, respectively. ERalpha/beta heterodimers were also detected in MCF-7 and T-47D. Approximately 6.6% of both ERalpha and ERbeta1 proteins formed ERalpha/beta1 heterodimers in MCF-7. In addition, 18.1% and 22.4% of ERalpha and ERbeta proteins formed ERalpha/beta2 heterodimers and ERalpha/beta5 heterodimers in MCF-7, respectively. In addition, by using proximity ligation assay (PLA) in MCF-7, estradiol-induced ERalpha/alpha homodimers and ERalpha/beta1 heterodimers were both detected after 15 to 45 min of treatment and at 15 min, respectively. The percentage of total ER proteins could also be determined using N-SIM. By using both methods, it has become possible to evaluate precise localization and ratio of ER dimers among different cell types. Twit Text FOAVip In Situ Evaluation of Estrogen Receptor Dimers in Breast Carcinoma Cells: Visualization of Protein-Protein Interactions ????Acta Histochem Cytochem http://www.kidney.de/pget.php?&tw=1&pmid=28522883 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28522883 #FOAvip English Wikipedia <ref>{{Cite pmid|28522883}}</ref> In Situ Evaluation of Estrogen Receptor Dimers in Breast Carcinoma Cells: Visualization of Protein-Protein Interactions #MMPMID28522883 Iwabuchi E; Miki Y; Ono K; Onodera Y; Sasano H Acta Histochem Cytochem 2017[Apr]; 50 (2): 85-93 PMID28522883show ga The estrogen receptor (ER) functions as a dimer and is involved in several different biological functions. However ER dimeric proteins have not been identified by in situ methodologies. Structured illumination microscopy (SIM) has been recently developed, which enabled the localization of protein and protein interaction. Therefore, in this study, we firstly demonstrated that ERs formed both homodimers and heterodimers in breast carcinoma cell lines using Nikon's SIM (N-SIM). ERalpha/alpha homodimers were detected in the nuclei of both ERalpha-positive MCF-7 and T-47D cells; 23.0% and 13.4% of ERalpha proteins formed ERalpha/alpha homodimers, respectively. ERalpha/beta heterodimers were also detected in MCF-7 and T-47D. Approximately 6.6% of both ERalpha and ERbeta1 proteins formed ERalpha/beta1 heterodimers in MCF-7. In addition, 18.1% and 22.4% of ERalpha and ERbeta proteins formed ERalpha/beta2 heterodimers and ERalpha/beta5 heterodimers in MCF-7, respectively. In addition, by using proximity ligation assay (PLA) in MCF-7, estradiol-induced ERalpha/alpha homodimers and ERalpha/beta1 heterodimers were both detected after 15 to 45 min of treatment and at 15 min, respectively. The percentage of total ER proteins could also be determined using N-SIM. By using both methods, it has become possible to evaluate precise localization and ratio of ER dimers among different cell types. äIn Situ Evaluation of Estrogen Receptor Dimers in Breast Carcinoma Cel(epmc).pdf DeepDyve Pubget Overpricing