@article{graham_barley-maloney_stark_kaur_stolarchuk_sproat_leszczynska_malkiewicz_safwat_mucha_et al._2012, title={Functional Recognition of the Modified Human tRNA (Lys3) (UUU) Anticodon Domain by HIV's Nucleocapsid Protein and a Peptide Mimic (vol 410, pg 698, year 2011)}, volume={420}, number={3}, journal={Journal of Molecular Biology}, author={Graham, W. D. and Barley-Maloney, L. and Stark, C. J. and Kaur, A. and Stolarchuk, C. and Sproat, B. and Leszczynska, G. and Malkiewicz, A. and Safwat, N. and Mucha, P. and et al.}, year={2012}, pages={259–259} } @article{graham_barley-maloney_stark_kaur_stolyarchuk_sproat_leszczynska_malkiewicz_safwat_mucha_et al._2011, title={Functional recognition of the modified human tRNA(UUU)(Lys3) anticodon domain by HIV's nucleocapsid protein and a peptide mimic}, volume={410}, number={4}, journal={Journal of Molecular Biology}, author={Graham, W. D. and Barley-Maloney, L. and Stark, C. J. and Kaur, A. and Stolyarchuk, K. and Sproat, B. and Leszczynska, G. and Malkiewicz, A. and Safwat, N. and Mucha, P. and et al.}, year={2011}, pages={698–715} } @article{safwat_ninomiya-tsuji_gore_miller_2005, title={Transforming growth factor beta-activated kinase 1 is a key mediator of ovine follicle-stimulating hormone beta-subunit expression}, volume={146}, ISSN={["1945-7170"]}, url={http://www.scopus.com/inward/record.url?eid=2-s2.0-26844553319&partnerID=MN8TOARS}, DOI={10.1210/en.2005-0457}, abstractNote={FSH, a key regulator of gonadal function, contains a β-subunit (FSHβ) that is transcriptionally induced by activin, a member of the TGFβ-superfamily. This study used 4.7 kb of the ovine FSHβ-promoter linked to luciferase (oFSHβLuc) plus a well-characterized activin-responsive construct, p3TPLuc, to investigate the hypothesis that Smad3, TGFβ-activated kinase 1 (TAK1), or both cause activin-mediated induction of FSH. Overexpression of either Smad3 or TAK1 induced oFSHβLuc in gonadotrope-derived LβT2 cells as much as activin itself. Induction of p3TPLuc by activin is known to require Smad3 activation in many cell types, and this was true in LβT2 cells, where 10-fold induction by activin (2–8 h after activin treatment) was blocked more than 90% by two dominant negative (DN) inhibitors of Smad3 [DN-Smad3 (3SA) and DN-Smad3 (D407E)]. By contrast, 6.5-fold induction of oFSHβLuc by activin (10–24 h after activin treatment) was not blocked by either DN-Smad inhibitor, suggesting that activation of Smad3 did not trigger induction of oFSHβLuc. By contrast, inhibition of TAK1 by a DN-TAK1 construct led to a 50% decrease in activin-mediated induction of oFSHβLuc, and a specific inhibitor of TAK1 (5Z-7-Oxozeanol) blocked induction by 100%, indicating that TAK1 is necessary for activin induction of oFSHβLuc. Finally, inhibiting p38-MAPK (often activated by TAK1) blocked induction of oFSHβLuc by 60%. In conclusion, the data presented here indicate that activation of TAK1 (and probably p38-MAPK), but not Smad3, is necessary for triggering induction of oFSHβ by activin.}, number={11}, journal={ENDOCRINOLOGY}, author={Safwat, N and Ninomiya-Tsuji, J and Gore, AJ and Miller, WL}, year={2005}, month={Nov}, pages={4814–4824} } @article{wu_su_safwat_sebastian_miller_2004, title={Rapid, efficient isolation of murine gonadotropes and their use in revealing control of follicle-stimulating hormone by paracrine pituitary factors}, volume={145}, ISSN={["1945-7170"]}, DOI={10.1210/en.2004-0257}, abstractNote={FSH and LH are produced only in gonadotropes, which are reported to comprise 3-12% of mammalian pituitaries. Factors made within the pituitary are powerful regulators of FSH and also influence LH expression, but their identities and cellular origins are unknown because it is impossible to isolate and individually analyze different pituitary cell types. In this study FSH-producing gonadotropes were specifically tagged in vivo with a transgenic cell surface antigen (H-2Kk) so they could be purified in vitro using paramagnetic anti-H-2Kk microbeads. After enzymatic dispersion of pituitary cells, it took 1 h or less to extract 55 +/- 5% of FSH-producing gonadotropes at 95 +/- 0.5% purity, as judged by immunostaining for FSH or prolactin. Although this procedure selected for FSH expression, the isolated gonadotropes were also enriched 22-fold for LH-containing cells. For studies aimed at understanding factors that control FSH transcription, the purified gonadotropes were treated with activin A, which increased FSH expression 480% above basal levels (d 3 of culture). Coincubation of purified gonadotropes with pituitary nongonadotropes increased FSH expression 800% (d 3 of culture). Follistatin, an activin-binding protein, decreased FSH expression 35-50%, suggesting that gonadotropes make some activin and/or other follistatin-sensitive molecule(s) that induce FSH. These data show that paracrine factors from pituitary nongonadotropes can play a major role in controlling FSHbeta at the pituitary level. The study presented here describes a rapid, reliable, and efficient method for isolating any specialized cell type, including all cells that produce endocrine hormones.}, number={12}, journal={ENDOCRINOLOGY}, author={Wu, JC and Su, P and Safwat, NW and Sebastian, J and Miller, WL}, year={2004}, month={Dec}, pages={5832–5839} }