메뉴 건너뛰기




Volumn 17, Issue 12, 2016, Pages 783-797

Nuclear receptors outside the nucleus: extranuclear signalling by steroid receptors

Author keywords

[No Author keywords available]

Indexed keywords

ANDROGEN RECEPTOR; CELL NUCLEUS RECEPTOR; ESTROGEN RECEPTOR; PROGESTERONE RECEPTOR; STEROID RECEPTOR; VITAMIN D RECEPTOR; CELL RECEPTOR;

EID: 84991030712     PISSN: 14710072     EISSN: 14710080     Source Type: Journal    
DOI: 10.1038/nrm.2016.122     Document Type: Review
Times cited : (221)

References (120)
  • 1
    • 1542314421 scopus 로고    scopus 로고
    • Molecular mechanisms, physiological consequences and pharmacological implications of estrogen receptor action
    • Barkhem T, Nilsson S, & Gustafsson J. A. Molecular mechanisms, physiological consequences and pharmacological implications of estrogen receptor action. Am. J. Pharmacogenomics 4, 19-28 (2004).
    • (2004) Am. J. Pharmacogenomics , vol.4 , pp. 19-28
    • Barkhem, T.1    Nilsson, S.2    Gustafsson, J.A.3
  • 2
    • 0000221213 scopus 로고
    • Stress and the general adaptation syndrome
    • Selye H. Stress and the general adaptation syndrome. Br. Med. J. 1, 1383-1392 (1950).
    • (1950) Br. Med. J. , vol.1 , pp. 1383-1392
    • Selye, H.1
  • 3
    • 0017804115 scopus 로고
    • Hepatic intracellular distribution of pregnenolone 16α carbonitrile and its influence on adenyl cyclase activity in rat liver cells
    • Lykissas E. D, Kourounakis P, & Selye H. Hepatic intracellular distribution of pregnenolone 16α carbonitrile and its influence on adenyl cyclase activity in rat liver cells. Res. Commun. Chem. Pathol. Pharmacol. 19, 173-176 (1978).
    • (1978) Res. Commun. Chem. Pathol. Pharmacol , vol.19 , pp. 173-176
    • Lykissas, E.D.1    Kourounakis, P.2    Selye, H.3
  • 4
    • 26444587598 scopus 로고
    • Early effects of estradiol and cortisol on water and electrolyte shifts in the uterus of the immature rat
    • Spaziani E, & Szego C. M. Early effects of estradiol and cortisol on water and electrolyte shifts in the uterus of the immature rat. Am. J. Physiol. 197, 355-359 (1959).
    • (1959) Am. J. Physiol , vol.197 , pp. 355-359
    • Spaziani, E.1    Szego, C.M.2
  • 5
    • 0014140501 scopus 로고
    • Adenosine 3, 5 monophosphate in rat uterus: Acute elevation by estrogen
    • Szego C. M, & Davis J. S. Adenosine 3?, 5? monophosphate in rat uterus: acute elevation by estrogen. Proc. Natl Acad. Sci. USA 58, 1711-1718 (1967).
    • (1967) Proc. Natl Acad. Sci. USA , vol.58 , pp. 1711-1718
    • Szego, C.M.1    Davis, J.S.2
  • 6
    • 0017354142 scopus 로고
    • Specific binding sites for oestrogen at the outer surfaces of isolated endometrial cells
    • Pietras R. J, & Szego C. M. Specific binding sites for oestrogen at the outer surfaces of isolated endometrial cells. Nature 265, 69-72 (1977).
    • (1977) Nature , vol.265 , pp. 69-72
    • Pietras, R.J.1    Szego, C.M.2
  • 7
    • 0035869056 scopus 로고    scopus 로고
    • BRI1 is a critical component of a plasma-membrane receptor for plant steroids
    • Wang Z. Y, Seto H, Fujioka S, Yoshida S, & Chory J. BRI1 is a critical component of a plasma-membrane receptor for plant steroids. Nature 410, 380-383 (2001).
    • (2001) Nature , vol.410 , pp. 380-383
    • Wang, Z.Y.1    Seto, H.2    Fujioka, S.3    Yoshida, S.4    Chory, J.5
  • 8
    • 37349081370 scopus 로고    scopus 로고
    • Extranuclear steroid receptors: Nature and actions
    • Hammes S. R, & Levin E. R. Extranuclear steroid receptors: nature and actions. Endocr. Rev. 28, 726-741 (2007).
    • (2007) Endocr. Rev , vol.28 , pp. 726-741
    • Hammes, S.R.1    Levin, E.R.2
  • 9
    • 84863545530 scopus 로고    scopus 로고
    • Paxillin mediates extranuclear and intranuclear signaling in prostate cancer proliferation
    • Sen A, et al. Paxillin mediates extranuclear and intranuclear signaling in prostate cancer proliferation. J. Clin. Invest. 122, 2469-2481 (2012).
    • (2012) J. Clin. Invest , vol.122 , pp. 2469-2481
    • Sen, A.1
  • 10
    • 77956555910 scopus 로고    scopus 로고
    • Paxillin regulates androgen-And epidermal growth factor-induced MAPK signaling and cell proliferation in prostate cancer cells
    • Sen A, et al. Paxillin regulates androgen-And epidermal growth factor-induced MAPK signaling and cell proliferation in prostate cancer cells. J. Biol. Chem. 285, 28787-28795 (2010).
    • (2010) J. Biol. Chem , vol.285 , pp. 28787-28795
    • Sen, A.1
  • 11
    • 0034675994 scopus 로고    scopus 로고
    • Steroid-induced androgen receptor-oestradiol receptor β-Src complex triggers prostate cancer cell proliferation
    • Migliaccio A, et al. Steroid-induced androgen receptor-oestradiol receptor β-Src complex triggers prostate cancer cell proliferation. EMBO J. 19, 5406-5417 (2000).
    • (2000) EMBO J. , vol.19 , pp. 5406-5417
    • Migliaccio, A.1
  • 12
    • 0032036584 scopus 로고    scopus 로고
    • Activation of the Src/p21ras/Erk pathway by progesterone receptor via cross-Talk with estrogen receptor
    • Migliaccio A, et al. Activation of the Src/p21ras/Erk pathway by progesterone receptor via cross-Talk with estrogen receptor. EMBO J. 17, 2008-2018 (1998).
    • (1998) EMBO J. , vol.17 , pp. 2008-2018
    • Migliaccio, A.1
  • 13
    • 85028266773 scopus 로고    scopus 로고
    • Progesterone receptor B enhances estrogen responsiveness of breast cancer cells via scaffolding PELP1-And estrogen receptor-containing transcription complexes
    • Daniel A. R, et al. Progesterone receptor B enhances estrogen responsiveness of breast cancer cells via scaffolding PELP1-And estrogen receptor-containing transcription complexes. Oncogene 34, 506-515 (2015).
    • (2015) Oncogene , vol.34 , pp. 506-515
    • Daniel, A.R.1
  • 15
    • 84892495900 scopus 로고    scopus 로고
    • Minireview: Dynamic structures of nuclear hormone receptors: New promises and challenges
    • Simons S. S. Jr, Edwards D. P, & Kumar R. Minireview: dynamic structures of nuclear hormone receptors: new promises and challenges. Mol. Endocrinol. 28, 173-182 (2014).
    • (2014) Mol. Endocrinol , vol.28 , pp. 173-182
    • Simons, S.S.1    Edwards, D.P.2    Kumar, R.3
  • 16
    • 79953300720 scopus 로고    scopus 로고
    • Selective mutations in estrogen receptor α D domain alters nuclear translocation and non-estrogen response element gene regulatory mechanisms
    • Burns K. A, Li Y, Arao Y, Petrovich R. M, & Korach K. S. Selective mutations in estrogen receptor α D domain alters nuclear translocation and non-estrogen response element gene regulatory mechanisms. J. Biol. Chem. 286, 12640-12649 (2011).
    • (2011) J. Biol. Chem , vol.286 , pp. 12640-12649
    • Burns, K.A.1    Li, Y.2    Arao, Y.3    Petrovich, R.M.4    Korach, K.S.5
  • 17
    • 0032446607 scopus 로고    scopus 로고
    • The structural basis of estrogen receptor/coactivator recognition and the antagonism of this interaction by tamoxifen
    • Shiau A. K, et al. The structural basis of estrogen receptor/coactivator recognition and the antagonism of this interaction by tamoxifen. Cell 95, 927-937 (1998).
    • (1998) Cell , vol.95 , pp. 927-937
    • Shiau, A.K.1
  • 18
    • 0027429548 scopus 로고
    • Alteration of reproductive function but not prenatal sexual development after insertional disruption of the mouse estrogen receptor gene
    • Lubahn D. B, et al. Alteration of reproductive function but not prenatal sexual development after insertional disruption of the mouse estrogen receptor gene. Proc. Natl Acad. Sci. USA 90, 11162-11166 (1993).
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 11162-11166
    • Lubahn, D.B.1
  • 19
    • 0029115517 scopus 로고
    • Mice lacking progesterone receptor exhibit pleiotropic reproductive abnormalities
    • Lydon J. P, et al. Mice lacking progesterone receptor exhibit pleiotropic reproductive abnormalities. Genes Dev. 9, 2266-2278 (1995).
    • (1995) Genes Dev , vol.9 , pp. 2266-2278
    • Lydon, J.P.1
  • 20
    • 0028925081 scopus 로고
    • Membrane estrogen receptors identified by multiple antibody labeling and impeded-ligand binding
    • Pappas T. C, Gametchu B, & Watson C. S. Membrane estrogen receptors identified by multiple antibody labeling and impeded-ligand binding. FASEB J. 9, 404-410 (1995).
    • (1995) FASEB J. , vol.9 , pp. 404-410
    • Pappas, T.C.1    Gametchu, B.2    Watson, C.S.3
  • 21
    • 0033304691 scopus 로고    scopus 로고
    • Estrogen receptor-α detected on the plasma membrane of aldehyde-fixed GH3/B6/F10 rat pituitary tumor cells by enzyme-linked immunocytochemistry
    • Norfleet A. M, Thomas M. L, Gametchu B, & Watson C. S. Estrogen receptor-α detected on the plasma membrane of aldehyde-fixed GH3/B6/F10 rat pituitary tumor cells by enzyme-linked immunocytochemistry. Endocrinology 140, 3805-3814 (1999).
    • (1999) Endocrinology , vol.140 , pp. 3805-3814
    • Norfleet, A.M.1    Thomas, M.L.2    Gametchu, B.3    Watson, C.S.4
  • 22
    • 0001548401 scopus 로고    scopus 로고
    • Cell membrane and nuclear estrogen receptors (ERs) originate from a single transcript: Studies of ERα and ERβ expressed in Chinese hamster ovary cells
    • Razandi M, Pedram A, Greene G. L, & Levin E. R. Cell membrane and nuclear estrogen receptors (ERs) originate from a single transcript: studies of ERα and ERβ expressed in Chinese hamster ovary cells. Mol. Endocrinol. 13, 307-319 (1999).
    • (1999) Mol. Endocrinol , vol.13 , pp. 307-319
    • Razandi, M.1    Pedram, A.2    Greene, G.L.3    Levin, E.R.4
  • 23
    • 33747841976 scopus 로고    scopus 로고
    • Nature of functional estrogen receptors at the plasma membrane
    • Pedram A, Razandi M, & Levin E. R. Nature of functional estrogen receptors at the plasma membrane. Mol. Endocrinol. 20, 1996-2009 (2006).
    • (2006) Mol. Endocrinol , vol.20 , pp. 1996-2009
    • Pedram, A.1    Razandi, M.2    Levin, E.R.3
  • 24
    • 0037174675 scopus 로고    scopus 로고
    • Reversal of bone loss in mice by nongenotropic signaling of sex steroids
    • Kousteni S, et al. Reversal of bone loss in mice by nongenotropic signaling of sex steroids. Science 298, 843-846 (2002).
    • (2002) Science , vol.298 , pp. 843-846
    • Kousteni, S.1
  • 25
    • 0037446887 scopus 로고    scopus 로고
    • Plasma membrane localization and function of the estrogen receptor α variant (ER46) in human endothelial cells
    • Li L, Haynes M. P, & Bender J. R. Plasma membrane localization and function of the estrogen receptor α variant (ER46) in human endothelial cells. Proc. Natl Acad. Sci. USA 100, 4807-4812 (2003).
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 4807-4812
    • Li, L.1    Haynes, M.P.2    Bender, J.R.3
  • 26
    • 33745160700 scopus 로고    scopus 로고
    • A variant of estrogen receptor-α hER α36: Transduction of estrogen-And antiestrogen-dependent membrane-initiated mitogenic signaling
    • Wang Z, et al. A variant of estrogen receptor-α, hER α36: transduction of estrogen-And antiestrogen-dependent membrane-initiated mitogenic signaling. Proc. Natl Acad. Sci. USA 103, 9063-9068 (2006).
    • (2006) Proc Natl Acad. Sci. USA , vol.103 , pp. 9063-9068
    • Wang, Z.1
  • 27
    • 0034783960 scopus 로고    scopus 로고
    • Mechanisms of estrogen action
    • Nilsson S, et al. Mechanisms of estrogen action. Physiol. Rev. 81, 1535-1565 (2001).
    • (2001) Physiol. Rev , vol.81 , pp. 1535-1565
    • Nilsson, S.1
  • 28
    • 0031785733 scopus 로고    scopus 로고
    • Differentially expressed messenger RNA isoforms of the human estrogen receptor-α gene are generated by alternative splicing and promoter usage
    • Flouriot G, Griffin C, Kenealy M, Sonntag-Buck V, & Gannon F. Differentially expressed messenger RNA isoforms of the human estrogen receptor-α gene are generated by alternative splicing and promoter usage. Mol. Endocrinol. 12, 1939-1954 (1998).
    • (1998) Mol. Endocrinol , vol.12 , pp. 1939-1954
    • Flouriot, G.1    Griffin, C.2    Kenealy, M.3    Sonntag-Buck, V.4    Gannon, F.5
  • 29
    • 34547928773 scopus 로고    scopus 로고
    • A conserved mechanism for steroid receptor translocation to the plasma membrane
    • Pedram A, et al. A conserved mechanism for steroid receptor translocation to the plasma membrane. J. Biol. Chem. 282, 22278-22288 (2007).
    • (2007) J. Biol Chem , vol.282 , pp. 22278-22288
    • Pedram, A.1
  • 30
    • 0035923642 scopus 로고    scopus 로고
    • Evidence that androgens are the primary steroids produced by Xenopus laevis ovaries and may signal through the classical androgen receptor to promote oocyte maturation
    • Lutz L. B, et al. Evidence that androgens are the primary steroids produced by Xenopus laevis ovaries and may signal through the classical androgen receptor to promote oocyte maturation. Proc. Natl Acad. Sci. USA 98, 13728-13733 (2001).
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 13728-13733
    • Lutz, L.B.1
  • 31
    • 0034731406 scopus 로고    scopus 로고
    • G protein βγ subunits inhibit nongenomic progesterone-induced signaling and maturation in Xenopus laevis oocytes. Evidence for a release of inhibition mechanism for cell cycle progression
    • Lutz L. B, Kim B, Jahani D, & Hammes S. R. G protein βγ subunits inhibit nongenomic progesterone-induced signaling and maturation in Xenopus laevis oocytes. Evidence for a release of inhibition mechanism for cell cycle progression. J. Biol. Chem. 275, 41512-41520 (2000).
    • (2000) J. Biol. Chem , vol.275 , pp. 41512-41520
    • Lutz, L.B.1    Kim, B.2    Jahani, D.3    Hammes, S.R.4
  • 32
    • 33845967099 scopus 로고    scopus 로고
    • Testosterone and progesterone rapidly attenuate plasma membrane Gβγ-mediated signaling in Xenopus laevis oocytes by signaling through classical steroid receptors
    • Evaul K, Jamnongjit M, Bhagavath B, & Hammes S. R. Testosterone and progesterone rapidly attenuate plasma membrane Gβγ-mediated signaling in Xenopus laevis oocytes by signaling through classical steroid receptors. Mol. Endocrinol. 21, 186-196 (2007).
    • (2007) Mol. Endocrinol , vol.21 , pp. 186-196
    • Evaul, K.1    Jamnongjit, M.2    Bhagavath, B.3    Hammes, S.R.4
  • 33
    • 77954828598 scopus 로고    scopus 로고
    • Granulosa cell-specific androgen receptors are critical regulators of ovarian development and function
    • Sen A, & Hammes S. R. Granulosa cell-specific androgen receptors are critical regulators of ovarian development and function. Mol. Endocrinol. 24, 1393-1403 (2010).
    • (2010) Mol. Endocrinol , vol.24 , pp. 1393-1403
    • Sen, A.1    Hammes, S.R.2
  • 34
    • 84896875131 scopus 로고    scopus 로고
    • Androgens regulate ovarian follicular development by increasing follicle stimulating hormone receptor and microRNA 125b expression
    • Sen A, et al. Androgens regulate ovarian follicular development by increasing follicle stimulating hormone receptor and microRNA 125b expression. Proc. Natl Acad. Sci. USA 111, 3008-3013 (2014).
    • (2014) Proc. Natl Acad. Sci. USA , vol.111 , pp. 3008-3013
    • Sen, A.1
  • 35
    • 0037371863 scopus 로고    scopus 로고
    • Two domains of the progesterone receptor interact with the estrogen receptor and are required for progesterone activation of the c Src/Erk pathway in mammalian cells
    • Ballare C, et al. Two domains of the progesterone receptor interact with the estrogen receptor and are required for progesterone activation of the c Src/Erk pathway in mammalian cells. Mol. Cell. Biol. 23, 1994-2008 (2003).
    • (2003) Mol. Cell. Biol , vol.23 , pp. 1994-2008
    • Ballare, C.1
  • 36
    • 0034852802 scopus 로고    scopus 로고
    • Progesterone receptor contains a proline-rich motif that directly interacts with SH3 domains and activates c Src family tyrosine kinases
    • Boonyaratanakornkit V, et al. Progesterone receptor contains a proline-rich motif that directly interacts with SH3 domains and activates c Src family tyrosine kinases. Mol. Cell 8, 269-280 (2001).
    • (2001) Mol. Cell , vol.8 , pp. 269-280
    • Boonyaratanakornkit, V.1
  • 37
    • 2442624604 scopus 로고    scopus 로고
    • Ribozyme knockdown functionally links a 1, 25(OH)2D3 membrane binding protein (1, 25D3 MARRS) and phosphate uptake in intestinal cells
    • Nemere I, et al. Ribozyme knockdown functionally links a 1, 25(OH)2D3 membrane binding protein (1, 25D3 MARRS) and phosphate uptake in intestinal cells. Proc. Natl Acad. Sci. USA 101, 7392-7397 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 7392-7397
    • Nemere, I.1
  • 38
    • 68849103260 scopus 로고    scopus 로고
    • The Vitamin D sterol-Vitamin D receptor ensemble model offers unique insights into both genomic and rapid-response signaling
    • Mizwicki M. T, & Norman A. W. The vitamin D sterol-vitamin D receptor ensemble model offers unique insights into both genomic and rapid-response signaling. Sci. Signal. 2, re4 (2009).
    • (2009) Sci. Signal , vol.2 , pp. re4
    • Mizwicki, M.T.1    Norman, A.W.2
  • 39
    • 84901202692 scopus 로고    scopus 로고
    • Nongenomic thyroid hormone signaling occurs through a plasma membrane-localized receptor
    • Kalyanaraman H, et al. Nongenomic thyroid hormone signaling occurs through a plasma membrane-localized receptor. Sci. Signal. 7, ra48 (2014).
    • (2014) Sci. Signal , vol.7 , pp. ra48
    • Kalyanaraman, H.1
  • 40
    • 84907042872 scopus 로고    scopus 로고
    • A rapid cytoplasmic mechanism for PI3 kinase regulation by the nuclear thyroid hormone receptor, TRβ, and genetic evidence for its role in the maturation of mouse hippocampal synapses in vivo
    • Martin N. P, et al. A rapid cytoplasmic mechanism for PI3 kinase regulation by the nuclear thyroid hormone receptor, TRβ, and genetic evidence for its role in the maturation of mouse hippocampal synapses in vivo. Endocrinology 155 3713-3724 (2014).
    • (2014) Endocrinology , vol.155 , pp. 3713-3724
    • Martin, N.P.1
  • 41
    • 0033780783 scopus 로고    scopus 로고
    • Estrogen-induced activation of Erk 1 and Erk 2 requires the G protein-coupled receptor homolog GPR30, and occurs via trans-Activation of the epidermal growth factor receptor through release of HB EGF
    • Filardo E. J, Quinn J. A, Bland K. I, & Frackelton A. R. Jr. Estrogen-induced activation of Erk 1 and Erk 2 requires the G protein-coupled receptor homolog, GPR30, and occurs via trans-Activation of the epidermal growth factor receptor through release of HB EGF. Mol. Endocrinol. 14, 1649-1660 (2000).
    • (2000) Mol. Endocrinol , vol.14 , pp. 1649-1660
    • Filardo, E.J.1    Quinn, J.A.2    Bland, K.I.3    Frackelton, A.R.4
  • 42
    • 12344307170 scopus 로고    scopus 로고
    • Identity of an estrogen membrane receptor coupled to a G protein in human breast cancer cells
    • Thomas P, Pang Y, Filardo E. J, & Dong J. Identity of an estrogen membrane receptor coupled to a G protein in human breast cancer cells. Endocrinology 146, 624-632 (2005).
    • (2005) Endocrinology , vol.146 , pp. 624-632
    • Thomas, P.1    Pang, Y.2    Filardo, E.J.3    Dong, J.4
  • 43
    • 14844343093 scopus 로고    scopus 로고
    • A transmembrane intracellular estrogen receptor mediates rapid cell signaling
    • Revankar C. M, Cimino D. F, Sklar L. A, Arterburn J. B, & Prossnitz E. R. A transmembrane intracellular estrogen receptor mediates rapid cell signaling. Science 307 1625-1630 (2005).
    • (2005) Science , vol.307 , pp. 1625-1630
    • Revankar, C.M.1    Cimino, D.F.2    Sklar, L.A.3    Arterburn, J.B.4    Prossnitz, E.R.5
  • 44
    • 53249107839 scopus 로고    scopus 로고
    • G protein-coupled receptor 30 localizes to the endoplasmic reticulum and is not activated by estradiol
    • Otto C, et al. G protein-coupled receptor 30 localizes to the endoplasmic reticulum and is not activated by estradiol. Endocrinology 149 4846-4856 (2008).
    • (2008) Endocrinology , vol.149 , pp. 4846-4856
    • Otto, C.1
  • 45
    • 63849242931 scopus 로고    scopus 로고
    • Expression pattern of G protein-coupled receptor 30 in LacZ reporter mice
    • Isensee J, et al. Expression pattern of G protein-coupled receptor 30 in LacZ reporter mice. Endocrinology 150, 1722-1730 (2009).
    • (2009) Endocrinology , vol.150 , pp. 1722-1730
    • Isensee, J.1
  • 46
    • 58149512521 scopus 로고    scopus 로고
    • GPR30 does not mediate estrogenic responses in reproductive organs in mice
    • Otto C, et al. GPR30 does not mediate estrogenic responses in reproductive organs in mice. Biol. Reprod. 80, 34-41 (2009).
    • (2009) Biol. Reprod , vol.80 , pp. 34-41
    • Otto, C.1
  • 47
    • 33847755409 scopus 로고    scopus 로고
    • G protein-coupled receptor 30 (GPR30) mediates gene expression changes and growth response to 17β estradiol and selective GPR30 ligand G-1 in ovarian cancer cells
    • Albanito L, et al. G protein-coupled receptor 30 (GPR30) mediates gene expression changes and growth response to 17β estradiol and selective GPR30 ligand G-1 in ovarian cancer cells. Cancer Res. 67, 1859-1866 (2007).
    • (2007) Res C. , vol.67 , pp. 1859-1866
    • Albanito, L.1
  • 48
    • 50649101049 scopus 로고    scopus 로고
    • Nuclear and extranuclear pathway inputs in the regulation of global gene expression by estrogen receptors
    • Madak-Erdogan Z, et al. Nuclear and extranuclear pathway inputs in the regulation of global gene expression by estrogen receptors. Mol. Endocrinol. 22, 2116-2127 (2008).
    • (2008) Mol. Endocrinol , vol.22 , pp. 2116-2127
    • Madak-Erdogan, Z.1
  • 49
    • 77951214876 scopus 로고    scopus 로고
    • Estradiol induces export of sphingosine 1 phosphate from breast cancer cells via ABCC1 and ABCG2
    • Takabe K, et al. Estradiol induces export of sphingosine 1 phosphate from breast cancer cells via ABCC1 and ABCG2. J. Biol. Chem. 285, 10477-10486 (2010).
    • (2010) J. Biol. Chem , vol.285 , pp. 10477-10486
    • Takabe, K.1
  • 50
    • 84949591872 scopus 로고    scopus 로고
    • The G protein coupled estrogen receptor, GPER: The inside and inside-out story
    • Gaudet H. M, Cheng S. B, Christensen E. M, & Filardo E. J. The G protein coupled estrogen receptor, GPER: the inside and inside-out story. Mol. Cell. Endocrinol. 3, 207-219 (2015).
    • (2015) Mol. Cell. Endocrinol , vol.3 , pp. 207-219
    • Gaudet, H.M.1    Cheng, S.B.2    Christensen, E.M.3    Filardo, E.J.4
  • 51
    • 33845483366 scopus 로고    scopus 로고
    • Progesterone regulation of human granulosa/luteal cell viability by an RU486 independent mechanism
    • Engmann L, Losel R, Wehling M, & Peluso J. J. Progesterone regulation of human granulosa/luteal cell viability by an RU486 independent mechanism. J. Clin. Endocrinol. Metab. 91, 4962-4968 (2006).
    • (2006) J. Clin. Endocrinol. Metab , vol.91 , pp. 4962-4968
    • Engmann, L.1    Losel, R.2    Wehling, M.3    Peluso, J.J.4
  • 52
    • 84919460145 scopus 로고    scopus 로고
    • Progesterone receptor membrane component 1 deficiency attenuates growth while promoting chemosensitivity of human endometrial xenograft tumors
    • Friel A. M, et al. Progesterone receptor membrane component 1 deficiency attenuates growth while promoting chemosensitivity of human endometrial xenograft tumors. Cancer Lett. 356, 434-442 (2015).
    • (2015) Cancer Lett , vol.356 , pp. 434-442
    • Friel, A.M.1
  • 53
    • 84956666572 scopus 로고    scopus 로고
    • Progesterone receptor membrane component 1 regulates hepcidin biosynthesis
    • Li X, et al. Progesterone receptor membrane component 1 regulates hepcidin biosynthesis. J. Clin. Invest. 126, 389-401 (2016).
    • (2016) J. Clin. Invest , vol.126 , pp. 389-401
    • Li, X.1
  • 54
    • 0344885580 scopus 로고    scopus 로고
    • Identification, classification, and partial characterization of genes in humans and other vertebrates homologous to a fish membrane progestin receptor
    • Zhu Y, Bond J, & Thomas P. Identification, classification, and partial characterization of genes in humans and other vertebrates homologous to a fish membrane progestin receptor. Proc. Natl Acad. Sci. USA 100, 2237-2242 (2003).
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 2237-2242
    • Zhu, Y.1    Bond, J.2    Thomas, P.3
  • 55
    • 0344885581 scopus 로고    scopus 로고
    • Cloning, expression, and characterization of a membrane progestin receptor and evidence it is an intermediary in meiotic maturation of fish oocytes
    • Zhu Y, Rice C. D, Pang Y, Pace M, & Thomas P. Cloning, expression, and characterization of a membrane progestin receptor and evidence it is an intermediary in meiotic maturation of fish oocytes. Proc. Natl Acad. Sci. USA 100, 2231-2236 (2003).
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 2231-2236
    • Zhu, Y.1    Rice, C.D.2    Pang, Y.3    Pace, M.4    Thomas, P.5
  • 56
    • 67651146633 scopus 로고    scopus 로고
    • Progesterone receptor A (PRA) and PRB-independent effects of progesterone on gonadotropin-releasing hormone release
    • Sleiter N, et al. Progesterone receptor A (PRA) and PRB-independent effects of progesterone on gonadotropin-releasing hormone release. Endocrinology 150, 3833-3844 (2009).
    • (2009) Endocrinology , vol.150 , pp. 3833-3844
    • Sleiter, N.1
  • 57
    • 84948973471 scopus 로고    scopus 로고
    • Structural and functional evidence for testosterone activation of GPRC6A in peripheral tissues
    • Pi M, et al. Structural and functional evidence for testosterone activation of GPRC6A in peripheral tissues. Mol. Endocrinol. 29, 1759-1773 (2015).
    • (2015) Mol. Endocrinol , vol.29 , pp. 1759-1773
    • Pi, M.1
  • 58
    • 78650038629 scopus 로고    scopus 로고
    • GPRC6A mediates the non-genomic effects of steroids
    • Pi M, Parrill A. L, & Quarles L. D. GPRC6A mediates the non-genomic effects of steroids. J. Biol. Chem. 285, 39953-39964 (2010).
    • (2010) J. Biol. Chem , vol.285 , pp. 39953-39964
    • Pi, M.1    Parrill, A.L.2    Quarles, L.D.3
  • 60
    • 84855398593 scopus 로고    scopus 로고
    • DHHC 7 and -21 are palmitoylacyltransferases for sex steroid receptors
    • Pedram A, Razandi M, Deschenes R. J, & Levin E. R. DHHC 7 and -21 are palmitoylacyltransferases for sex steroid receptors. Mol. Biol. Cell 23, 188-199 (2012).
    • (2012) Mol. Biol. Cell , vol.23 , pp. 188-199
    • Pedram, A.1    Razandi, M.2    Deschenes, R.J.3    Levin, E.R.4
  • 61
    • 34249682915 scopus 로고    scopus 로고
    • Role of ERβ palmitoylation in the inhibition of human colon cancer cell proliferation
    • Galluzzo P, Caiazza F, Moreno S, & Marino M. Role of ERβ palmitoylation in the inhibition of human colon cancer cell proliferation. Endocr. Relat. Cancer 14, 153-167 (2007).
    • (2007) Endocr. Relat. Cancer , vol.14 , pp. 153-167
    • Galluzzo, P.1    Caiazza, F.2    Moreno, S.3    Marino, M.4
  • 62
    • 11144332004 scopus 로고    scopus 로고
    • Palmitoylation-dependent estrogen receptor α membrane localization: Regulation by 17β estradiol
    • Acconcia F, et al. Palmitoylation-dependent estrogen receptor α membrane localization: regulation by 17β estradiol. Mol. Biol. Cell 16, 231-237 (2005).
    • (2005) Mol. Biol. Cell , vol.16 , pp. 231-237
    • Acconcia, F.1
  • 63
    • 77953460074 scopus 로고    scopus 로고
    • Heat shock protein 27 is required for sex steroid receptor trafficking to and functioning at the plasma membrane
    • Razandi M, Pedram A, & Levin E. R. Heat shock protein 27 is required for sex steroid receptor trafficking to and functioning at the plasma membrane. Mol. Cell. Biol. 30, 3249-3261 (2010).
    • (2010) Mol. Cell. Biol , vol.30 , pp. 3249-3261
    • Razandi, M.1    Pedram, A.2    Levin, E.R.3
  • 64
    • 84902687970 scopus 로고    scopus 로고
    • Caveolin 1 regulates genomic action of the glucocorticoid receptor in neural stem cells
    • Peffer M. E, et al. Caveolin 1 regulates genomic action of the glucocorticoid receptor in neural stem cells. Mol. Cell. Biol. 34, 2611-2623 (2014).
    • (2014) Mol. Cell. Biol , vol.34 , pp. 2611-2623
    • Peffer, M.E.1
  • 65
    • 0036139164 scopus 로고    scopus 로고
    • ERs associate with and regulate the production of caveolin: Implications for signaling and cellular actions
    • Razandi M, Oh P, Pedram A, Schnitzer J, & Levin E. R. ERs associate with and regulate the production of caveolin: implications for signaling and cellular actions. Mol. Endocrinol. 16, 100-115 (2002).
    • (2002) Mol. Endocrinol , vol.16 , pp. 100-115
    • Razandi, M.1    Oh, P.2    Pedram, A.3    Schnitzer, J.4    Levin, E.R.5
  • 66
    • 34250836804 scopus 로고    scopus 로고
    • Direct interactions with Gαi and Gβγ mediate nongenomic signaling by estrogen receptor α
    • Kumar P, et al. Direct interactions with Gαi and Gβγ mediate nongenomic signaling by estrogen receptor α. Mol. Endocrinol. 21, 1370-1380 (2007).
    • (2007) Mol. Endocrinol , vol.21 , pp. 1370-1380
    • Kumar, P.1
  • 67
    • 0037462733 scopus 로고    scopus 로고
    • Proximal events in signaling by plasma membrane estrogen receptors
    • Razandi M, Pedram A, Park S. T, & Levin E. R. Proximal events in signaling by plasma membrane estrogen receptors. J. Biol. Chem. 278, 2701-2712 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 2701-2712
    • Razandi, M.1    Pedram, A.2    Park, S.T.3    Levin, E.R.4
  • 68
    • 1242341918 scopus 로고    scopus 로고
    • The role of Shc and insulin-like growth factor 1 receptor in mediating the translocation of estrogen receptor α to the plasma membrane
    • Song R. X, et al. The role of Shc and insulin-like growth factor 1 receptor in mediating the translocation of estrogen receptor α to the plasma membrane. Proc. Natl Acad. Sci. USA 101, 2076-2081 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 2076-2081
    • Song, R.X.1
  • 69
    • 42549141260 scopus 로고    scopus 로고
    • The nutritional flavanone naringenin triggers antiestrogenic effects by regulating estrogen receptor α-palmitoylation
    • Galluzzo P, Ascenzi P, Bulzomi P, & Marino M. The nutritional flavanone naringenin triggers antiestrogenic effects by regulating estrogen receptor α-palmitoylation. Endocrinology 149, 2567-2575 (2008).
    • (2008) Endocrinology , vol.149 , pp. 2567-2575
    • Galluzzo, P.1    Ascenzi, P.2    Bulzomi, P.3    Marino, M.4
  • 70
    • 84899671764 scopus 로고    scopus 로고
    • Lysosomal function is involved in 17β estradiol-induced estrogen receptor α degradation and cell proliferation
    • Totta P, Pesiri V, Marino M, & Acconcia F. Lysosomal function is involved in 17β estradiol-induced estrogen receptor α degradation and cell proliferation. PLoS ONE 9, e94880 (2014).
    • (2014) PLoS ONE , vol.9 , pp. e94880
    • Totta, P.1    Pesiri, V.2    Marino, M.3    Acconcia, F.4
  • 71
    • 33846138978 scopus 로고    scopus 로고
    • Progesterone receptors upregulate Wnt 1 to induce epidermal growth factor receptor transactivation and c Src-dependent sustained activation of Erk1/2 mitogen-Activated protein kinase in breast cancer cells
    • Faivre E. J, & Lange C. A. Progesterone receptors upregulate Wnt 1 to induce epidermal growth factor receptor transactivation and c Src-dependent sustained activation of Erk1/2 mitogen-Activated protein kinase in breast cancer cells. Mol. Cell. Biol. 27, 466-480 (2007).
    • (2007) Mol. Cell. Biol , vol.27 , pp. 466-480
    • Faivre, E.J.1    Lange, C.A.2
  • 72
    • 79551678920 scopus 로고    scopus 로고
    • Mechanisms underlying rapid aldosterone effects in the kidney
    • Thomas W, & Harvey B. J. Mechanisms underlying rapid aldosterone effects in the kidney. Annu. Rev. Physiol. 73, 335-357 (2011).
    • (2011) Annu. Rev. Physiol , vol.73 , pp. 335-357
    • Thomas, W.1    Harvey, B.J.2
  • 73
    • 43749108417 scopus 로고    scopus 로고
    • EF domains are sufficient for nongenomic mineralocorticoid receptor actions
    • Grossmann C, Freudinger R, Mildenberger S, Husse B, & Gekle M. EF domains are sufficient for nongenomic mineralocorticoid receptor actions. J. Biol. Chem. 283, 7109-7116 (2008).
    • (2008) J. Biol. Chem , vol.283 , pp. 7109-7116
    • Grossmann, C.1    Freudinger, R.2    Mildenberger, S.3    Husse, B.4    Gekle, M.5
  • 74
    • 1942442455 scopus 로고    scopus 로고
    • Early nongenomic events in aldosterone action in renal collecting duct cells: PKCα activation, mineralocorticoid receptor phosphorylation, and cross-Talk with the genomic response
    • Le Moellic C, et al. Early nongenomic events in aldosterone action in renal collecting duct cells: PKCα activation, mineralocorticoid receptor phosphorylation, and cross-Talk with the genomic response. J. Am. Soc. Nephrol. 15, 1145-1160 (2004).
    • (2004) J. Am. Soc. Nephrol , vol.15 , pp. 1145-1160
    • Le Moellic, C.1
  • 75
    • 34250690433 scopus 로고    scopus 로고
    • Kinases and protein phosphorylation as regulators of steroid hormone action
    • Weigel N. L, & Moore N. L. Kinases and protein phosphorylation as regulators of steroid hormone action. Nucl. Recept. Signal. 5, e005 (2007).
    • (2007) Nucl. Recept. Signal , vol.5 , pp. e005
    • Weigel, N.L.1    Moore, N.L.2
  • 76
    • 77954648696 scopus 로고    scopus 로고
    • Reprogramming the posttranslational code of SRC 3 confers a switch in mammalian systems biology
    • York B, et al. Reprogramming the posttranslational code of SRC 3 confers a switch in mammalian systems biology. Proc. Natl Acad. Sci. USA 107, 11122-11127 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 11122-11127
    • York, B.1
  • 77
    • 24644497683 scopus 로고    scopus 로고
    • Rapid estrogen-induced phosphorylation of the SRC 3 coactivator occurs in an extranuclear complex containing estrogen receptor
    • Zheng F. F, Wu R. C, Smith C. L, & O'Malley B. W. Rapid estrogen-induced phosphorylation of the SRC 3 coactivator occurs in an extranuclear complex containing estrogen receptor. Mol. Cell. Biol. 25, 8273-8284 (2005).
    • (2005) Mol. Cell. Biol , vol.25 , pp. 8273-8284
    • Zheng, F.F.1    Wu, R.C.2    Smith, C.L.3    O'Malley, B.W.4
  • 78
    • 11144230050 scopus 로고    scopus 로고
    • SMRT and N CoR corepressors are regulated by distinct kinase signaling pathways
    • Jonas B. A, & Privalsky M. L. SMRT and N CoR corepressors are regulated by distinct kinase signaling pathways. J. Biol. Chem. 279, 54676-54686 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 54676-54686
    • Jonas, B.A.1    Privalsky, M.L.2
  • 79
    • 84884416492 scopus 로고    scopus 로고
    • Phosphorylation: A fundamental regulator of steroid receptor action
    • Trevino L. S, & Weigel N. L. Phosphorylation: a fundamental regulator of steroid receptor action. Trends Endocrinol. Metab. 24, 515-524 (2013).
    • (2013) Trends Endocrinol. Metab , vol.24 , pp. 515-524
    • Trevino, L.S.1    Weigel, N.L.2
  • 80
    • 77955606282 scopus 로고    scopus 로고
    • Extranuclear estrogen receptor-α stimulates NeuroD1 binding to the insulin promoter and favors insulin synthesis
    • Wong W. P, et al. Extranuclear estrogen receptor-α stimulates NeuroD1 binding to the insulin promoter and favors insulin synthesis. Proc. Natl Acad. Sci. USA 107, 13057-13062 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 13057-13062
    • Wong, W.P.1
  • 81
    • 84890346903 scopus 로고    scopus 로고
    • Reprogramming of non-genomic estrogen signaling by the stemness factor SOX2 enhances the tumor-initiating capacity of breast cancer cells
    • Vazquez-Martin A, et al. Reprogramming of non-genomic estrogen signaling by the stemness factor SOX2 enhances the tumor-initiating capacity of breast cancer cells. Cell Cycle 12, 3471-3477 (2013).
    • (2013) Cell Cycle , vol.12 , pp. 3471-3477
    • Vazquez-Martin, A.1
  • 82
    • 84928203124 scopus 로고    scopus 로고
    • Progesterone generates cancer stem cells through membrane progesterone receptor-Triggered signaling in basal-like human mammary cells
    • Vares G, et al. Progesterone generates cancer stem cells through membrane progesterone receptor-Triggered signaling in basal-like human mammary cells. Cancer Lett. 362, 167-173 (2015).
    • (2015) Cancer Lett , vol.362 , pp. 167-173
    • Vares, G.1
  • 83
    • 84974824389 scopus 로고    scopus 로고
    • Membrane and nuclear estrogen receptor α collaborate to suppress adipogenesis but not triglyceride content
    • Pedram A, Razandi M, Blumberg B, & Levin E. R. Membrane and nuclear estrogen receptor α collaborate to suppress adipogenesis but not triglyceride content. FASEB J. 30, 230-240 (2016).
    • (2016) FASEB J. , vol.30 , pp. 230-240
    • Pedram, A.1    Razandi, M.2    Blumberg, B.3    Levin, E.R.4
  • 84
    • 84878331707 scopus 로고    scopus 로고
    • Estrogen reduces lipid content in the liver exclusively from membrane receptor signaling
    • Pedram A, et al. Estrogen reduces lipid content in the liver exclusively from membrane receptor signaling. Sci. Signal. 6, ra36 (2013).
    • (2013) Sci. Signal , vol.6 , pp. ra36
    • Pedram, A.1
  • 85
    • 79960977229 scopus 로고    scopus 로고
    • Estrogen receptor activation reduces lipid synthesis in pancreatic islets and prevents β cell failure in rodent models of type 2 diabetes
    • Tiano J. P, et al. Estrogen receptor activation reduces lipid synthesis in pancreatic islets and prevents β cell failure in rodent models of type 2 diabetes. J. Clin. Invest. 121, 3331-3342 (2011).
    • (2011) J. Clin. Invest , vol.121 , pp. 3331-3342
    • Tiano, J.P.1
  • 86
    • 84862737646 scopus 로고    scopus 로고
    • Molecular mechanisms of estrogen receptors suppression of lipogenesis in pancreatic β-cells
    • Tiano J. P, & Mauvais-Jarvis F. Molecular mechanisms of estrogen receptors suppression of lipogenesis in pancreatic β-cells. Endocrinology 153, 2997-3005 (2012).
    • (2012) Endocrinology , vol.153 , pp. 2997-3005
    • Tiano, J.P.1    Mauvais-Jarvis, F.2
  • 87
    • 77954837839 scopus 로고    scopus 로고
    • Xenoestrogen-induced regulation of EZH2 and histone methylation via estrogen receptor signaling to PI3K/AKT
    • Bredfeldt T. G, et al. Xenoestrogen-induced regulation of EZH2 and histone methylation via estrogen receptor signaling to PI3K/AKT. Mol. Endocrinol. 24, 993-1006 (2010).
    • (2010) Mol. Endocrinol , vol.24 , pp. 993-1006
    • Bredfeldt, T.G.1
  • 88
    • 84901412371 scopus 로고    scopus 로고
    • Membrane-localized estrogen receptor α is required for normal organ development and function
    • Pedram A, Razandi M, Lewis M, Hammes S, & Levin E. R. Membrane-localized estrogen receptor α is required for normal organ development and function. Dev. Cell 29, 482-490 (2014).
    • (2014) Dev. Cell , vol.29 , pp. 482-490
    • Pedram, A.1    Razandi, M.2    Lewis, M.3    Hammes, S.4    Levin, E.R.5
  • 89
    • 84890487889 scopus 로고    scopus 로고
    • Estrogen regulates histone deacetylases to prevent cardiac hypertrophy
    • Pedram A, et al. Estrogen regulates histone deacetylases to prevent cardiac hypertrophy. Mol. Biol. Cell 24, 3805-3818 (2013).
    • (2013) Mol. Biol. Cell , vol.24 , pp. 3805-3818
    • Pedram, A.1
  • 90
    • 84903437266 scopus 로고    scopus 로고
    • MTORC2 in the center of cancer metabolic reprogramming
    • Masui K, Cavenee W. K, & Mischel P. S. mTORC2 in the center of cancer metabolic reprogramming. Trends Endocrinol. Metab. 25, 364-373 (2014).
    • (2014) Trends Endocrinol. Metab , vol.25 , pp. 364-373
    • Masui, K.1    Cavenee, W.K.2    Mischel, P.S.3
  • 91
    • 84861411190 scopus 로고    scopus 로고
    • Phosphorylation by p38 mitogen-Activated protein kinase promotes estrogen receptor α turnover and functional activity via the SCF(Skp2) proteasomal complex
    • Bhatt S, Xiao Z, Meng Z, & Katzenellenbogen B. S. Phosphorylation by p38 mitogen-Activated protein kinase promotes estrogen receptor α turnover and functional activity via the SCF(Skp2) proteasomal complex. Mol. Cell. Biol. 32, 1928-1943 (2012).
    • (2012) Mol. Cell. Biol , vol.32 , pp. 1928-1943
    • Bhatt, S.1    Xiao, Z.2    Meng, Z.3    Katzenellenbogen, B.S.4
  • 92
    • 0037351881 scopus 로고    scopus 로고
    • Cyclic, proteasome-mediated turnover of unliganded and liganded ERα on responsive promoters is an integral feature of estrogen signaling
    • Reid G, et al. Cyclic, proteasome-mediated turnover of unliganded and liganded ERα on responsive promoters is an integral feature of estrogen signaling. Mol. Cell 11, 695-707 (2003).
    • (2003) Mol. Cell , vol.11 , pp. 695-707
    • Reid, G.1
  • 93
    • 80052013008 scopus 로고    scopus 로고
    • Long-lasting behavioral responses to stress involve a direct interaction of glucocorticoid receptors with ERK1/2-MSK1-Elk 1 signaling
    • Gutierrez-Mecinas M, et al. Long-lasting behavioral responses to stress involve a direct interaction of glucocorticoid receptors with ERK1/2-MSK1-Elk 1 signaling. Proc. Natl Acad. Sci. USA 108, 13806-13811 (2011).
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 13806-13811
    • Gutierrez-Mecinas, M.1
  • 94
    • 84938703029 scopus 로고    scopus 로고
    • Rapid nongenomic glucocorticoid actions in male mouse hypothalamic neuroendocrine cells are dependent on the nuclear glucocorticoid receptor
    • Nahar J, et al. Rapid nongenomic glucocorticoid actions in male mouse hypothalamic neuroendocrine cells are dependent on the nuclear glucocorticoid receptor. Endocrinology 156, 2831-2842 (2015).
    • (2015) Endocrinology , vol.156 , pp. 2831-2842
    • Nahar, J.1
  • 95
    • 63649148223 scopus 로고    scopus 로고
    • Developmental phenotype of a membrane only estrogen receptor α (MOER) mouse
    • Pedram A, et al. Developmental phenotype of a membrane only estrogen receptor α (MOER) mouse. J. Biol. Chem. 284, 3488-3495 (2009).
    • (2009) J. Biol. Chem , vol.284 , pp. 3488-3495
    • Pedram, A.1
  • 96
    • 84878632677 scopus 로고    scopus 로고
    • The role of estrogens in control of energy balance and glucose homeostasis
    • Mauvais-Jarvis F, Clegg D. J, & Hevener A. L. The role of estrogens in control of energy balance and glucose homeostasis. Endocr. Rev. 34, 309-338 (2013).
    • (2013) Endocr. Rev , vol.34 , pp. 309-338
    • Mauvais-Jarvis, F.1    Clegg, D.J.2    Hevener, A.L.3
  • 97
    • 73249129499 scopus 로고    scopus 로고
    • Rapid regulation of KATP channel activity by 17β estradiol in pancreatic β-cells involves the estrogen receptor β and the atrial natriuretic peptide receptor
    • Soriano S, et al. Rapid regulation of KATP channel activity by 17β estradiol in pancreatic β-cells involves the estrogen receptor β and the atrial natriuretic peptide receptor. Mol. Endocrinol. 23, 1973-1982 (2009).
    • (2009) Mol. Endocrinol , vol.23 , pp. 1973-1982
    • Soriano, S.1
  • 98
    • 84870360401 scopus 로고    scopus 로고
    • Estrogen modulates metabolic pathway adaptation to available glucose in breast cancer cells
    • O'Mahony F, Razandi M, Pedram A, Harvey B. J, & Levin E. R. Estrogen modulates metabolic pathway adaptation to available glucose in breast cancer cells. Mol. Endocrinol. 26, 2058-2070 (2012).
    • (2012) Mol. Endocrinol , vol.26 , pp. 2058-2070
    • O'Mahony, F.1    Razandi, M.2    Pedram, A.3    Harvey, B.J.4    Levin, E.R.5
  • 99
    • 77950354885 scopus 로고    scopus 로고
    • Insulin-sensitizing therapy attenuates type 2 diabetes-mediated mammary tumor progression
    • Fierz Y, Novosyadlyy R, Vijayakumar A, Yakar S, & LeRoith D. Insulin-sensitizing therapy attenuates type 2 diabetes-mediated mammary tumor progression. Diabetes 59, 686-693 (2010).
    • (2010) Diabetes , vol.59 , pp. 686-693
    • Fierz, Y.1    Novosyadlyy, R.2    Vijayakumar, A.3    Yakar, S.4    LeRoith, D.5
  • 100
    • 76549136489 scopus 로고    scopus 로고
    • Insulin-mediated acceleration of breast cancer development and progression in a nonobese model of type 2 diabetes
    • Novosyadlyy R, et al. Insulin-mediated acceleration of breast cancer development and progression in a nonobese model of type 2 diabetes. Cancer Res. 70, 741-751 (2010).
    • (2010) Cancer Res , vol.70 , pp. 741-751
    • Novosyadlyy, R.1
  • 101
    • 22544488420 scopus 로고    scopus 로고
    • Estrogen inhibits cardiomyocyte hypertrophy in vitro Antagonism of calcineurin-related hypertrophy through induction of MCIP1
    • Pedram A, Razandi M, Aitkenhead M, & Levin E. R. Estrogen inhibits cardiomyocyte hypertrophy in vitro. Antagonism of calcineurin-related hypertrophy through induction of MCIP1. J. Biol. Chem. 280, 26339-26348 (2005).
    • (2005) J. Biol. Chem , vol.280 , pp. 26339-26348
    • Pedram, A.1    Razandi, M.2    Aitkenhead, M.3    Levin, E.R.4
  • 103
    • 0032589745 scopus 로고    scopus 로고
    • Estrogen receptor α mediates the nongenomic activation of endothelial nitric oxide synthase by estrogen
    • Chen Z, et al. Estrogen receptor α mediates the nongenomic activation of endothelial nitric oxide synthase by estrogen. J. Clin. Invest. 103, 401-406 (1999).
    • (1999) J. Clin. Invest , vol.103 , pp. 401-406
    • Chen, Z.1
  • 104
    • 84892595887 scopus 로고    scopus 로고
    • Mutation of the palmitoylation site of estrogen receptor α in vivo reveals tissue-specific roles for membrane versus nuclear actions
    • Adlanmerini M, et al. Mutation of the palmitoylation site of estrogen receptor α in vivo reveals tissue-specific roles for membrane versus nuclear actions. Proc. Natl Acad. Sci. USA 111, E283-E290 (2014).
    • (2014) Proc. Natl Acad. Sci. USA , vol.111 , pp. E283-E290
    • Adlanmerini, M.1
  • 105
    • 34948820661 scopus 로고    scopus 로고
    • 27 Hydroxycholesterol is an endogenous SERM that inhibits the cardiovascular effects of estrogen
    • Umetani M, et al. 27 Hydroxycholesterol is an endogenous SERM that inhibits the cardiovascular effects of estrogen. Nat. Med. 13, 1185-1192 (2007).
    • (2007) Nat Med , vol.13 , pp. 1185-1192
    • Umetani, M.1
  • 106
    • 79953160837 scopus 로고    scopus 로고
    • 27 Hydroxycholesterol: The first identified endogenous SERM
    • Umetani M, & Shaul P. W. 27 Hydroxycholesterol: the first identified endogenous SERM. Trends Endocrinol. Metab. 22, 130-135 (2011).
    • (2011) Trends Endocrinol Metab , vol.22 , pp. 130-135
    • Umetani, M.1    Shaul, P.W.2
  • 107
    • 84887617570 scopus 로고    scopus 로고
    • 27 Hydroxycholesterol promotes cell-Autonomous ER positive breast cancer growth
    • Wu Q, et al. 27 Hydroxycholesterol promotes cell-Autonomous, ER positive breast cancer growth. Cell Rep. 5, 637-645 (2013).
    • (2013) Cell Rep , vol.5 , pp. 637-645
    • Wu, Q.1
  • 108
    • 84881233906 scopus 로고    scopus 로고
    • LXRβ/estrogen receptor-α signaling in lipid rafts preserves endothelial integrity
    • Ishikawa T, et al. LXRβ/estrogen receptor-α signaling in lipid rafts preserves endothelial integrity. J. Clin. Invest. 123, 3488-3497 (2013).
    • (2013) J. Clin. Invest , vol.123 , pp. 3488-3497
    • Ishikawa, T.1
  • 110
    • 84894070412 scopus 로고    scopus 로고
    • Activated retinoid receptors are required for the migration and fate maintenance of subsets of cortical neurons
    • Choi J, Park S, & Sockanathan S. Activated retinoid receptors are required for the migration and fate maintenance of subsets of cortical neurons. Development 141, 1151-1160 (2014).
    • (2014) Development , vol.141 , pp. 1151-1160
    • Choi, J.1    Park, S.2    Sockanathan, S.3
  • 111
    • 10044255446 scopus 로고    scopus 로고
    • The nuclear orphan receptor COUP-TFII is required for limb and skeletal muscle development
    • Lee C. T, et al. The nuclear orphan receptor COUP-TFII is required for limb and skeletal muscle development. Mol. Cell. Biol. 24, 10835-10843 (2004).
    • (2004) Mol. Cell. Biol , vol.24 , pp. 10835-10843
    • Lee, C.T.1
  • 112
    • 79958235622 scopus 로고    scopus 로고
    • Glucocorticoid receptor stimulation and the regulation of neonatal cerebellar neural progenitor cell apoptosis
    • Noguchi K. K, Lau K, Smith D. J, Swiney B. S, & Farber N. B. Glucocorticoid receptor stimulation and the regulation of neonatal cerebellar neural progenitor cell apoptosis. Neurobiol. Dis. 43, 356-363 (2011).
    • (2011) Neurobiol. Dis , vol.43 , pp. 356-363
    • Noguchi, K.K.1    Lau, K.2    Smith, D.J.3    Swiney, B.S.4    Farber, N.B.5
  • 113
    • 0033791461 scopus 로고    scopus 로고
    • Progesterone induces side-branching of the ductal epithelium in the mammary glands of peripubertal mice
    • Atwood C. S, et al. Progesterone induces side-branching of the ductal epithelium in the mammary glands of peripubertal mice. J. Endocrinol. 167, 39-52 (2000).
    • (2000) J. Endocrinol , vol.167 , pp. 39-52
    • Atwood, C.S.1
  • 115
    • 84946209803 scopus 로고    scopus 로고
    • Estrogen receptor β modulates apoptosis complexes and the inflammasome to drive the pathogenesis of endometriosis
    • Han S. J, et al. Estrogen receptor β modulates apoptosis complexes and the inflammasome to drive the pathogenesis of endometriosis. Cell 163, 960-974 (2015).
    • (2015) Cell , vol.163 , pp. 960-974
    • Han, S.J.1
  • 116
    • 33744514462 scopus 로고    scopus 로고
    • Functional estrogen receptors in the mitochondria of breast cancer cells
    • Pedram A, Razandi M, Wallace D. C, & Levin E. R. Functional estrogen receptors in the mitochondria of breast cancer cells. Mol. Biol. Cell 17, 2125-2137 (2006).
    • (2006) Mol. Biol. Cell , vol.17 , pp. 2125-2137
    • Pedram, A.1    Razandi, M.2    Wallace, D.C.3    Levin, E.R.4
  • 117
    • 84888287050 scopus 로고    scopus 로고
    • Brain region-And sex-specific modulation of mitochondrial glucocorticoid receptor phosphorylation in fluoxetine treated stressed rats: Effects on energy metabolism
    • Adzic M, et al. Brain region-And sex-specific modulation of mitochondrial glucocorticoid receptor phosphorylation in fluoxetine treated stressed rats: effects on energy metabolism. Psychoneuroendocrinology 38, 2914-2924 (2013).
    • (2013) Psychoneuroendocrinology , vol.38 , pp. 2914-2924
    • Adzic, M.1
  • 118
    • 84877927667 scopus 로고    scopus 로고
    • Glucocorticoids and their receptors: Insights into specific roles in mitochondria
    • Lee S. R, et al. Glucocorticoids and their receptors: insights into specific roles in mitochondria. Prog. Biophys Mol. Biol. 112, 44-54 (2013).
    • (2013) Prog. Biophys Mol. Biol , vol.112 , pp. 44-54
    • Lee, S.R.1
  • 119
    • 84863005492 scopus 로고    scopus 로고
    • Glucocorticoid and estrogen receptors are reduced in mitochondria of lung epithelial cells in asthma
    • Simoes D. C, et al. Glucocorticoid and estrogen receptors are reduced in mitochondria of lung epithelial cells in asthma. PLoS ONE 7, e39183 (2012).
    • (2012) PLoS ONE , vol.7 , pp. e39183
    • Simoes, D.C.1
  • 120
    • 84880311908 scopus 로고    scopus 로고
    • Tamoxifen regulates cell fate through mitochondrial estrogen receptor β in breast cancer
    • Razandi M, Pedram A, Jordan V. C, Fuqua S, & Levin E. R. Tamoxifen regulates cell fate through mitochondrial estrogen receptor β in breast cancer. Oncogene 32, 3274-3285 (2013).
    • (2013) Oncogene , vol.32 , pp. 3274-3285
    • Razandi, M.1    Pedram, A.2    Jordan, V.C.3    Fuqua, S.4    Levin, E.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.