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Volumn 51, Issue , 2011, Pages 99-115

Membrane receptor for thyroid hormone: Physiologic and pharmacologic implications

Author keywords

angiogenesis; cancer cell proliferation; growth factors; integrin v 3; ion transport; nanoparticulate tetrac; protein trafficking; tetrac

Indexed keywords

ANTINEOPLASTIC AGENT; BASIC FIBROBLAST GROWTH FACTOR; CETUXIMAB; DOXORUBICIN; FIBROBLAST GROWTH FACTOR 2; LEVOTHYROXINE; LIOTHYRONINE; NANOPARTICLE; SODIUM PROTON EXCHANGE PROTEIN; TETRAIODOTHYROACETIC ACID; THYROID HORMONE RECEPTOR; THYRONINE; THYROXINE DERIVATIVE; UNCLASSIFIED DRUG; VASCULOTROPIN; VITRONECTIN RECEPTOR;

EID: 79951978814     PISSN: 03621642     EISSN: 15454304     Source Type: Book Series    
DOI: 10.1146/annurev-pharmtox-010510-100512     Document Type: Article
Times cited : (171)

References (71)
  • 1
    • 22144494707 scopus 로고    scopus 로고
    • 3 contains a cell surface receptor site for thyroid hormone that is linked to activation of mitogen-activated protein kinase and induction of angiogenesis
    • DOI 10.1210/en.2005-0102
    • Bergh JJ, Lin HY, Lansing L, Mohamed SN, Davis FB, et al. 2005. Integrin ocv|33 contains a cell surface receptor site for thyroid hormone that is linked to activation of mitogen-activated protein kinase and induction of angiogenesis. Endocrinology 146:2864-71 (Pubitemid 41002793)
    • (2005) Endocrinology , vol.146 , Issue.7 , pp. 2864-2871
    • Bergh, J.J.1    Lin, H.-Y.2    Lansing, L.3    Mohamed, S.N.4    Davis, F.B.5    Mousa, S.6    Davis, P.J.7
  • 3
    • 33645517462 scopus 로고    scopus 로고
    • Proangiogenesis action of the thyroid hormone analog 3,5- diiodothyropropionic acid (DITPA) is initiated at the cell surface and is integrin mediated
    • Mousa SA, O'Connor L, Davis FB, Davis PJ. 2006. Proangiogenesis action of the thyroid hormone analog 3,5-diiodothyropropionic acid (DITPA) is initiated at the cell surface and is integrin mediated. Endocrinology 147:1602-7
    • (2006) Endocrinology , vol.147 , pp. 1602-7
    • Mousa, S.A.1    O'Connor, L.2    Davis, F.B.3    Davis, P.J.4
  • 4
    • 3042693890 scopus 로고    scopus 로고
    • Thyroid hormone causes mitogen-activated protein kinase-dependent phosphorylation of the nuclear estrogen receptor
    • DOI 10.1210/en.2004-0308
    • Tang HY, Lin HY, Zhang S, Davis FB, Davis PJ. 2004. Thyroid hormone causes mitogen-activated protein kinase-dependent phosphorylation of the nuclear estrogen receptor. Endocrinology 145:3265-72 (Pubitemid 38829999)
    • (2004) Endocrinology , vol.145 , Issue.7 , pp. 3265-3272
    • Tang, H.-Y.1    Lin, H.-Y.2    Zhang, S.3    Davis, F.B.4    Davis, P.J.5
  • 5
    • 33847060499 scopus 로고    scopus 로고
    • Thyroid hormone is a MAPK-dependent growth factor for thyroid cancer cells and is anti-apoptotic
    • DOI 10.1016/j.steroids.2006.11.014, PII S0039128X06002509, FASEB 2006 Summer Research Conference Mechanism of Action of Steroid Hormones: Integration of Membrane and Nucleus Initiated Effects
    • Lin HY, Tang HY, Shih A, Keating T, Cao G, et al. 2007. Thyroid hormone is a MAPK-dependent growth factor for thyroid cancer cells and is anti-apoptotic. Steroids 72:180-87 (Pubitemid 46273502)
    • (2007) Steroids , vol.72 , Issue.2 , pp. 180-187
    • Lin, H.-Y.1    Tang, H.-Y.2    Shih, A.3    Keating, T.4    Cao, G.5    Davis, P.J.6    Davis, F.B.7
  • 6
    • 66149090297 scopus 로고    scopus 로고
    • L-thyroxine vs. 3,5,3'-triiodo-L-thyronine and cell proliferation: Activation of mitogen-activated protein kinase and phosphatidylinositol 3-kinase
    • Lin HY, Sun M, Tang HY, Lin C, Luidens MK, et al. 2009. L-thyroxine vs. 3,5,3'-triiodo-L-thyronine and cell proliferation: activation of mitogen-activated protein kinase and phosphatidylinositol 3-kinase. Am. J. Physiol. Cell Physiol. 296:C980-91
    • (2009) Am. J. Physiol. Cell Physiol. , vol.296
    • Lin, H.Y.1    Sun, M.2    Tang, H.Y.3    Lin, C.4    Luidens, M.K.5
  • 8
    • 0029164368 scopus 로고
    • Thyroxine-dependent regulation of integrin-laminin interactions in astrocytes
    • Farwell AP, Tranter MP, Leonard JL. 1995. Thyroxine-dependent regulation of integrin-laminin interactions in astrocytes. Endocrinology 136:3909-15
    • (1995) Endocrinology , vol.136 , pp. 3909-15
    • Farwell, A.P.1    Tranter, M.P.2    Leonard, J.L.3
  • 10
    • 77953639982 scopus 로고    scopus 로고
    • Molecular aspects of thyroid hormone actions
    • Cheng SY, Leonard JL, Davis PJ. 2010. Molecular aspects of thyroid hormone actions. Endocr. Rev. 31:139-70
    • (2010) Endocr. Rev. , vol.31 , pp. 139-70
    • Cheng, S.Y.1    Leonard, J.L.2    Davis, P.J.3
  • 11
    • 32544432490 scopus 로고    scopus 로고
    • Thyroid hormone action at the cellular, genomic and target gene levels
    • DOI 10.1016/j.mce.2005.11.030, PII S0303720705004296
    • Yen PM, Ando S, Feng X, Liu Y, Maruvada P, Xia X. 2006. Thyroid hormone action at the cellular, genomic and target gene levels. Mol. Cell. Endocrinol. 246:121-27 (Pubitemid 43238405)
    • (2006) Molecular and Cellular Endocrinology , vol.246 , Issue.1-2 , pp. 121-127
    • Yen, P.M.1    Ando, S.2    Feng, X.3    Liu, Y.4    Maruvada, P.5    Xia, X.6
  • 12
    • 34548415678 scopus 로고    scopus 로고
    • Thyroid hormone mediated changes in gene expression can be initiated by cytosolic action of the thyroid hormone receptor |3 through the phosphatidylinositol 3-kinase pathway
    • Moeller LC, Cao X, Dumitrescu AM, Seo H, Refetoff S. 2006. Thyroid hormone mediated changes in gene expression can be initiated by cytosolic action of the thyroid hormone receptor |3 through the phosphatidylinositol 3-kinase pathway. Nucl. Recept. Signal. 4:e020
    • (2006) Nucl. Recept. Signal. , vol.4
    • Moeller, L.C.1    Cao, X.2    Dumitrescu, A.M.3    Seo, H.4    Refetoff, S.5
  • 14
    • 72649101718 scopus 로고    scopus 로고
    • Mini-review: Cell surface receptor for thyroid hormone and nongenomic regulation of ion fluxes in excitable cells
    • Davis PJ, Zhou M, Davis FB, Lansing L, Mousa SA, Lin HY. 2010. Mini-review: cell surface receptor for thyroid hormone and nongenomic regulation of ion fluxes in excitable cells. Physiol. Behav. 99:237-39
    • (2010) Physiol. Behav. , vol.99 , pp. 237-39
    • Davis, P.J.1    Zhou, M.2    Davis, F.B.3    Lansing, L.4    Mousa, S.A.5    Lin, H.Y.6
  • 16
    • 67650899238 scopus 로고    scopus 로고
    • Cytoplasm-to-nucleus shuttling of thyroid hormone receptor-131 (TR|31) is directed from a plasma membrane integrin receptor by thyroid hormone
    • Cao HJ, Lin HY, Luidens MK, Davis FB, Davis PJ. 2009. Cytoplasm-to-nucleus shuttling of thyroid hormone receptor-131 (TR|31) is directed from a plasma membrane integrin receptor by thyroid hormone. Endocr. Res. 34:31-42
    • (2009) Endocr. Res. , vol.34 , pp. 31-42
    • Cao, H.J.1    Lin, H.Y.2    Luidens, M.K.3    Davis, F.B.4    Davis, P.J.5
  • 17
    • 0021367047 scopus 로고
    • Effect of a protein-free diet on muscle protein turnover and nitrogen conservation in euthyroid and hyperthyroid rats
    • Carter WJ, van der Weijden Benjamin WS, Faas FH. 1984. Effect of a protein-free diet on muscle protein turnover and nitrogen conservation in euthyroid and hyperthyroid rats. Biochem. J. 217:471-76 (Pubitemid 14178977)
    • (1984) Biochemical Journal , vol.217 , Issue.2 , pp. 471-476
    • Carter, W.J.1    Van Der Weijden Benjamin, W.S.2    Faas, F.H.3
  • 18
    • 57349119069 scopus 로고    scopus 로고
    • Cellular and molecular basis of deiodinase-regulated thyroid hormone signaling
    • Gereben B, Zavacki AM, Ribich S, Kim BW, Huang SA, et al. 2008. Cellular and molecular basis of deiodinase-regulated thyroid hormone signaling. Endocr. Rev. 29:898-938
    • (2008) Endocr. Rev. , vol.29 , pp. 898-938
    • Gereben, B.1    Zavacki, A.M.2    Ribich, S.3    Kim, B.W.4    Huang, S.A.5
  • 19
    • 2942653137 scopus 로고    scopus 로고
    • Proangiogenic action of thyroid hormone is fibroblast growth factor-dependent and is initiated at the cell surface
    • DOI 10.1161/01.RES.0000130784.90237.4a
    • Davis FB, Mousa SA, O'Connor L, Mohamed S, Lin HY, et al. 2004. Proangiogenic action of thyroid hormone is fibroblast growth factor-dependent and is initiated at the cell surface. Circ. Res. 94:1500-6 (Pubitemid 38780323)
    • (2004) Circulation Research , vol.94 , Issue.11 , pp. 1500-1506
    • Davis, F.B.1    Mousa, S.A.2    O'Connor, L.3    Mohamed, S.4    Lin, H.-Y.5    Cao, H.J.6    Davis, P.J.7
  • 20
    • 49949152481 scopus 로고    scopus 로고
    • Tetraiodothyroacetic acid, a small molecule integrin ligand, blocks angiogenesis induced by vascular endothelial growth factor and basic fibroblast growth factor
    • Mousa SA, Bergh JJ, Dier E, Rebbaa A, O'Connor LJ, et al. 2008. Tetraiodothyroacetic acid, a small molecule integrin ligand, blocks angiogenesis induced by vascular endothelial growth factor and basic fibroblast growth factor. Angiogenesis 11:183-90
    • (2008) Angiogenesis , vol.11 , pp. 183-90
    • Mousa, S.A.1    Bergh, J.J.2    Dier, E.3    Rebbaa, A.4    O'Connor, L.J.5
  • 21
    • 67649333081 scopus 로고    scopus 로고
    • The pro-apoptotic action of stilbene-induced COX-2 in cancer cells: Convergence with the anti-apoptotic effect of thyroid hormone
    • Lin HY, Davis PJ, Tang HY, Mousa SA, Luidens MK, et al. 2009. The pro-apoptotic action of stilbene-induced COX-2 in cancer cells: convergence with the anti-apoptotic effect of thyroid hormone. Cell Cycle 8:1877-82
    • (2009) Cell Cycle , vol.8 , pp. 1877-82
    • Lin, H.Y.1    Davis, P.J.2    Tang, H.Y.3    Mousa, S.A.4    Luidens, M.K.5
  • 22
    • 77953632667 scopus 로고    scopus 로고
    • Human platelet aggregation and degranulation is induced in vitro by L-thyroxine, but not by 3,5,3'-triiodo-L-thyronine or diiodothyropropionic acid (DITPA)
    • Mousa SS, Davis FB, Davis PJ, Mousa SA. 2010. Human platelet aggregation and degranulation is induced in vitro by L-thyroxine, but not by 3,5,3'-triiodo-L-thyronine or diiodothyropropionic acid (DITPA). Clin. Appl. Thromb. Hemost. 16(3):288-93
    • (2010) Clin. Appl. Thromb. Hemost. , vol.16 , Issue.3 , pp. 288-93
    • Mousa, S.S.1    Davis, F.B.2    Davis, P.J.3    Mousa, S.A.4
  • 24
    • 9444293512 scopus 로고    scopus 로고
    • Rapid nongenomic effects of 3,5,3′-triiodo-L-thyronine on the intracellular pH of L-6 myoblasts are mediated by intracellular calcium mobilization and kinase pathways
    • DOI 10.1210/en.2004-0890
    • D'Arezzo S, Incerpi S, Davis FB, Acconcia F, Marino M, et al. 2004. Rapid nongenomic effects of 3,5,3'-triiodo-L-thyronine on the intracellular pH of L-6 myoblasts are mediated by intracellular calcium mobilization and kinase pathways. Endocrinology 145:5694-703 (Pubitemid 39564612)
    • (2004) Endocrinology , vol.145 , Issue.12 , pp. 5694-5703
    • D'Arezzo, S.1    Incerpi, S.2    Davis, F.B.3    Acconcia, F.4    Marino, M.5    Farias, R.N.6    Davis, P.J.7
  • 25
    • 27144496093 scopus 로고    scopus 로고
    • Membrane receptors mediating thyroid hormone action
    • DOI 10.1016/j.tem.2005.09.007, PII S1043276005002134
    • Davis PJ, Davis FB, Cody V. 2005. Membrane receptors mediating thyroid hormone action. Trends Endocrinol. Metab. 16:429-35 (Pubitemid 41506950)
    • (2005) Trends in Endocrinology and Metabolism , vol.16 , Issue.9 , pp. 429-435
    • Davis, P.J.1    Davis, F.B.2    Cody, V.3
  • 26
    • 41549094427 scopus 로고    scopus 로고
    • Mechanisms of nongenomic actions of thyroid hormone
    • DOI 10.1016/j.yfrne.2007.09.003, PII S0091302207000544
    • Davis PJ, Leonard JL, Davis FB. 2008. Mechanisms of nongenomic actions of thyroid hormone. Front. Neuroendocrinol. 29:211-18 (Pubitemid 351467119)
    • (2008) Frontiers in Neuroendocrinology , vol.29 , Issue.2 , pp. 211-218
    • Davis, P.J.1    Leonard, J.L.2    Davis, F.B.3
  • 28
    • 39449092245 scopus 로고    scopus 로고
    • Metabolic effects of thyroid hormone derivatives
    • DOI 10.1089/thy.2007.0248
    • Moreno M, de Lange P, Lombardi A, Silvestri E, Lanni A, Goglia F. 2008. Metabolic effects of thyroid hormone derivatives. Thyroid 18:239-53 (Pubitemid 351271526)
    • (2008) Thyroid , vol.18 , Issue.2 , pp. 239-253
    • Moreno, M.1    De Lange, P.2    Lombardi, A.3    Silvestri, E.4    Lanni, A.5    Goglia, F.6
  • 29
    • 33847051688 scopus 로고    scopus 로고
    • Molecular modeling of the thyroid hormone interactions with ocv|33 integrin
    • Cody V, Davis PJ, Davis FB. 2007. Molecular modeling of the thyroid hormone interactions with ocv|33 integrin. Steroids 72:166-70
    • (2007) Steroids , vol.72 , pp. 166-70
    • Cody, V.1    Davis, P.J.2    Davis, F.B.3
  • 30
    • 70449718848 scopus 로고    scopus 로고
    • Modification of survival pathway gene expression in human breast cancer cells by tetraiodothyroacetic acid (tetrac)
    • Glinskii AB, Glinsky GV, Lin HY, Tang HY, Sun M, et al. 2009. Modification of survival pathway gene expression in human breast cancer cells by tetraiodothyroacetic acid (tetrac). Cell Cycle 8:3554-62
    • (2009) Cell Cycle , vol.8 , pp. 3554-62
    • Glinskii, A.B.1    Glinsky, G.V.2    Lin, H.Y.3    Tang, H.Y.4    Sun, M.5
  • 31
    • 73349102140 scopus 로고    scopus 로고
    • Epidermal growth factor receptor inhibitors in cancer treatment: Advances, challenges and opportunities
    • Modjtahedi H, Essapen S. 2009. Epidermal growth factor receptor inhibitors in cancer treatment: advances, challenges and opportunities. Anticancer Drugs 20:851-55
    • (2009) Anticancer Drugs , vol.20 , pp. 851-55
    • Modjtahedi, H.1    Essapen, S.2
  • 33
    • 71949098379 scopus 로고    scopus 로고
    • Tetraiodothyroacetic acid (tetrac) and tetrac nanoparticles inhibit growth of human renal cell carcinoma xenografts
    • Yalcin M, Bharali DJ, Lansing L, Dyskin E, Mousa SS, et al. 2009. Tetraiodothyroacetic acid (tetrac) and tetrac nanoparticles inhibit growth of human renal cell carcinoma xenografts. Anticancer Res. 29:3825-31
    • (2009) Anticancer Res. , vol.29 , pp. 3825-31
    • Yalcin, M.1    Bharali, D.J.2    Lansing, L.3    Dyskin, E.4    Mousa, S.S.5
  • 34
    • 77951630790 scopus 로고    scopus 로고
    • Tetraiodothyroacetic acid (tetrac) and nanoparticulate tetrac arrest growth of medullary carcinoma of the thyroid
    • Yalcin M, Dyskin E, Lansing L, Bharali DJ, Mousa SS, et al. 2010. Tetraiodothyroacetic acid (tetrac) and nanoparticulate tetrac arrest growth of medullary carcinoma of the thyroid. J. Clin. Endocrinol. Metab. 95(4):1972-80
    • (2010) J. Clin. Endocrinol. Metab. , vol.95 , Issue.4 , pp. 1972-80
    • Yalcin, M.1    Dyskin, E.2    Lansing, L.3    Bharali, D.J.4    Mousa, S.S.5
  • 35
    • 77649308057 scopus 로고    scopus 로고
    • Tetraiodothyroacetic acid and tetraiodothyroacetic acid nanoparticle effectively inhibit the growth of human follicular thyroid cell carcinoma
    • Yalcin M, Bharali DJ, Dyskin E, Dier E, Lansing L, et al. 2010. Tetraiodothyroacetic acid and tetraiodothyroacetic acid nanoparticle effectively inhibit the growth of human follicular thyroid cell carcinoma. Thyroid 20:281-86
    • (2010) Thyroid , vol.20 , pp. 281-86
    • Yalcin, M.1    Bharali, D.J.2    Dyskin, E.3    Dier, E.4    Lansing, L.5
  • 36
    • 48749083302 scopus 로고    scopus 로고
    • Novel function of the thyroid hormone analog tetraiodothyroacetic acid: A cancer chemosensitizing and anti-cancer agent
    • Rebbaa A, Chu F, Davis FB, Davis PJ, Mousa SA. 2008. Novel function of the thyroid hormone analog tetraiodothyroacetic acid: a cancer chemosensitizing and anti-cancer agent. Angiogenesis 11:269-76
    • (2008) Angiogenesis , vol.11 , pp. 269-76
    • Rebbaa, A.1    Chu, F.2    Davis, F.B.3    Davis, P.J.4    Mousa, S.A.5
  • 38
    • 57249114643 scopus 로고    scopus 로고
    • HB-EGF stimulates eNOS expression and nitric oxide production and promotes eNOS dependent angiogenesis
    • DOI 10.1080/08977190802393596, PII 904264902
    • Mehta VB, Zhou Y, Radulescu A, Besner GE. 2008. HB-EGF stimulates eNOS expression and nitric oxide production and promotes eNOS dependent angiogenesis. Growth Factors 26:301-15 (Pubitemid 352781843)
    • (2008) Growth Factors , vol.26 , Issue.6 , pp. 301-315
    • Mehta, V.B.1    Zhou, Y.2    Radulescu, A.3    Besner, G.4
  • 39
    • 1642464918 scopus 로고    scopus 로고
    • Disparate effects of thyroid hormone on actions of epidermal growth factor and transforming growth factor-α are mediated by 3′,5′-cyclic adenosine 5′-monophosphate-dependent protein kinase II
    • DOI 10.1210/en.2003-0742
    • Shih A, Zhang S, Cao HJ, Tang HY, Davis FB, et al. 2004. Disparate effects of thyroid hormone on actions of epidermal growth factor and transforming growth factor-aare mediated by 3',5'-cyclic adenosine 5'-monophosphate-dependent protein kinase II. Endocrinology 145:1708-17 (Pubitemid 38402379)
    • (2004) Endocrinology , vol.145 , Issue.4 , pp. 1708-1717
    • Shih, A.1    Zhang, S.2    Cao, H.J.3    Tang, H.-Y.4    Davis, F.B.5    Davis, P.J.6    Lin, H.-Y.7
  • 40
    • 75149112409 scopus 로고    scopus 로고
    • Future of convection-enhanced delivery in the treatment of brain tumors
    • Bidros DS, Liu JK, Vogelbaum MA. 2010. Future of convection-enhanced delivery in the treatment of brain tumors. Future Oncol. 6:117-25
    • (2010) Future Oncol. , vol.6 , pp. 117-25
    • Bidros, D.S.1    Liu, J.K.2    Vogelbaum, M.A.3
  • 41
    • 73949155491 scopus 로고    scopus 로고
    • Overcoming multidrug resistance in cancer: Clinical studies of p-glycoprotein inhibitors
    • Coley HM. 2010. Overcoming multidrug resistance in cancer: clinical studies of p-glycoprotein inhibitors. Methods Mol. Biol. 596:341-58
    • (2010) Methods Mol. Biol. , vol.596 , pp. 341-58
    • Coley, H.M.1
  • 42
    • 55649115290 scopus 로고    scopus 로고
    • Down-regulation of P-glycoprotein expression by sustained intracellular acidification in K562/Dox cells
    • Lu Y, Pang T, Wang J, Xiong D, Ma L, et al. 2008. Down-regulation of P-glycoprotein expression by sustained intracellular acidification in K562/Dox cells. Biochem. Biophys. Res. Commun. 377:441-46
    • (2008) Biochem. Biophys. Res. Commun. , vol.377 , pp. 441-46
    • Lu, Y.1    Pang, T.2    Wang, J.3    Xiong, D.4    Ma, L.5
  • 44
  • 46
    • 65649109169 scopus 로고    scopus 로고
    • Role of thyroid hormone analogs in angiogenesis and the development of collaterals in rabbit hind limb ischemia model
    • El Eter E, Rabee H, Alkayali A, Mousa SA. 2007. Role of thyroid hormone analogs in angiogenesis and the development of collaterals in rabbit hind limb ischemia model. J. Thromb. Thrombolysis 5(Suppl. 1):375
    • (2007) J. Thromb. Thrombolysis , vol.5 , Issue.SUPPL. 1 , pp. 375
    • El Eter, E.1    Rabee, H.2    Alkayali, A.3    Mousa, S.A.4
  • 47
    • 24944500416 scopus 로고    scopus 로고
    • Topical thyroid hormone accelerates wound healing in mice
    • DOI 10.1210/en.2005-0192
    • Safer JD, Crawford TM, HolickMF. 2005. Topical thyroid hormone accelerates wound healing in mice. Endocrinology 146:4425-30 (Pubitemid 41324040)
    • (2005) Endocrinology , vol.146 , Issue.10 , pp. 4425-4430
    • Safer, J.D.1    Crawford, T.M.2    Holick, M.F.3
  • 48
    • 2042470094 scopus 로고    scopus 로고
    • A role for thyroid hormone in wound healing through keratin gene expression
    • DOI 10.1210/en.2003-1696
    • Safer JD, Crawford TM, Holick MF. 2004. A role for thyroid hormone in wound healing through keratin gene expression. Endocrinology 145:2357-61 (Pubitemid 38535065)
    • (2004) Endocrinology , vol.145 , Issue.5 , pp. 2357-2361
    • Safer, J.D.1    Crawford, T.M.2    Holick, M.F.3
  • 51
    • 41149125939 scopus 로고    scopus 로고
    • Thyroid hormone stimulation of extracellular signal-regulated kinase and cell proliferation in human osteoblast-like cells is initiated at integrin αvβ3
    • DOI 10.1677/JOE-07-0344
    • Scarlett A, Parsons MP, Hanson PL, Sidhu KK, Milligan TP, Burrin JM. 2008. Thyroid hormone stimulation of extracellular signal-regulated kinase and cell proliferation in human osteoblast-like cells is initiated at integrin ocv|33.J. Endocrinol. 196:509-17 (Pubitemid 351425506)
    • (2008) Journal of Endocrinology , vol.196 , Issue.3 , pp. 509-517
    • Scarlett, A.1    Parsons, M.P.2    Hanson, P.L.3    Sidhu, K.K.4    Milligan, T.P.5    Burrin, J.M.6
  • 52
    • 67849086870 scopus 로고    scopus 로고
    • The structure and function of platelet integrins
    • Bennett JS, Berger BW, Billings PC. 2009. The structure and function of platelet integrins. J. Thromb. Haemost. 7(Suppl. 1):200-5
    • (2009) J. Thromb. Haemost. , vol.7 , Issue.SUPPL. 1 , pp. 200-5
    • Bennett, J.S.1    Berger, B.W.2    Billings, P.C.3
  • 53
    • 77951765125 scopus 로고    scopus 로고
    • Hyperthyroidism and risk of ischemic stroke in young adults. A 5-year follow-up study
    • Sheu JJ, Kang JH, Lin HC, Lin HC. 2010. Hyperthyroidism and risk of ischemic stroke in young adults. A 5-year follow-up study. Stroke 41:961-66
    • (2010) Stroke , vol.41 , pp. 961-66
    • Sheu, J.J.1    Kang, J.H.2    Lin, H.C.3    Lin, H.C.4
  • 54
    • 57049101778 scopus 로고    scopus 로고
    • Sensory neuron sodium current requires nongenomic actions of thyroid hormone during development
    • Yonkers MA, Ribera AB. 2008. Sensory neuron sodium current requires nongenomic actions of thyroid hormone during development. J. Neurophysiol. 100:2719-25
    • (2008) J. Neurophysiol. , vol.100 , pp. 2719-25
    • Yonkers, M.A.1    Ribera, A.B.2
  • 55
    • 68149128512 scopus 로고    scopus 로고
    • Molecular components underlying nongenomic thyroid hormone signaling in embryonic zebrafish neurons
    • Yonkers MA, Ribera AB. 2009. Molecular components underlying nongenomic thyroid hormone signaling in embryonic zebrafish neurons. Neural Dev. 4:20
    • (2009) Neural Dev. , vol.4 , pp. 20
    • Yonkers, M.A.1    Ribera, A.B.2
  • 57
    • 11144261491 scopus 로고    scopus 로고
    • Regulation of cerebellar neuronal migration and neurite outgrowth by thyroxine and 3,3′,5′-triiodothyronine
    • DOI 10.1016/j.devbrainres.2004.07.016, PII S0165380604003360
    • Farwell AP, Dubord-Tomasetti SA, Pietrzykowski AZ, Stachelek SJ, Leonard JL. 2005. Regulation of cerebellar neuronal migration and neurite outgrowth by thyroxine and 3,3',5'-triiodothyronine. Brain Res. Dev. Brain Res. 154:121-35 (Pubitemid 40023136)
    • (2005) Developmental Brain Research , vol.154 , Issue.1 , pp. 121-135
    • Farwell, A.P.1    Dubord-Tomasetti, S.A.2    Pietrzykowski, A.Z.3    Stachelek, S.J.4    Leonard, J.L.5
  • 58
    • 0029869328 scopus 로고    scopus 로고
    • Thyroid hormone analogues potentiate the antiviral action of interferon-γ by two mechanisms
    • DOI 10.1002/(SICI)1097-4652(199605)167:2<269::AID-JCP10>3.0.CO;2-3
    • Lin HY, Thacore HR, Davis FB, Davis PJ. 1996. Thyroid hormone analogues potentiate the antiviral action of interferon-yby two mechanisms. J. Cell. Physiol. 167:269-76 (Pubitemid 26146983)
    • (1996) Journal of Cellular Physiology , vol.167 , Issue.2 , pp. 269-276
    • Lin, H.-Y.1    Thacore, H.R.2    Davis, F.B.3    Davis, P.J.4
  • 59
    • 0032915002 scopus 로고    scopus 로고
    • Short-term effects of thyroid hormones on the Na/H antiport in L-6 myoblasts: High molecular specificity for 3,3',5-triiodo-L-thyronine
    • DOI 10.1210/en.140.2.683
    • Incerpi S, Luly P, De Vito P, Farias RN. 1999. Short-term effects of thyroid hormones on the Na/H an-tiport in L-6 myoblasts: high molecular specificity for 3,3',5-triiodo-L-thyronine. Endocrinology 140:683-89 (Pubitemid 29058201)
    • (1999) Endocrinology , vol.140 , Issue.2 , pp. 683-689
    • Incerpi, S.1    Luly, P.2    De Vito, P.3    Farias, R.N.4
  • 60
    • 0034532451 scopus 로고    scopus 로고
    • Thyroxine promotes association of mitogen-activated protein kinase and nuclear thyroid hormone receptor (TR) and causes serine phosphorylation of TR
    • DOI 10.1074/jbc.M002560200
    • Davis PJ, Shih A, Lin HY, Martino LJ, Davis FB. 2000. Thyroxine promotes association of mitogen-activated protein kinase and nuclear thyroid hormone receptor (TR) and causes serine phosphorylation ofTR.J. Biol. Chem. 275:38032-39 (Pubitemid 32004926)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.48 , pp. 38032-38039
    • Davis, P.J.1    Shih, A.2    Lin, H.-Y.3    Martino, L.J.4    Davis, F.B.5
  • 61
    • 0035814921 scopus 로고    scopus 로고
    • Thyroid hormone promotes serine phosphorylation of p53 by mitogen-activated protein kinase
    • DOI 10.1021/bi001978b
    • Shih A, Lin HY, Davis FB, Davis PJ. 2001. Thyroid hormone promotes serine phosphorylation of p53 by mitogen-activated protein kinase. Biochemistry 40:2870-78 (Pubitemid 32198289)
    • (2001) Biochemistry , vol.40 , Issue.9 , pp. 2870-2878
    • Shih, A.1    Lin, H.-Y.2    Davis, F.B.3    Davis, P.J.4
  • 62
    • 0037732596 scopus 로고    scopus 로고
    • Identification of the putative MAP kinase docking site in the thyroid hormone receptor-β1 DNA-binding domain: Functional consequences of mutations at the docking site
    • DOI 10.1021/bi0273967
    • Lin HY, Zhang S, West BL, Tang HY, Passaretti T, et al. 2003. Identification of the putative MAP kinase docking site in the thyroid hormone receptor-131 DNA-binding domain: functional consequences of mutations at the docking site. Biochemistry 42:7571-79 (Pubitemid 36735834)
    • (2003) Biochemistry , vol.42 , Issue.24 , pp. 7571-7579
    • Lin, H.-Y.1    Zhang, S.2    West, B.L.3    Tang, H.-Y.4    Passaretti, T.5    Davis, F.B.6    Davis, P.J.7
  • 63
    • 0035815621 scopus 로고    scopus 로고
    • Nuclear Cytoplasmic Shuttling by Thyroid Hormone Receptors: Multiple protein interactions are required for nuclear retention
    • DOI 10.1074/jbc.M011112200
    • Baumann CT, Maruvada P, Hager GL, Yen PM. 2001. Nuclear cytoplasmic shuttling by thyroid hormone receptors: Multiple protein interactions are required for nuclear retention. J. Biol. Chem. 276:11237-45 (Pubitemid 38089310)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.14 , pp. 11237-11245
    • Baumann, C.T.1    Maruvada, P.2    Hager, G.L.3    Yen, P.M.4
  • 64
    • 0032538637 scopus 로고    scopus 로고
    • Hormone-induced translocation of thyroid hormone receptors in living cells visualized using a receptor green fluorescent protein chimera
    • DOI 10.1074/jbc.273.42.27058
    • Zhu XG, Hanover JA, Hager GL, Cheng SY. 1998. Hormone-induced translocation of thyroid hormone receptors in living cells visualized using a receptor green fluorescent protein chimera. J. Biol. Chem. 273:27058-63 (Pubitemid 28500409)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.42 , pp. 27058-27063
    • Zhu, X.-G.1    Hanover, J.A.2    Hager, G.L.3    Cheng, S.-Y.4
  • 67
    • 33645515261 scopus 로고    scopus 로고
    • Integrin trafficking and the control of cell migration
    • Caswell PT, Norman JC. 2006. Integrin trafficking and the control of cell migration. Traffic 7:14-21
    • (2006) Traffic , vol.7 , pp. 14-21
    • Caswell, P.T.1    Norman, J.C.2
  • 68
    • 44549084576 scopus 로고    scopus 로고
    • Thyroid hormone induces nuclear accumulation of monomeric integrin ov and formation of integrin-nucleoprotein complexes
    • Lin HY, Tang HY, Lin C, Davis FB, Davis PJ. 2007. Thyroid hormone induces nuclear accumulation of monomeric integrin ov and formation of integrin-nucleoprotein complexes. Thyroid 17(Suppl. 1):S129
    • (2007) Thyroid , vol.17 , Issue.SUPPL. 1
    • Lin, H.Y.1    Tang, H.Y.2    Lin, C.3    Davis, F.B.4    Davis, P.J.5
  • 69
    • 33644973069 scopus 로고    scopus 로고
    • Quantifying the specific binding between West Nile virus envelope domain III protein and the cellular receptor ocv|33 integrin
    • Lee JW, Chu JJ, Ng ML. 2006. Quantifying the specific binding between West Nile virus envelope domain III protein and the cellular receptor ocv|33 integrin. J. Biol. Chem. 281:1352-60
    • (2006) J. Biol. Chem. , vol.281 , pp. 1352-60
    • Lee, J.W.1    Chu, J.J.2    Ng, M.L.3
  • 70
    • 67650770190 scopus 로고    scopus 로고
    • Cooperation between integrin ocv|33 and VEGFR2 in angiogenesis
    • Somanath PR, Malinin NL, Byzova TV. 2009. Cooperation between integrin ocv|33 and VEGFR2 in angiogenesis. Angiogenesis 12:177-85
    • (2009) Angiogenesis , vol.12 , pp. 177-85
    • Somanath, P.R.1    Malinin, N.L.2    Byzova, T.V.3
  • 71
    • 51249114772 scopus 로고    scopus 로고
    • Integrin ocv|33 mediates upregulation of epidermal growth-factor receptor expression and activity in human ovarian cancer cells
    • LossnerD,Abou-Ajram C, Benge A, Reuning U. 2008. Integrin ocv|33 mediates upregulation of epidermal growth-factor receptor expression and activity in human ovarian cancer cells. Int. J. Biochem. Cell Biol. 40:2746-61
    • (2008) Int. J. Biochem. Cell Biol. , vol.40 , pp. 2746-61
    • Lossnerdabou-Ajram, C.1    Benge, A.2    Reuning, U.3


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