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Volumn 78, Issue 4, 1998, Pages 1193-1231

Current understanding of the molecular actions of vitamin D

Author keywords

[No Author keywords available]

Indexed keywords

CALCITRIOL; CALCITRIOL DERIVATIVE; CALCIUM ION; LEXACALCITOL; RETINOID X RECEPTOR; SEOCALCITOL; VITAMIN D DERIVATIVE; VITAMIN D RECEPTOR;

EID: 0031755168     PISSN: 00319333     EISSN: None     Source Type: Journal    
DOI: 10.1152/physrev.1998.78.4.1193     Document Type: Review
Times cited : (1074)

References (368)
  • 3
    • 0001407630 scopus 로고    scopus 로고
    • Extrarenal production and action of active vitamin D metabolites in human lymphoproliferative disases
    • edited by D. Feldman, F. H. Glorieux, and J. W. Pike. San Diego, CA: Academic
    • ADAMS, J. S. Extrarenal production and action of active vitamin D metabolites in human lymphoproliferative disases. In: Vitamin D, edited by D. Feldman, F. H. Glorieux, and J. W. Pike. San Diego, CA: Academic, 1997, p. 903-921.
    • (1997) Vitamin D , pp. 903-921
    • Adams, J.S.1
  • 4
    • 0021847794 scopus 로고
    • 3 sterols by cultured alveolar macrophages from patients with sarcoidosis
    • 3 sterols by cultured alveolar macrophages from patients with sarcoidosis. J. Exp. Med. 161: 755-765, 1985.
    • (1985) J. Exp. Med. , vol.161 , pp. 755-765
    • Adams, J.S.1    Gacad, M.A.2
  • 5
    • 0028093170 scopus 로고
    • Further oxidation of hydroxycalcidiol by calcidiol 24-hydroxylase: A study with the mature enzyme expressed in Escherichia coli
    • AKIYOSHI-SHIBATA, M., T. SAKAKI, Y. OHYAMA, M. NOSHIRO, K. OKUDA, AND Y. YABUSAKI. Further oxidation of hydroxycalcidiol by calcidiol 24-hydroxylase: a study with the mature enzyme expressed in Escherichia coli. Eur. J. Biochem. 224: 335-343, 1994.
    • (1994) Eur. J. Biochem. , vol.224 , pp. 335-343
    • Akiyoshi-Shibata, M.1    Sakaki, T.2    Ohyama, Y.3    Noshiro, M.4    Okuda, K.5    Yabusaki, Y.6
  • 6
    • 0029149894 scopus 로고
    • 3: Direct inhibition of NFATp/AP-1 complex formation by a nuclear hormone receptor
    • 3: direct inhibition of NFATp/AP-1 complex formation by a nuclear hormone receptor. Mol. Cell. Biol. 15: 5789-5799, 1994.
    • (1994) Mol. Cell. Biol. , vol.15 , pp. 5789-5799
    • Alroy, I.1    Towers, T.L.2    Freedman, L.P.3
  • 7
    • 0024394549 scopus 로고
    • Cloning, structure and expression of the mitochondrial cytochrome P-450 sterol 26-hydroxylase, a bile acid biosynthetic enzyme
    • ANDERSSON, S., D. L. DAVIS, H. DAHLBACK, AND H. JORNVALL. Cloning, structure and expression of the mitochondrial cytochrome P-450 sterol 26-hydroxylase, a bile acid biosynthetic enzyme. J. Biol. Chem. 264: 8222-8229, 1989.
    • (1989) J. Biol. Chem. , vol.264 , pp. 8222-8229
    • Andersson, S.1    Davis, D.L.2    Dahlback, H.3    Jornvall, H.4
  • 11
    • 3643070537 scopus 로고
    • Cholecalciferol 23-yne derivatives, their pharmaceutical compositions, their use in the treatment of calcium-related diseases, and their antitumor activity, US 4,804,502
    • BAGGIOLINI, E. G., J. J. PARTRIDGE, S. J. SHIVEY, G. A. TRUITT, AND M. R. VSKOKOVIC. Cholecalciferol 23-yne derivatives, their pharmaceutical compositions, their use in the treatment of calcium-related diseases, and their antitumor activity, US 4,804,502. Chem. Abstr. 111: 58160d, 1989.
    • (1989) Chem. Abstr. , vol.111
    • Baggiolini, E.G.1    Partridge, J.J.2    Shivey, S.J.3    Truitt, G.A.4    Vskokovic, M.R.5
  • 16
    • 0028132146 scopus 로고
    • In vivo regulation of rat intestinal 24-hydroxylase: Potential new role of calcitonin
    • BECKMAN, M. J., J. P. GOFF, T. A. REINHARDT, D. C. BEITZ, AND R. L. HORST. In vivo regulation of rat intestinal 24-hydroxylase: potential new role of calcitonin. Endocrinology 135: 11951-1955, 1994.
    • (1994) Endocrinology , vol.135 , pp. 11951-11955
    • Beckman, M.J.1    Goff, J.P.2    Reinhardt, T.A.3    Beitz, D.C.4    Horst, R.L.5
  • 17
    • 0015987155 scopus 로고
    • Selective binding properties of vitamin D transport proteins in chick plasma in vitro
    • BELSEY, R. E., H. F. DELUCA, AND J. T. POTTS. Selective binding properties of vitamin D transport proteins in chick plasma in vitro. Nature 247: 208-209, 1974.
    • (1974) Nature , vol.247 , pp. 208-209
    • Belsey, R.E.1    Deluca, H.F.2    Potts, J.T.3
  • 19
    • 0021089040 scopus 로고
    • 3 in human peripheral blood mononuclear cells. Presence in monocytes and induction in T lymphocytes following activation
    • 3 in human peripheral blood mononuclear cells. Presence in monocytes and induction in T lymphocytes following activation. J. Clin. Endocrinol. 57: 1308-1311, 1983.
    • (1983) J. Clin. Endocrinol. , vol.57 , pp. 1308-1311
    • Bhalla, A.K.1    Amento, E.P.2    Clemens, T.L.3    Holick, M.F.4    Krane, S.M.5
  • 20
    • 0015919728 scopus 로고
    • The regulation of the rat liver calciferol-25-hydroxylase
    • BHATTACHARYYA, M. H., AND H. F. DELUCA. The regulation of the rat liver calciferol-25-hydroxylase. J. Biol. Chem. 248: 2969-2973, 1973.
    • (1973) J. Biol. Chem. , vol.248 , pp. 2969-2973
    • Bhattacharyya, M.H.1    Deluca, H.F.2
  • 21
    • 0042757918 scopus 로고    scopus 로고
    • Vitamin D and skin
    • edited by D. Feldman, F. H. Glorieux, and J. W. Pike. San Diego, CA: Academic, chapt. 25
    • BIKLE, D. D. Vitamin D and skin. In: Vitamin D, edited by D. Feldman, F. H. Glorieux, and J. W. Pike. San Diego, CA: Academic, 1997, chapt. 25, p. 379-394.
    • (1997) Vitamin D , pp. 379-394
    • Bikle, D.D.1
  • 23
    • 0002038198 scopus 로고
    • Synthesis and biological activity of 1-hydroxylated vitamin D analogues with polyunsaturated side chains
    • edited by A. W. Norman, R. Bouillon, and M. Thomasset. Berlin: de Gruyter
    • BINDERUP, E., M. J. CALVERLY, AND L. BINDERUP. Synthesis and biological activity of 1-hydroxylated vitamin D analogues with polyunsaturated side chains. In: Vitamin D: Gene Regulation, Structure-function Analysis and Clinical Application, edited by A. W. Norman, R. Bouillon, and M. Thomasset. Berlin: de Gruyter, 1991, p. 192-193.
    • (1991) Vitamin D: Gene Regulation, Structure-function Analysis and Clinical Application , pp. 192-193
    • Binderup, E.1    Calverly, M.J.2    Binderup, L.3
  • 24
    • 0023873187 scopus 로고
    • Effects of a novel vitamin D analog MC903 on cell proliferation and differentiation in vitro and on calcium metabolism in vivo
    • BINDERUP, L., AND E. BRAMM. Effects of a novel vitamin D analog MC903 on cell proliferation and differentiation in vitro and on calcium metabolism in vivo. Biochem. Pharmacol. 37: 889-895, 1988.
    • (1988) Biochem. Pharmacol. , vol.37 , pp. 889-895
    • Binderup, L.1    Bramm, E.2
  • 29
    • 3643134031 scopus 로고    scopus 로고
    • 2 vitamin D analogs: E-ring analogs
    • edited by A. W. Norman, R. Bouillon, and M. Thomasset. Riverside: Univ. of California
    • 2 vitamin D analogs: E-ring analogs. In: Vitamin D. Chemistry, Biology and Clinical Applications of the Steroid Hormone, edited by A. W. Norman, R. Bouillon, and M. Thomasset. Riverside: Univ. of California, 1997, p. 59-64.
    • (1997) Vitamin D. Chemistry, Biology and Clinical Applications of the Steroid Hormone , pp. 59-64
    • Bouillon, R.1
  • 30
    • 0025989583 scopus 로고
    • Vitamin D analogs with low affinity for the vitamin D binding protein: Enhanced in vitro and decreased in vivo activity
    • BOUILLON, R., K. ALLEWAERT, D. Z. XIANG, B. K. TAN, AND H. VAN BAELEN. Vitamin D analogs with low affinity for the vitamin D binding protein: enhanced in vitro and decreased in vivo activity. J. Bone Miner. Res. 6: 1051-1057, 1991.
    • (1991) J. Bone Miner. Res. , vol.6 , pp. 1051-1057
    • Bouillon, R.1    Allewaert, K.2    Xiang, D.Z.3    Tan, B.K.4    Van Baelen, H.5
  • 31
    • 0028988403 scopus 로고
    • Structure-function relationships in the vitamin D endocrine system
    • BOUILLON, R., W. H. OKAMURA, AND A. W. NORMAN. Structure-function relationships in the vitamin D endocrine system. Endocr. Rev. 16: 200-257, 1995.
    • (1995) Endocr. Rev. , vol.16 , pp. 200-257
    • Bouillon, R.1    Okamura, W.H.2    Norman, A.W.3
  • 32
    • 0029012163 scopus 로고
    • Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-α
    • BOURGUET, W., M. RUFF, P. CHAMBON, H. GRONEMEYER, AND D. MORAS. Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-α. Nature 375: 377-382, 1995.
    • (1995) Nature , vol.375 , pp. 377-382
    • Bourguet, W.1    Ruff, M.2    Chambon, P.3    Gronemeyer, H.4    Moras, D.5
  • 33
    • 0002344083 scopus 로고    scopus 로고
    • 3
    • edited by D. Feldman, F. H. Glorieux, and J. W. Pike. San Diego, CA: Academic, chapt. 26
    • 3. In: Vitamin D, edited by D. Feldman, F. H. Glorieux, and J. W. Pike. San Diego, CA: Academic, 1997, chapt. 26, p. 395-421.
    • (1997) Vitamin D , pp. 395-421
    • Boyan, B.D.1    Dean, D.D.2    Sylvia, V.L.3    Schwartz, Z.4
  • 35
    • 0015308498 scopus 로고
    • The response of intestinal calcium transport to 25-hydroxyvitamin D in nephrectomized rats
    • BOYLE, I. T., L. MIRAVET, R. W. GRAY, M. F. HOLICK, AND H. F. DELUCA. The response of intestinal calcium transport to 25-hydroxyvitamin D in nephrectomized rats. Endocrinology 90: 605-608, 1972.
    • (1972) Endocrinology , vol.90 , pp. 605-608
    • Boyle, I.T.1    Miravet, L.2    Gray, R.W.3    Holick, M.F.4    Deluca, H.F.5
  • 37
    • 0021398385 scopus 로고
    • A maternal defect is responsible for the growth failure in vitamin D-deficient rat pups
    • Endocrinol. Metab. 19
    • BROMMAGE, R., AND H. F. DELUCA. A maternal defect is responsible for the growth failure in vitamin D-deficient rat pups. Am. J. Physiol. 256 (Endocrinol. Metab. 19): E216-E220, 1984.
    • (1984) Am. J. Physiol. , vol.256
    • Brommage, R.1    Deluca, H.F.2
  • 40
    • 0028318182 scopus 로고
    • 3 cooperate to promote differentiation of the human promyeloid leukemia cell line HL60 to monocytes
    • 3 cooperate to promote differentiation of the human promyeloid leukemia cell line HL60 to monocytes. Leukemia 8: 806-815, 1994.
    • (1994) Leukemia , vol.8 , pp. 806-815
    • Brown, G.1    Bunce, C.M.2    Rowlands, D.C.3    Williams, G.R.4
  • 44
    • 0025868097 scopus 로고
    • Characterization of human sterol 27-hydroxylase. A mitochondrial cytochrome P-450 that catalyzes multiple oxidation reactions in bile acid biosynthesis
    • CALI, J. J., AND D. W. RUSSELL. Characterization of human sterol 27-hydroxylase. A mitochondrial cytochrome P-450 that catalyzes multiple oxidation reactions in bile acid biosynthesis. J. Biol. Chem. 266: 7774-7778, 1991.
    • (1991) J. Biol. Chem. , vol.266 , pp. 7774-7778
    • Cali, J.J.1    Russell, D.W.2
  • 45
    • 0023555287 scopus 로고
    • Synthesis of MC-903, a biologically active vitamin D metabolite analog
    • CALVERLEY, M. J. Synthesis of MC-903, a biologically active vitamin D metabolite analog. Tetrahedron 43: 4609-4619, 1987.
    • (1987) Tetrahedron , vol.43 , pp. 4609-4619
    • Calverley, M.J.1
  • 46
    • 0004482370 scopus 로고
    • The 20-epi modification in the vitamin D series: Selective enhancement of "non-classical" receptor-mediated effects
    • edited by A. W. Norman, R. Bouillon, and M. Thomasset. Berlin: de Gruyter
    • CALVERLEY, M. J., E. BINDERUP, AND L. BINDERUP. The 20-epi modification in the vitamin D series: selective enhancement of "non-classical" receptor-mediated effects. In: Vitamin D: Gene Regulation, Structure-Function Analysis and Clinical Application, edited by A. W. Norman, R. Bouillon, and M. Thomasset. Berlin: de Gruyter, 1991, p. 163-164.
    • (1991) Vitamin D: Gene Regulation, Structure-Function Analysis and Clinical Application , pp. 163-164
    • Calverley, M.J.1    Binderup, E.2    Binderup, L.3
  • 47
    • 0001086707 scopus 로고
    • Vitamin D
    • edited by B. R. T. Toronto. Orlando, FL: Academic
    • CALVERLEY, M. J., AND G. JONES. Vitamin D. In: Antitumor Steroids, edited by B. R. T. Toronto. Orlando, FL: Academic, 1992, p. 193-270.
    • (1992) Antitumor Steroids , pp. 193-270
    • Calverley, M.J.1    Jones, G.2
  • 48
    • 0030032309 scopus 로고    scopus 로고
    • A composite element binding the vitamin D receptor, retinoid X receptor α, and a member of CTF/NF-1 family of transcription factors mediates the vitamin D responsiveness of the c-fos promoter
    • CANDELIERE, G. A., P. W. JURUTKA, M. R. HAUSSLER, AND R. ST-ARNAUD. A composite element binding the vitamin D receptor, retinoid X receptor α, and a member of CTF/NF-1 family of transcription factors mediates the vitamin D responsiveness of the c-fos promoter. Mol. Cell. Biol. 16: 584-92, 1996.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 584-592
    • Candeliere, G.A.1    Jurutka, P.W.2    Haussler, M.R.3    St-Arnaud, R.4
  • 50
    • 0031908097 scopus 로고    scopus 로고
    • 3 prevents and ameliorates symptoms in two experimental models of human arthritis
    • 3 prevents and ameliorates symptoms in two experimental models of human arthritis. J. Nutr. 128: 68-72, 1998.
    • (1998) J. Nutr. , vol.128 , pp. 68-72
    • Cantorna, M.T.1    Hayes, C.E.2    Deluca, H.F.3
  • 51
    • 0032103001 scopus 로고    scopus 로고
    • 3 is a positive regulator for the two anti-encephalitogenic cytokines TGF-β1 and IL-4
    • 3 is a positive regulator for the two anti-encephalitogenic cytokines TGF-β1 and IL-4. J. Immunol. 160: 5314-5319, 1998.
    • (1998) J. Immunol. , vol.160 , pp. 5314-5319
    • Cantorna, M.T.1    Woodward, W.D.2    Hayes, C.E.3    Deluca, H.F.4
  • 53
    • 0029099609 scopus 로고
    • 3: Interplay with retinoid and thyroid hormone signalling
    • 3: interplay with retinoid and thyroid hormone signalling. Eur. J. Biochem. 231: 517-527, 1995.
    • (1995) Eur. J. Biochem. , vol.231 , pp. 517-527
    • Carlberg, C.1
  • 55
    • 0028170822 scopus 로고
    • 3 (VD) analogues MC903, EB1089, and KH1060 activate the VD receptor: Homodimers show higher ligand sensitivity than heterodimers with retinoid X receptors
    • 3 (VD) analogues MC903, EB1089, and KH1060 activate the VD receptor: homodimers show higher ligand sensitivity than heterodimers with retinoid X receptors. J. Steroid Biochem. Mol. Biol. 51: 137-142, 1994.
    • (1994) J. Steroid Biochem. Mol. Biol. , vol.51 , pp. 137-142
    • Carlberg, C.1    Mathiasen, I.S.2    Saurat, J.H.3    Binderup, L.4
  • 57
    • 0020043385 scopus 로고
    • Calcitonin alters behaviour of isolated osteoclasts
    • CHAMBERS, T. J., AND C. J. MAGNUS. Calcitonin alters behaviour of isolated osteoclasts. J. Pathol. 136: 27-39, 1982.
    • (1982) J. Pathol. , vol.136 , pp. 27-39
    • Chambers, T.J.1    Magnus, C.J.2
  • 58
    • 0029794132 scopus 로고    scopus 로고
    • A decade of molecular biology of retinoic acid receptors
    • CHAMBON, P. A decade of molecular biology of retinoic acid receptors. FASEB J. 10: 940-954, 1996.
    • (1996) FASEB J. , vol.10 , pp. 940-954
    • Chambon, P.1
  • 59
    • 0030740253 scopus 로고    scopus 로고
    • Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P/CAF and CBP/p300
    • CHEN, H., R. J. LIN, R. L. SCHLITZ, D. CHAKRAVART, A. NASH, L. NAGY, M. L. PRIVALSKY, Y. NAKATANI, AND R. M. EVANS. Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P/CAF and CBP/p300. Cell 90: 569-580, 1997.
    • (1997) Cell , vol.90 , pp. 569-580
    • Chen, H.1    Lin, R.J.2    Schlitz, R.L.3    Chakravart, D.4    Nash, A.5    Nagy, L.6    Privalsky, M.L.7    Nakatani, Y.8    Evans, R.M.9
  • 60
    • 0029097233 scopus 로고
    • A transcriptional co-repressor that interacts with nuclear hormone receptors
    • CHEN, J. D., AND R. M. EVANS. A transcriptional co-repressor that interacts with nuclear hormone receptors. Nature 377: 454-457, 1995.
    • (1995) Nature , vol.377 , pp. 454-457
    • Chen, J.D.1    Evans, R.M.2
  • 61
    • 0028982622 scopus 로고
    • 3 24-hydroxylase gene and identification of two vitamin D-responsive elements
    • 3 24-hydroxylase gene and identification of two vitamin D-responsive elements. Biochim. Biophys. Acta 1263: 1-9, 1995.
    • (1995) Biochim. Biophys. Acta , vol.1263 , pp. 1-9
    • Chen, K.S.1    Deluca, H.F.2
  • 63
    • 0016227717 scopus 로고
    • Role of vitamin D metabolites in phosphate transport of rat intestine
    • CHEN, T. C., L. CASTILLO, M. KORYCKA-DAHL, AND H. F. DELUCA. Role of vitamin D metabolites in phosphate transport of rat intestine. J. Nutr. 104: 1056-1060, 1974.
    • (1974) J. Nutr. , vol.104 , pp. 1056-1060
    • Chen, T.C.1    Castillo, L.2    Korycka-Dahl, M.3    Deluca, H.F.4
  • 64
    • 0028301243 scopus 로고
    • Characterization of the ligand binding domain of human retinoid X receptor α expressed in Escherichia coli
    • CHENG, L., A. W. NORRIS, B. F. TATE, M. ROSENBERGER, J. F. GRIPPO, AND E. LI. Characterization of the ligand binding domain of human retinoid X receptor α expressed in Escherichia coli. J. Biol. Chem. 269: 18662-18667, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 18662-18667
    • Cheng, L.1    Norris, A.W.2    Tate, B.F.3    Rosenberger, M.4    Grippo, J.F.5    Li, E.6
  • 65
    • 0020572230 scopus 로고
    • Cellular mechanisms of insulin release. The effects of vitamin D deficiency and repletion of the rat insulin secretion
    • CHERTOW, B. S., W. I. SIVITZ, N. G. BARANETSKY, S. A. CLARK, A. WAITE, AND H. F. DELUCA. Cellular mechanisms of insulin release. The effects of vitamin D deficiency and repletion of the rat insulin secretion. Endocrinology 113: 1511-1518, 1983.
    • (1983) Endocrinology , vol.113 , pp. 1511-1518
    • Chertow, B.S.1    Sivitz, W.I.2    Baranetsky, N.G.3    Clark, S.A.4    Waite, A.5    Deluca, H.F.6
  • 66
    • 0022531044 scopus 로고
    • Islet insulin release and net calcium retention in vitro in vitamin D-deficient rats
    • CHERTOW, B. S., W. I. SIVITZ, N. G. BARANETSKY, M. B. CORDLE, AND H. F. DELUCA. Islet insulin release and net calcium retention in vitro in vitamin D-deficient rats. Diabetes 35: 771-775, 1986.
    • (1986) Diabetes , vol.35 , pp. 771-775
    • Chertow, B.S.1    Sivitz, W.I.2    Baranetsky, N.G.3    Cordle, M.B.4    Deluca, H.F.5
  • 68
    • 0000836739 scopus 로고    scopus 로고
    • 28K
    • edited by D. Feldman, F. H. Glorieux, and J. W. Pike. San Diego, CA: Academic, chapt. 13
    • 28K. In: Vitamin D, edited by D. Feldman, F. H. Glorieux, and J. W. Pike. San Diego, CA: Academic, 1997, chapt. 13, p. 209-221.
    • (1997) Vitamin D , pp. 209-221
    • Christakos, S.1    Beck, J.D.2    Hyllner, S.J.3
  • 69
    • 0026535453 scopus 로고
    • Molecular aspects of the calbindins
    • CHRISTAKOS, S., R. GILL, S. LEE, AND H. LI. Molecular aspects of the calbindins. J. Nutr. 122: 678-682, 1992.
    • (1992) J. Nutr. , vol.122 , pp. 678-682
    • Christakos, S.1    Gill, R.2    Lee, S.3    Li, H.4
  • 70
    • 0003094062 scopus 로고    scopus 로고
    • Vitamin D binding protein
    • edited by D. Feldman, F. H. Glorieux, and J. W. Pike. San Diego, CA: Academic
    • COOKE, N. C., AND J. G. HADDAD. Vitamin D binding protein. In: Vitamin D, edited by D. Feldman, F. H. Glorieux, and J. W. Pike. San Diego, CA: Academic, 1997, p. 87-101.
    • Vitamin D , vol.1997 , pp. 87-101
    • Cooke, N.C.1    Haddad, J.G.2
  • 71
    • 0029059719 scopus 로고
    • Retinoid receptors cause distortion of the retinoic acid response element in the phosphoenolpyruvate carboxykinase gene promoter
    • COTT, D. K., R. K. HALL, AND D. K. GRANNER. Retinoid receptors cause distortion of the retinoic acid response element in the phosphoenolpyruvate carboxykinase gene promoter. Biochem. J. 310: 483-490, 1995.
    • (1995) Biochem. J. , vol.310 , pp. 483-490
    • Cott, D.K.1    Hall, R.K.2    Granner, D.K.3
  • 72
    • 0004482369 scopus 로고
    • 3 receptor on sodium dodecyl sulfate/polyacrylamide gels by renaturation and immunoblotting
    • 3 receptor on sodium dodecyl sulfate/polyacrylamide gels by renaturation and immunoblotting. Proc. Natl. Acad. Sci. USA 82: 7825-7829, 1985.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 7825-7829
    • Dame, M.C.1    Pierce, E.A.2    Deluca, H.F.3
  • 75
    • 0029691514 scopus 로고    scopus 로고
    • Recent advances in the molecular biology of vitamin D action
    • DARWISH, H. M., AND H. F. DELUCA. Recent advances in the molecular biology of vitamin D action. Prog. Nucleic Acid Res. Mol. Biol. 53: 321-344, 1996.
    • (1996) Prog. Nucleic Acid Res. Mol. Biol. , vol.53 , pp. 321-344
    • Darwish, H.M.1    Deluca, H.F.2
  • 76
    • 0030588233 scopus 로고    scopus 로고
    • 3 receptor to positive and negative vitamin D response elements
    • 3 receptor to positive and negative vitamin D response elements. Arch. Biochem. Biophys. 334: 223-234, 1996.
    • (1996) Arch. Biochem. Biophys. , vol.334 , pp. 223-234
    • Darwish, H.M.1    Deluca, H.F.2
  • 77
    • 0023407184 scopus 로고
    • Molecular cloning of the cDNA and chromosomal gene for vitamin D-dependent calcium-binding protein of rat intestine
    • DARWISH, H. M., J. KRISINGER, M. STROM, AND H. F. DELUCA. Molecular cloning of the cDNA and chromosomal gene for vitamin D-dependent calcium-binding protein of rat intestine. Proc. Natl. Acad. Sci. USA 84: 6108-6111, 1987.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 6108-6111
    • Darwish, H.M.1    Krisinger, J.2    Strom, M.3    Deluca, H.F.4
  • 79
    • 3643085150 scopus 로고
    • Active compounds
    • edited by W. H. Sebrell, Jr., and R. S. Harris. New York: Academic, chapt. IV
    • DELUCA, H. F. Active compounds. In: The Vitamins. Chemistry, Physiology, Pathology, Methods, edited by W. H. Sebrell, Jr., and R. S. Harris. New York: Academic, 1971, chapt. IV, p. 223-232.
    • (1971) The Vitamins. Chemistry, Physiology, Pathology, Methods , pp. 223-232
    • Deluca, H.F.1
  • 80
    • 0018401913 scopus 로고
    • Vitamin D: Metabolism and function
    • edited by F. Gross, M. M. Grumbach, A. Labhart, M. B. Lipsett, T. Mann, L. T. Samuels, and J. Zander. New York: Springer-Verlag
    • DELUCA, H. F. Vitamin D: metabolism and function. In: Monographs on Endocrinology, edited by F. Gross, M. M. Grumbach, A. Labhart, M. B. Lipsett, T. Mann, L. T. Samuels, and J. Zander. New York: Springer-Verlag, 1979, p. 1-78.
    • (1979) Monographs on Endocrinology , pp. 1-78
    • Deluca, H.F.1
  • 81
    • 0018658290 scopus 로고
    • The transformation of a vitamin into a hormone: The vitamin D story
    • New York: Academic, ser. 75
    • DELUCA, H. F. The transformation of a vitamin into a hormone: the vitamin D story. In: The Harvey Lectures. New York: Academic, 1981, ser. 75, p. 333-379.
    • (1981) The Harvey Lectures , pp. 333-379
    • Deluca, H.F.1
  • 83
    • 0023110868 scopus 로고
    • Kinetics and regulation of 25-hydroxycholecalciferol 1α-hydroxylase from cells isolated from human term decidua
    • DELVIN, E. E., AND A. ARABIAN. Kinetics and regulation of 25-hydroxycholecalciferol 1α-hydroxylase from cells isolated from human term decidua. Eur. J. Biochem. 164: 659-662, 1987.
    • (1987) Eur. J. Biochem. , vol.164 , pp. 659-662
    • Delvin, E.E.1    Arabian, A.2
  • 87
    • 0030698176 scopus 로고    scopus 로고
    • The vitamin D analog KH1060 is rapidly degraded both in vivo and in vitro via several pathways: Principal metabolites generated retain significant biological activity
    • DILWORTH, F. J., G. R. WILLIAMS, A.-M. KISSMEYER, J. LOGSTED-MIELSEN, E. BINDERUP, M. J. CALVERLEY, H. L. J. MAKIN, AND G. JONES. The vitamin D analog KH1060 is rapidly degraded both in vivo and in vitro via several pathways: principal metabolites generated retain significant biological activity. Endocrinology 138: 5485-5496, 1997.
    • (1997) Endocrinology , vol.138 , pp. 5485-5496
    • Dilworth, F.J.1    Williams, G.R.2    Kissmeyer, A.-M.3    Logsted-Mielsen, J.4    Binderup, E.5    Calverley, M.J.6    Makin, H.L.J.7    Jones, G.8
  • 92
    • 0028006619 scopus 로고
    • The avian vitamin D receptors: Primary structures and their origins
    • ELAROUSSI, M. A., J. M. PRAHL, AND H. F. DELUCA. The avian vitamin D receptors: primary structures and their origins. Proc. Natl. Acad. Sci. USA 91: 11596-11600, 1994.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 11596-11600
    • Elaroussi, M.A.1    Prahl, J.M.2    Deluca, H.F.3
  • 93
    • 0030611744 scopus 로고    scopus 로고
    • 2 partially dissociates between preservation of cancellous bone mass and effects on calcium homeostasis in ovarectomized rats
    • 2 partially dissociates between preservation of cancellous bone mass and effects on calcium homeostasis in ovarectomized rats. Calcif. Tissue Int. 60: 449-456, 1997.
    • (1997) Calcif. Tissue Int. , vol.60 , pp. 449-456
    • Erben, R.G.1    Bante, U.2    Birner, H.3    Stangassinger, M.4
  • 95
    • 0023913120 scopus 로고
    • The steroid and thyroid hormone receptor superfamily
    • EVANS, R. M. The steroid and thyroid hormone receptor superfamily. Science 240: 889-895, 1988.
    • (1988) Science , vol.240 , pp. 889-895
    • Evans, R.M.1
  • 97
    • 0004208435 scopus 로고
    • New York: Reinhold
    • FIESER, L. F., AND M. FIESER. Steroids. New York: Reinhold, 1959, p. 144-146.
    • (1959) Steroids , pp. 144-146
    • Fieser, L.F.1    Fieser, M.2
  • 98
    • 0029002298 scopus 로고
    • Unique response pathways are established by allosteric interactions among nuclear hormone receptors
    • FORMAN, B. M., K. UMESONO, H. CHEN, AND R. M. EVANS. Unique response pathways are established by allosteric interactions among nuclear hormone receptors. Cell 81: 541-550, 1995.
    • (1995) Cell , vol.81 , pp. 541-550
    • Forman, B.M.1    Umesono, K.2    Chen, H.3    Evans, R.M.4
  • 100
    • 0014958183 scopus 로고
    • Unique biosynthesis by kidney of a biologically active vitamin D metabolite
    • FRASER, D. R., AND E. KODICEK. Unique biosynthesis by kidney of a biologically active vitamin D metabolite. Nature 228: 764-766, 1970.
    • (1970) Nature , vol.228 , pp. 764-766
    • Fraser, D.R.1    Kodicek, E.2
  • 101
    • 0028310263 scopus 로고
    • Cellular mode of action of parathyroid hormone
    • FRIEDLANDER, G., AND C. AMIEL. Cellular mode of action of parathyroid hormone. Adv. Nephrol 23: 265-279, 1994.
    • (1994) Adv. Nephrol , vol.23 , pp. 265-279
    • Friedlander, G.1    Amiel, C.2
  • 102
    • 0030782757 scopus 로고    scopus 로고
    • Cloning of human 25-hydroxyvitamin D-1α-hydroxylase and mutations causing vitamin D-dependent rickets type 1
    • FU, G. K., D. LIN, M. Y. H. ZHANG, D. D. BIKLE, C. H. L. SHACKLETON, W. L. MILLER, AND A. A. PORTALE. Cloning of human 25-hydroxyvitamin D-1α-hydroxylase and mutations causing vitamin D-dependent rickets type 1. Mol. Endocrinol. 11: 1961-1970, 1997.
    • (1997) Mol. Endocrinol. , vol.11 , pp. 1961-1970
    • Fu, G.K.1    Lin, D.2    Zhang, M.Y.H.3    Bikle, D.D.4    Shackleton, C.H.L.5    Miller, W.L.6    Portale, A.A.7
  • 103
    • 0031410426 scopus 로고    scopus 로고
    • Complete structure of the human gene for the vitamin D 1α-hydroxylase, P450c1α
    • FU, G. K., A. A. PORTALE, AND W. L. MILLER. Complete structure of the human gene for the vitamin D 1α-hydroxylase, P450c1α. DNA Cell Biol. 16: 1499-1507, 1997.
    • (1997) DNA Cell Biol. , vol.16 , pp. 1499-1507
    • Fu, G.K.1    Portale, A.A.2    Miller, W.L.3
  • 107
    • 0025272220 scopus 로고
    • 3 on calcium balance and bone turnover and its effect on vertebral fracture rate
    • 3 on calcium balance and bone turnover and its effect on vertebral fracture rate. Metabolism 39: 30-34, 1990.
    • (1990) Metabolism , vol.39 , pp. 30-34
    • Gallagher, J.C.1    Riggs, B.L.2
  • 108
    • 0024320850 scopus 로고
    • The effect of calcitriol on patients with postmenopausal osteoporosis with special reference to fracture frequency
    • GALLAGHER, J. C., B. L. RIGGS, R. R. RECKER, AND D. GOLDGAR. The effect of calcitriol on patients with postmenopausal osteoporosis with special reference to fracture frequency. Proc. Soc. Exp. Biol. Med. 191: 287-292, 1989.
    • (1989) Proc. Soc. Exp. Biol. Med. , vol.191 , pp. 287-292
    • Gallagher, J.C.1    Riggs, B.L.2    Recker, R.R.3    Goldgar, D.4
  • 109
    • 0015367525 scopus 로고
    • Control of 25-hydroxycholecalciferol metabolism by the parathyroid glands
    • GARABEDIAN, M., M. F. HOLICK, H. F. DELUCA, AND I. T. BOYLE. Control of 25-hydroxycholecalciferol metabolism by the parathyroid glands. Proc. Natl. Acad. Sci. USA 69: 1673-1676, 1972.
    • (1972) Proc. Natl. Acad. Sci. USA , vol.69 , pp. 1673-1676
    • Garabedian, M.1    Holick, M.F.2    Deluca, H.F.3    Boyle, I.T.4
  • 111
    • 0025041449 scopus 로고
    • 3 endocrine complex. How are they regulated at the molecular level?
    • 3 endocrine complex. How are they regulated at the molecular level? J. Bone Miner. Res. 5: 897-903, 1990.
    • (1990) J. Bone Miner. Res. , vol.5 , pp. 897-903
    • Ghazarian, J.G.1
  • 112
    • 0016159925 scopus 로고
    • Mitochondrial cytochrome P-450. A component of chick kidney 25-hydroxycholecalciferol-1α-hydroxylase
    • GHAZARIAN, J. G., C. R. JEFCOATE, J. C. KNUTSON, W. ORME-JOHNSON, AND H. F. DELUCA. Mitochondrial cytochrome P-450. A component of chick kidney 25-hydroxycholecalciferol-1α-hydroxylase. J. Biol. Chem. 249: 3026-3033, 1974.
    • (1974) J. Biol. Chem. , vol.249 , pp. 3026-3033
    • Ghazarian, J.G.1    Jefcoate, C.R.2    Knutson, J.C.3    Orme-Johnson, W.4    Deluca, H.F.5
  • 114
    • 0018938515 scopus 로고
    • Lack of direct effect of 1,25-dihydroxycholecalciferol on parathyroid hormone secretion by normal bovine parathyroid glands
    • GOLDEN, P., A. GREENWALT, K. MARTIN, E. BELLORIN-FONT, R. MAZEY, S. KLAHR, AND E. SLATOPOLSKY. Lack of direct effect of 1,25-dihydroxycholecalciferol on parathyroid hormone secretion by normal bovine parathyroid glands. Endocrinology 107: 602-607, 1980.
    • (1980) Endocrinology , vol.107 , pp. 602-607
    • Golden, P.1    Greenwalt, A.2    Martin, K.3    Bellorin-Font, E.4    Mazey, R.5    Klahr, S.6    Slatopolsky, E.7
  • 117
    • 0015502105 scopus 로고
    • 25-Hydroxycholecalciferol-1α-hydroxylase: Subcellular distribution and properties
    • GRAY, R. W., J. L. OMDAHL, J. G. GHAZARIAN, AND H. F. DELUCA. 25-Hydroxycholecalciferol-1α-hydroxylase: subcellular distribution and properties. J. Biol. Chem. 247: 7528-7532, 1972.
    • (1972) J. Biol. Chem. , vol.247 , pp. 7528-7532
    • Gray, R.W.1    Omdahl, J.L.2    Ghazarian, J.G.3    Deluca, H.F.4
  • 118
    • 3643129894 scopus 로고
    • 3-25-hydroxylase (CYP27) lacks a classical VDRE but contains silencer sequence
    • 3-25-hydroxylase (CYP27) lacks a classical VDRE but contains silencer sequence (Abstract). J. Bone Miner. Res. 9: S289, 1994.
    • (1994) J. Bone Miner. Res. , vol.9
    • Guo, Y.-D.1    Jones, G.2
  • 119
    • 0027305109 scopus 로고
    • Transfected human liver cytochrome P-450 hydroxylates vitamin D analogs at different side-chain positions
    • GUO, Y.-D., S. STRUGNELL, D. W. BACK, AND G. JONES. Transfected human liver cytochrome P-450 hydroxylates vitamin D analogs at different side-chain positions. Proc. Natl. Acad. Sci. USA 90: 8668-8672, 1993.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 8668-8672
    • Guo, Y.-D.1    Strugnell, S.2    Back, D.W.3    Jones, G.4
  • 120
    • 0025820544 scopus 로고
    • Cloning of a human gene encoding the general transcription initiation factor IIB
    • HA, I., W. S. LANE, AND D. REINBERG. Cloning of a human gene encoding the general transcription initiation factor IIB. Nature 352: 689-695, 1991.
    • (1991) Nature , vol.352 , pp. 689-695
    • Ha, I.1    Lane, W.S.2    Reinberg, D.3
  • 121
    • 0018777769 scopus 로고
    • Vitamin D deficiency and reproduction in rats
    • HALLORAN, B. P., AND H. F. DELUCA. Vitamin D deficiency and reproduction in rats. Science 204: 73-74, 1979.
    • (1979) Science , vol.204 , pp. 73-74
    • Halloran, B.P.1    Deluca, H.F.2
  • 122
    • 0019136483 scopus 로고
    • Effect of vitamin D deficiency on fertility and reproductive capacity in the female rat
    • HALLORAN, B. P., AND H. F. DELUCA. Effect of vitamin D deficiency on fertility and reproductive capacity in the female rat. J. Nutr. 110: 1573-1580, 1980.
    • (1980) J. Nutr. , vol.110 , pp. 1573-1580
    • Halloran, B.P.1    Deluca, H.F.2
  • 125
    • 3643115386 scopus 로고
    • Calcium-binding protein and calcium absorption after vitamin D administration
    • HARMEYER, J., AND H. F. DELUCA. Calcium-binding protein and calcium absorption after vitamin D administration. Biochem. J. 170: 93-102, 1969.
    • (1969) Biochem. J. , vol.170 , pp. 93-102
    • Harmeyer, J.1    Deluca, H.F.2
  • 126
    • 0040446313 scopus 로고
    • Intestinal transport of phosphate: Action of vitamin D. calcium, and potassium
    • HARRISON, H. E., AND H. C. HARRISON. Intestinal transport of phosphate: action of vitamin D. calcium, and potassium. Am. J. Physiol. 201: 1007-1012, 1961.
    • (1961) Am. J. Physiol. , vol.201 , pp. 1007-1012
    • Harrison, H.E.1    Harrison, H.C.2
  • 127
    • 0022509794 scopus 로고
    • Vitamin D receptors: Nature and function
    • HAUSSLER, M. R. Vitamin D receptors: nature and function. Annu. Rev. Nutr. 6: 527-562, 1986.
    • (1986) Annu. Rev. Nutr. , vol.6 , pp. 527-562
    • Haussler, M.R.1
  • 128
    • 0029082307 scopus 로고
    • New understanding of the molecular mechanism of receptor-mediated genomic actions of the vitamin D hormone
    • HAUSSLER, M. R., P. W. JURUTKA, J. C. HSIEH, P. D. THOMPSON, S. H. SELZNICK, C. A. HAUSSLER, AND G. K. WHITFIELD. New understanding of the molecular mechanism of receptor-mediated genomic actions of the vitamin D hormone. Bone 17, Suppl.: 33S-38S, 1995.
    • (1995) Bone , vol.17 , Issue.SUPPL.
    • Haussler, M.R.1    Jurutka, P.W.2    Hsieh, J.C.3    Thompson, P.D.4    Selznick, S.H.5    Haussler, C.A.6    Whitfield, G.K.7
  • 129
    • 0023922715 scopus 로고
    • 3 25-hydroxylase of rat liver mitochondria
    • 3 25-hydroxylase of rat liver mitochondria. J. Biochem. 103: 863-866, 1988.
    • (1988) J. Biochem. , vol.103 , pp. 863-866
    • Hayashi, S.1    Usui, E.2    Okuda, K.3
  • 130
    • 0003003486 scopus 로고    scopus 로고
    • Vitamin D: Role in the calcium economy
    • edited by D. Feldman, F. H. Glorieux, and J. W. Pike. San Diego, CA: Academic, chapt. 31
    • HEANEY, R. P. Vitamin D: role in the calcium economy. In: Vitamin D, edited by D. Feldman, F. H. Glorieux, and J. W. Pike. San Diego, CA: Academic, 1997, chapt. 31, p. 485-497.
    • (1997) Vitamin D , pp. 485-497
    • Heaney, R.P.1
  • 132
    • 0002618597 scopus 로고    scopus 로고
    • 3 1α-hydroxylase
    • edited by D. Feldman, F. H. Glorieux, and J. W. Pike. San Diego, CA: Academic
    • 3 1α-hydroxylase. In: Vitamin D, edited by D. Feldman, F. H. Glorieux, and J. W. Pike. San Diego, CA: Academic, 1997, p. 57-68.
    • (1997) Vitamin D , pp. 57-68
    • Henry, H.L.1
  • 135
    • 0028181223 scopus 로고
    • 3 modulates phosphorylation of serine 205 in the human vitamin D receptor: Site-directed mutagenesis of this residue promotes alternative phosphorylation
    • 3 modulates phosphorylation of serine 205 in the human vitamin D receptor: site-directed mutagenesis of this residue promotes alternative phosphorylation. Biochemistry 33: 4300-4311, 1994.
    • (1994) Biochemistry , vol.33 , pp. 4300-4311
    • Hilliard IV, G.M.1    Cook, R.G.2    Weigel, N.L.3    Pike, J.W.4
  • 139
    • 0015212896 scopus 로고
    • Isolation and identification of 1,25-dihydroxycholecalciferol. A metabolite of vitamin D active in the intestine
    • HOLICK, M. F., H. K. SCHNOES, H. F. DELUCA, T. SUDA, AND R. J. COUSINS. Isolation and identification of 1,25-dihydroxycholecalciferol. A metabolite of vitamin D active in the intestine. Biochemistry 10: 2799-2804, 1971.
    • (1971) Biochemistry , vol.10 , pp. 2799-2804
    • Holick, M.F.1    Schnoes, H.K.2    Deluca, H.F.3    Suda, T.4    Cousins, R.J.5
  • 140
    • 0002745656 scopus 로고    scopus 로고
    • Detection of vitamin D and its major metabolites
    • edited by D. Feldman, F. H. Glorieux, and J. W. Pike. San Diego, CA: Academic
    • HOLLIS, B. W. Detection of vitamin D and its major metabolites. In: Vitamin D, edited by D. Feldman, F. H. Glorieux, and J. W. Pike. San Diego, CA: Academic, 1997, p. 587-606.
    • (1997) Vitamin D , pp. 587-606
    • Hollis, B.W.1
  • 145
    • 0018097745 scopus 로고
    • 3 receptors in parathyroid glands. Preliminary characterization of cytoplasmic and nuclear binding components
    • 3 receptors in parathyroid glands. Preliminary characterization of cytoplasmic and nuclear binding components. J. Biol. Chem. 252: 1065-1073, 1978.
    • (1978) J. Biol. Chem. , vol.252 , pp. 1065-1073
    • Hughes, M.R.1    Haussler, M.R.2
  • 149
    • 17644447202 scopus 로고
    • 1- But not 24-hydroxylation of vitamin D is required for growth and reproduction in rats
    • Endocrinol. Metab. 7
    • JARNAGIN, K., R. BROMMAGE, H. F. DELUCA, S. YAMADA, AND H. TAKAYAMA. 1- But not 24-hydroxylation of vitamin D is required for growth and reproduction in rats. Am. J. Physiol. 244 (Endocrinol. Metab. 7): E290-E297, 1983.
    • (1983) Am. J. Physiol. , vol.244
    • Jarnagin, K.1    Brommage, R.2    Deluca, H.F.3    Yamada, S.4    Takayama, H.5
  • 150
    • 0030964709 scopus 로고    scopus 로고
    • Cloning and characterization of the mouse vitamin D receptor promoter
    • JEHAN, F., AND H. F. DELUCA. Cloning and characterization of the mouse vitamin D receptor promoter. Proc. Natl. Acad. Sci. USA 94: 10138-10143, 1997.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 10138-10143
    • Jehan, F.1    Deluca, H.F.2
  • 153
    • 0028180374 scopus 로고
    • 9k gene. Complete structure and implications on steroid hormone regulation
    • 9k gene. Complete structure and implications on steroid hormone regulation. J. Mol. Biol. 235: 1231-1238, 1994.
    • (1994) J. Mol. Biol. , vol.235 , pp. 1231-1238
    • Jeung, E.B.1    Leung, P.C.2    Krisinger, J.3
  • 154
    • 0029737695 scopus 로고    scopus 로고
    • Transcriptional activation and dimerization functions in the human vitamin D receptor
    • JIN, C. H., S. A. KERNER, M. H. HONG, AND J. W. PIKE. Transcriptional activation and dimerization functions in the human vitamin D receptor. Mol. Endocrinol. 10: 945-957, 1996.
    • (1996) Mol. Endocrinol. , vol.10 , pp. 945-957
    • Jin, C.H.1    Kerner, S.A.2    Hong, M.H.3    Pike, J.W.4
  • 155
    • 0001674512 scopus 로고    scopus 로고
    • Human vitamin D receptor dependent transactivation in Saccharomyces cerevisiae requires retinoid X receptor
    • JIN, C. H., AND J. W. PIKE. Human vitamin D receptor dependent transactivation in Saccharomyces cerevisiae requires retinoid X receptor. Mol. Endocrinol. 10: 196-205, 1996.
    • (1996) Mol. Endocrinol. , vol.10 , pp. 196-205
    • Jin, C.H.1    Pike, J.W.2
  • 157
    • 0027137421 scopus 로고
    • A dialogue on analogues: Newer vitamin-D drugs for use in bone disease, psoriasis, and cancer
    • JONES, G., AND M. J. CALVERLEY. A dialogue on analogues: newer vitamin-D drugs for use in bone disease, psoriasis, and cancer. Trends Endocrinol. Metab. 4: 297-303, 1993.
    • (1993) Trends Endocrinol. Metab. , vol.4 , pp. 297-303
    • Jones, G.1    Calverley, M.J.2
  • 158
    • 0023739838 scopus 로고
    • Isolation and identification of seven metabolites of 25-hydroxydihydrotachysterol 3 formed in the isolated perfused rat kidney: A model for the study of side-chain metabolism of vitamin D
    • JONES, G., N. EDWARDS, D. VRIEZEN, C. PORTEOUS, D. J. H. TRAFFORD, J. CUNNINGHAM, AND H. L. J. MAKIN. Isolation and identification of seven metabolites of 25-hydroxydihydrotachysterol 3 formed in the isolated perfused rat kidney: a model for the study of side-chain metabolism of vitamin D. Biochemistry 27: 7070-7079, 1988.
    • (1988) Biochemistry , vol.27 , pp. 7070-7079
    • Jones, G.1    Edwards, N.2    Vriezen, D.3    Porteous, C.4    Trafford, D.J.H.5    Cunningham, J.6    Makin, H.L.J.7
  • 163
    • 0030071227 scopus 로고    scopus 로고
    • 3 receptor binding site in the rat atrial natriuretic factor promoter
    • 3 receptor binding site in the rat atrial natriuretic factor promoter. Biochem. Biophys. Res. Commun. 218: 882-886, 1996.
    • (1996) Biochem. Biophys. Res. Commun. , vol.218 , pp. 882-886
    • Kahlen, J.P.1    Carlberg, C.2
  • 164
    • 0028917957 scopus 로고
    • Cloning and sequencing of the gene encoding the mouse vitamin D receptor
    • KAMEI, Y., T. KAWADA, T. FUKUWATARI, T. ONO, S. KATO, AND E. SUGIMOTO. Cloning and sequencing of the gene encoding the mouse vitamin D receptor. Gene 152: 281-282, 1995.
    • (1995) Gene , vol.152 , pp. 281-282
    • Kamei, Y.1    Kawada, T.2    Fukuwatari, T.3    Ono, T.4    Kato, S.5    Sugimoto, E.6
  • 169
    • 0031149846 scopus 로고    scopus 로고
    • 3 dependency of vitamin D receptor-retinoid X receptor-vitamin D-responsive element complex
    • 3 dependency of vitamin D receptor-retinoid X receptor-vitamin D-responsive element complex. Arch. Biochem. Biophys. 341: 75-80, 1997.
    • (1997) Arch. Biochem. Biophys. , vol.341 , pp. 75-80
    • Kimmel-Jehan, C.1    Jehan, F.2    Deluca, H.F.3
  • 171
    • 0028960317 scopus 로고
    • Pharmacokinetic studies of vitamin D analogues: Relationship to vitamin D binding protein (DBP)
    • KISSMEYER, A.-M., I. S. MATHIASEN, S. LATINI, AND L. BINDERUP. Pharmacokinetic studies of vitamin D analogues: relationship to vitamin D binding protein (DBP). Endocrine 3: 263-266, 1995.
    • (1995) Endocrine , vol.3 , pp. 263-266
    • Kissmeyer, A.-M.1    Mathiasen, I.S.2    Latini, S.3    Binderup, L.4
  • 174
    • 0015944642 scopus 로고
    • 3-24-hydroxylase. Subcellular location and properties
    • 3-24-hydroxylase. Subcellular location and properties. Biochemistry 13: 1543-1548, 1974.
    • (1974) Biochemistry , vol.13 , pp. 1543-1548
    • Knutson, J.C.1    Deluca, H.F.2
  • 177
    • 0028987267 scopus 로고
    • 3 enhances the expression of transforming growth factor β1 and its latent form binding protein in cultured breast carcinoma cells
    • 3 enhances the expression of transforming growth factor β1 and its latent form binding protein in cultured breast carcinoma cells. Cancer Res. 55: 1540-1546, 1995.
    • (1995) Cancer Res. , vol.55 , pp. 1540-1546
    • Koli, K.1    Keski-Oja, J.2
  • 179
    • 0030480969 scopus 로고    scopus 로고
    • The CBP co-activator is a histone acetyltransferase
    • KOUZARIDES, T., AND A. J. BANNISTER. The CBP co-activator is a histone acetyltransferase. Nature 384: 641-643, 1997.
    • (1997) Nature , vol.384 , pp. 641-643
    • Kouzarides, T.1    Bannister, A.J.2
  • 180
    • 0014669230 scopus 로고
    • Effects of vitamin D on phosphate transport and incorporation into mucosal constituents of rat intestinal mucosa
    • KOWARSKI, S., AND D. SCHACHTER. Effects of vitamin D on phosphate transport and incorporation into mucosal constituents of rat intestinal mucosa. J. Biol. Chem. 244: 211-217, 1969.
    • (1969) J. Biol. Chem. , vol.244 , pp. 211-217
    • Kowarski, S.1    Schachter, D.2
  • 183
    • 0026586944 scopus 로고
    • 3 receptor gene expression and enhances hormone action
    • 3 receptor gene expression and enhances hormone action. Mol. Endocrinol. 6: 198-206, 1992.
    • (1992) Mol. Endocrinol. , vol.6 , pp. 198-206
    • Krishnan, A.V.1    Feldman, D.2
  • 186
    • 0000601908 scopus 로고    scopus 로고
    • Vitamin D and the kidney
    • edited by D. Feldman, F. H. Glorieux, and J. W. Pike. San Diego, CA: Academic, chapt. 17
    • KUMAR, R. Vitamin D and the kidney. In: Vitamin D, edited by D. Feldman, F. H. Glorieux, and J. W. Pike. San Diego, CA: Academic, 1997, chapt. 17, p. 275-292.
    • (1997) Vitamin D , pp. 275-292
    • Kumar, R.1
  • 188
    • 0005232267 scopus 로고    scopus 로고
    • Pivoting 20-normal and 20-epi calcitriols: Synthesis and crystal structure of a "doucle side chain" analogue
    • edited by A. W. Norman, R. Bouillon, and M. Thomasset. Riverside: Univ. of California
    • KUREK-TYRLIK, A., F. Z. MAKAEV, J. WICHA, V. ZHABINSKII, AND M. J. CALVERLEY. Pivoting 20-normal and 20-epi calcitriols: synthesis and crystal structure of a "doucle side chain" analogue. In: Vitamin D. Chemistry, Biology and Clinical Applications of the Steroid Hormone, edited by A. W. Norman, R. Bouillon, and M. Thomasset. Riverside: Univ. of California, 1997, p. 31-32.
    • (1997) Vitamin D. Chemistry, Biology and Clinical Applications of the Steroid Hormone , pp. 31-32
    • Kurek-Tyrlik, A.1    Makaev, F.Z.2    Wicha, J.3    Zhabinskii, V.4    Calverley, M.J.5
  • 190
    • 0024381423 scopus 로고
    • Vitamin D is necessary for reproductive functions in the male rat
    • KWIECINSKI, G. G., G. I. PETRIE, AND H. F. DELUCA. Vitamin D is necessary for reproductive functions in the male rat. J. Nutr. 119: 741-744, 1989.
    • (1989) J. Nutr. , vol.119 , pp. 741-744
    • Kwiecinski, G.G.1    Petrie, G.I.2    Deluca, H.F.3
  • 191
    • 0024562859 scopus 로고
    • 3 restores fertility of vitamin D-deficient female rats
    • Endocrinol. Metab. 19
    • 3 restores fertility of vitamin D-deficient female rats. Am J. Physiol. 256 (Endocrinol. Metab. 19): E483-E487, 1989.
    • (1989) Am J. Physiol. , vol.256
    • Kwiecinski, G.G.1    Petrie, G.I.2    Deluca, H.F.3
  • 192
    • 0025369001 scopus 로고
    • Mapping autosomal recessive vitamin D dependency type I to chromosome 12q14 by linkage analysis
    • LABUDA, M., K. MORGAN, AND F. H. GLORIEUX. Mapping autosomal recessive vitamin D dependency type I to chromosome 12q14 by linkage analysis. Am. J. Human Genet. 47: 28-36, 1990.
    • (1990) Am. J. Human Genet. , vol.47 , pp. 28-36
    • Labuda, M.1    Morgan, K.2    Glorieux, F.H.3
  • 194
    • 0027222793 scopus 로고
    • Structure of the retinoid X receptor α DNA-binding domain: A helix required for homodimeric DNA binding
    • LEE, M. S., S. A. KLIEWER, J. PROVENCAL, P. E. WRIGHT, AND R. M. EVANS. Structure of the retinoid X receptor α DNA-binding domain: a helix required for homodimeric DNA binding. Science 260: 1117-1121, 1993.
    • (1993) Science , vol.260 , pp. 1117-1121
    • Lee, M.S.1    Kliewer, S.A.2    Provencal, J.3    Wright, P.E.4    Evans, R.M.5
  • 195
    • 0002833974 scopus 로고    scopus 로고
    • 3 in immunosuppression: Lessons from autoimmunity and transplantation
    • edited by D, Feldman, F. H. Glorieux, and J. W. Pike. San Diego, CA: Academic, chapt. 69
    • 3 in immunosuppression: lessons from autoimmunity and transplantation. In: Vitamin D, edited by D, Feldman, F. H. Glorieux, and J. W. Pike. San Diego, CA: Academic, 1997, chapt. 69, p. 1167-1181.
    • (1997) Vitamin D , pp. 1167-1181
    • Lemire, J.1
  • 197
    • 0030027490 scopus 로고    scopus 로고
    • 3 receptor- and retinoid X receptor-mediated gene activation in vivo
    • 3 receptor- and retinoid X receptor-mediated gene activation in vivo. Mol. Cell. Biol. 16: 1006-1016, 1996.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 1006-1016
    • Lemon, B.D.1    Freedman, L.P.2
  • 202
    • 0023665225 scopus 로고
    • 3 in osteosarcoma cell line UMR-106. Characterization of products
    • 3 in osteosarcoma cell line UMR-106. Characterization of products. J. Biol. Chem. 262: 14394-14401, 1987.
    • (1987) J. Biol. Chem. , vol.262 , pp. 14394-14401
    • Lohnes, D.1    Jones, G.2
  • 203
    • 0027016138 scopus 로고
    • 3 in target cells. Proceedings of the First International Congress on Vitamins and Biofactors in Life Science
    • 3 in target cells. Proceedings of the First International Congress on Vitamins and Biofactors in Life Science. J. Nutr. Sci. Vitaminol. Special Issue: 75-78, 1992.
    • (1992) J. Nutr. Sci. Vitaminol. , Issue.SPECIAL ISSUE , pp. 75-78
    • Lohnes, D.1    Jones, G.2
  • 204
    • 0028867731 scopus 로고
    • The ligand binding domain of the human retinoic acid receptor γ is predominantly α-helical with a Trp residue in the ligand binding site
    • LUPISELLA, J. A., J. E. DRISCOLL, W. J. METZLER, AND P. R. RECZEK. The ligand binding domain of the human retinoic acid receptor γ is predominantly α-helical with a Trp residue in the ligand binding site. J. Biol. Chem. 270: 24884-24890, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 24884-24890
    • Lupisella, J.A.1    Driscoll, J.E.2    Metzler, W.J.3    Reczek, P.R.4
  • 207
    • 0018643961 scopus 로고
    • Characteristics of the rat liver microsomal enzyme system converting cholecalciferol to 25-hydroxycholecalciferol. Evidence for participation of cytochrome P-450
    • MADHOK, T. C., AND H. F. DELUCA. Characteristics of the rat liver microsomal enzyme system converting cholecalciferol to 25-hydroxycholecalciferol. Evidence for participation of cytochrome P-450. Biochem. J. 184: 491-499, 1979.
    • (1979) Biochem. J. , vol.184 , pp. 491-499
    • Madhok, T.C.1    Deluca, H.F.2
  • 208
    • 0024447295 scopus 로고
    • 3 to calcitroic acid. Evidence for a pathway in kidney and bone involving 24-oxidation
    • 3 to calcitroic acid. Evidence for a pathway in kidney and bone involving 24-oxidation. Biochem. J. 262: 173-180, 1989.
    • (1989) Biochem. J. , vol.262 , pp. 173-180
    • Makin, G.1    Lohnes, D.2    Byford, V.3    Ray, R.4    Jones, G.5
  • 209
    • 0002418732 scopus 로고    scopus 로고
    • Hereditary 1,25-dihydroxyvitamin D resistant rickets
    • edited by D. Feldman, F. H. Glorieux, and J. W. Pike. San Diego, CA: Academic
    • MALLOY, P. J., J. W. PIKE, AND D. FELDMAN. Hereditary 1,25-dihydroxyvitamin D resistant rickets. In: Vitamin D, edited by D. Feldman, F. H. Glorieux, and J. W. Pike. San Diego, CA: Academic, 1997, p. 765-787.
    • (1997) Vitamin D , pp. 765-787
    • Malloy, P.J.1    Pike, J.W.2    Feldman, D.3
  • 210
    • 0029562554 scopus 로고
    • The RXR heterodimers and orphan receptors
    • MANGELSDORF, D. J., AND R. M. EVANS. The RXR heterodimers and orphan receptors. Cell 83: 841-850, 1995.
    • (1995) Cell , vol.83 , pp. 841-850
    • Mangelsdorf, D.J.1    Evans, R.M.2
  • 211
    • 0025270737 scopus 로고
    • Nuclear receptor that identifies a novel retinoic acid response pathway
    • MANGELSDORF, D. J., E. S. ONG, J. A. DYCK, AND R. M. EVANS. Nuclear receptor that identifies a novel retinoic acid response pathway. Nature 345: 224-229, 1990.
    • (1990) Nature , vol.345 , pp. 224-229
    • Mangelsdorf, D.J.1    Ong, E.S.2    Dyck, J.A.3    Evans, R.M.4
  • 215
    • 0028033322 scopus 로고
    • In vitro metabolism of the anti-psoriatic vitamin D analog, calcipotriol, in two cultured human keratinocyte models
    • MASUDA, S., S. STRUGNELL, M. J. CALVERLY, H. L. J. MAKIN, R. KREMER, AND G. JONES. In vitro metabolism of the anti-psoriatic vitamin D analog, calcipotriol, in two cultured human keratinocyte models. J. Biol. Chem. 269: 4794-4803, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 4794-4803
    • Masuda, S.1    Strugnell, S.2    Calverly, M.J.3    Makin, H.L.J.4    Kremer, R.5    Jones, G.6
  • 216
    • 0030771215 scopus 로고    scopus 로고
    • Evidence for ligand-dependent intramolecular folding of the AF-2 domain in vitamin D receptor-activated transcription and coactivator interaction
    • MASUYAMA, H., C. M. BROWNFIELD, R. ST.-ARNAUD, AND P. N. MACDONALD. Evidence for ligand-dependent intramolecular folding of the AF-2 domain in vitamin D receptor-activated transcription and coactivator interaction. Mol. Endocrinol. 11: 1507-1517, 1997.
    • (1997) Mol. Endocrinol. , vol.11 , pp. 1507-1517
    • Masuyama, H.1    Brownfield, C.M.2    St-Arnaud, R.3    Macdonald, P.N.4
  • 217
    • 0031024327 scopus 로고    scopus 로고
    • The N-terminal domain of transcription factor TFIIB is required for direct interaction with the vitamin D receptor and participates in vitamin D-mediated transcription
    • MASUYAMA, H., S. C. JEFCOAT, JR., AND P. N. MACDONALD. The N-terminal domain of transcription factor TFIIB is required for direct interaction with the vitamin D receptor and participates in vitamin D-mediated transcription. Mol. Endocrinol. 11: 218-228, 1997.
    • (1997) Mol. Endocrinol. , vol.11 , pp. 218-228
    • Masuyama, H.1    Jefcoat Jr., S.C.2    Macdonald, P.N.3
  • 219
    • 0023134513 scopus 로고
    • Molecular cloning of complementary DNA encoding the avian receptor for vitamin D
    • MCDONNELL, D. P., D. J. MANGELSDORF, J. W. PIKE, M. R. HAUSSLER, AND B. W. O'MALLEY. Molecular cloning of complementary DNA encoding the avian receptor for vitamin D. Science 235: 1214-1217, 1987.
    • (1987) Science , vol.235 , pp. 1214-1217
    • Mcdonnell, D.P.1    Mangelsdorf, D.J.2    Pike, J.W.3    Haussler, M.R.4    O'Malley, B.W.5
  • 221
    • 0023037395 scopus 로고
    • Osteoblast-like cells in the presence of parathyroid hormone release soluble factor that stimulates osteoclastic bone resorption
    • MCSHEEY, P. M., AND T. J. CHAMBERS. Osteoblast-like cells in the presence of parathyroid hormone release soluble factor that stimulates osteoclastic bone resorption. Endocrinology 119: 1654-1659, 1986.
    • (1986) Endocrinology , vol.119 , pp. 1654-1659
    • Mcsheey, P.M.1    Chambers, T.J.2
  • 222
    • 0023394349 scopus 로고
    • 3 stimulates rat osteoblastic cells to release a soluble factor that increases osteoclastic bone resorption
    • 3 stimulates rat osteoblastic cells to release a soluble factor that increases osteoclastic bone resorption. J. Clin. Invest. 80: 425-429, 1987.
    • (1987) J. Clin. Invest. , vol.80 , pp. 425-429
    • Mcsheeny, P.M.J.1    Chambers, T.J.2
  • 223
    • 0022617765 scopus 로고
    • 3 receptors on osteoclasts of calcium-deficient chicken despite demonstrable receptors on circulating monocytes
    • 3 receptors on osteoclasts of calcium-deficient chicken despite demonstrable receptors on circulating monocytes. J. Clin. Invest. 77: 312-314, 1986.
    • (1986) J. Clin. Invest. , vol.77 , pp. 312-314
    • Merke, J.1    Klaus, G.2    Hugel, U.3    Waldherr, R.4    Ritz, E.5
  • 224
    • 0025277249 scopus 로고
    • 3 metabolism in a human osteosarcoma cell line and human bone cells
    • 3 metabolism in a human osteosarcoma cell line and human bone cells. J. Bone Miner. Res. 5: 597-607, 1990.
    • (1990) J. Bone Miner. Res. , vol.5 , pp. 597-607
    • Miller, B.E.1    Chin, D.P.2    Jones, G.3
  • 230
    • 0025940221 scopus 로고
    • 3 analogs potently induce the human osteocalcin gene promoter stably transfectd into rat osteosarcoma cells (ROSCO-2)
    • 3 analogs potently induce the human osteocalcin gene promoter stably transfectd into rat osteosarcoma cells (ROSCO-2). J. Bone Miner. Res. 6: 893-899, 1991.
    • (1991) J. Bone Miner. Res. , vol.6 , pp. 893-899
    • Morrison, N.A.1    Eisman, J.A.2
  • 232
  • 234
    • 0030953186 scopus 로고    scopus 로고
    • Nuclear receptor repression mediated by a complex containing SMRT, mSin3A, and histone deacetylase
    • NAGY, L., H.-Y. KAO, D. CHAKRAVARTI, R. J. LIN, C. A. HASSIG, D. E. AYER, S. L. SCHREIBER, AND R. M. EVANS. Nuclear receptor repression mediated by a complex containing SMRT, mSin3A, and histone deacetylase. Cell 89: 373-380, 1997.
    • (1997) Cell , vol.89 , pp. 373-380
    • Nagy, L.1    Kao, H.-Y.2    Chakravarti, D.3    Lin, R.J.4    Hassig, C.A.5    Ayer, D.E.6    Schreiber, S.L.7    Evans, R.M.8
  • 237
    • 0028010865 scopus 로고
    • The C-terminal region of the vitamin D receptor is essential to form a complex with a receptor auxiliary factor required for high affinity binding to the vitamin D-responsive element
    • NAKAJIMA, S., J. C. HSIEH, P. N. MACDONALD, M. A. GALLIGAN, C. A. HAUSSLER, G. K. WHITFIELD, AND M. R. HAUSSLER. The C-terminal region of the vitamin D receptor is essential to form a complex with a receptor auxiliary factor required for high affinity binding to the vitamin D-responsive element. Mol. Endocrinol. 8: 159-172, 1994.
    • (1994) Mol. Endocrinol. , vol.8 , pp. 159-172
    • Nakajima, S.1    Hsieh, J.C.2    Macdonald, P.N.3    Galligan, M.A.4    Haussler, C.A.5    Whitfield, G.K.6    Haussler, M.R.7
  • 239
    • 0343308627 scopus 로고    scopus 로고
    • Parathyroid hormone synthesis, secretion and action
    • edited by F. L. Coe, M. J. Favus, C. Pak, J. Parks, and G. Preminger. New York: Raven
    • NAVEH-MANY, T., AND J. SILVER. Parathyroid hormone synthesis, secretion and action. In: Kidney Stones: Medical and Surgiral Management, edited by F. L. Coe, M. J. Favus, C. Pak, J. Parks, and G. Preminger. New York: Raven, 1996, p. 175-199.
    • (1996) Kidney Stones: Medical and Surgiral Management , pp. 175-199
    • Naveh-Many, T.1    Silver, J.2
  • 240
    • 0011264352 scopus 로고
    • The biochemistry and physiology of vitamin D
    • NICOLAYSEN, R., AND N. EEG-LARSEN. The biochemistry and physiology of vitamin D. Vitamin Horm. 11: 29-60, 1953.
    • (1953) Vitamin Horm. , vol.11 , pp. 29-60
    • Nicolaysen, R.1    Eeg-Larsen, N.2
  • 242
    • 0027456452 scopus 로고
    • The development of vitamin D analogues for the treatment of osteoporosis
    • NISHII, Y., K. SATO, AND T. KOBAYASHI. The development of vitamin D analogues for the treatment of osteoporosis. Osteoporosis Int. 1, Suppl.: S190-S193, 1993.
    • (1993) Osteoporosis Int. , vol.1 , Issue.SUPPL.
    • Nishii, Y.1    Sato, K.2    Kobayashi, T.3
  • 243
    • 0028929644 scopus 로고
    • Vitamin D receptor contains multiple dimerization interfaces that are functionally different
    • NISHIKAWA, J.-I., M. KITAUA, I. MASAYOSHI, AND T. NISHIHARA. Vitamin D receptor contains multiple dimerization interfaces that are functionally different. Nucleic Acids Res. 23: 606-611, 1995.
    • (1995) Nucleic Acids Res. , vol.23 , pp. 606-611
    • Nishikawa, J.-I.1    Kitaua, M.2    Masayoshi, I.3    Nishihara, T.4
  • 245
    • 0002748049 scopus 로고    scopus 로고
    • 3: A case study of transcaltachia (rapid hormonal stimulation of intestinal calcium transport)
    • edited by D. Feldman, F. H. Glorieux, and J. W. Pike. San Diego, CA: Academic, chapt. 15
    • 3: a case study of transcaltachia (rapid hormonal stimulation of intestinal calcium transport). In: Vitamin D, edited by D. Feldman, F. H. Glorieux, and J. W. Pike. San Diego, CA: Academic, 1997, chapt. 15, p. 233-258.
    • (1997) Vitamin D , pp. 233-258
    • Norman, A.W.1
  • 246
    • 0019195340 scopus 로고
    • 3 are both indispensable for calcium and phosphorus homeostasis
    • 3 are both indispensable for calcium and phosphorus homeostasis. Life Sci. 27: 229-231, 1980.
    • (1980) Life Sci. , vol.27 , pp. 229-231
    • Norman, A.W.1    Henry, H.L.2    Malluche, H.H.3
  • 247
    • 0020415442 scopus 로고
    • 3 present in intestine and kidney
    • 3 present in intestine and kidney. J. Biol. Chem. 257: 8261-8271, 1982.
    • (1982) J. Biol. Chem. , vol.257 , pp. 8261-8271
    • Ohnuma, N.1    Norman, A.W.2
  • 253
    • 0029082103 scopus 로고
    • Recent progress in enzymology and molecular biology of enzymes involved in vitamin D metabolism
    • OKUDA, K. I., E. USUI, AND Y. OHYAMA. Recent progress in enzymology and molecular biology of enzymes involved in vitamin D metabolism. J. Lipid Res. 36: 1641-1652, 1995.
    • (1995) J. Lipid Res. , vol.36 , pp. 1641-1652
    • Okuda, K.I.1    Usui, E.2    Ohyama, Y.3
  • 254
    • 0028846193 scopus 로고
    • Sequence and characterization of a coactivator for the steroid hormone receptor superfamily
    • ONATE, S. A., S. Y. TSAI, M. J. TSAI, AND B. W. O'MALLEY. Sequence and characterization of a coactivator for the steroid hormone receptor superfamily. Science 270: 1354-1357, 1995.
    • (1995) Science , vol.270 , pp. 1354-1357
    • Onate, S.A.1    Tsai, S.Y.2    Tsai, M.J.3    O'Malley, B.W.4
  • 256
    • 0018133391 scopus 로고
    • 24,25-Dihydroxyvitamin D is a metabolite of vitamin D essential for bone formation
    • ORNOY, A., D. GOODWIN, D. NOFF, AND S. EDELSTEIN. 24,25-Dihydroxyvitamin D is a metabolite of vitamin D essential for bone formation. Nature 276: 517-519, 1978.
    • (1978) Nature , vol.276 , pp. 517-519
    • Ornoy, A.1    Goodwin, D.2    Noff, D.3    Edelstein, S.4
  • 257
    • 3643145566 scopus 로고
    • The calcium and phosphorus metabolism in rickets, with special reference to ultraviolet ray therapy
    • ORR, W. J., L. E. HOLT, JR., L. WILKINS, AND F. H. BOONE. The calcium and phosphorus metabolism in rickets, with special reference to ultraviolet ray therapy. Am. J. Dis. Child. 26: 362-372, 1923.
    • (1923) Am. J. Dis. Child. , vol.26 , pp. 362-372
    • Orr, W.J.1    Holt Jr., L.E.2    Wilkins, L.3    Boone, F.H.4
  • 258
    • 0024556838 scopus 로고
    • Calcitriol treatment is not effective in post-menopausal osteoporosis
    • OTT, S., AND C. H. CHESNUT. Calcitriol treatment is not effective in post-menopausal osteoporosis. Ann. Intern. Med. 118: 267-274, 1989.
    • (1989) Ann. Intern. Med. , vol.118 , pp. 267-274
    • Ott, S.1    Chesnut, C.H.2
  • 262
    • 3643120550 scopus 로고    scopus 로고
    • Two distinct dimerization interfaces differentially modulate target gene specificity of nuclear hormone receptors
    • PERLMANN, T., K. UMESONO, P. N. RANGARAJAN, B. N. FORMAN, AND R. M. EVANS. Two distinct dimerization interfaces differentially modulate target gene specificity of nuclear hormone receptors. Mol. Endocrinol. 9: 1166-1179, 1996.
    • (1996) Mol. Endocrinol. , vol.9 , pp. 1166-1179
    • Perlmann, T.1    Umesono, K.2    Rangarajan, P.N.3    Forman, B.N.4    Evans, R.M.5
  • 263
    • 0028973378 scopus 로고
    • Thyroid hormone receptor β mutants associated with generalized resistance to thyroid hormone show defects in their ligand-sensitive repression function
    • PIEDRAFITA, F. J., M. A. ORTIZ, AND M. PFAHL. Thyroid hormone receptor β mutants associated with generalized resistance to thyroid hormone show defects in their ligand-sensitive repression function. Mol. Endocrinol. 9: 1533-1548, 1995.
    • (1995) Mol. Endocrinol. , vol.9 , pp. 1533-1548
    • Piedrafita, F.J.1    Ortiz, M.A.2    Pfahl, M.3
  • 264
    • 0025980571 scopus 로고
    • Role of intracellular free calcium in the cornified envelope formation of keratinocytes: Differences in the mode of action of extracellular calcium and 1,25 dihydroxyvitamin D
    • PILLAI, S., AND D. D. BIKLE. Role of intracellular free calcium in the cornified envelope formation of keratinocytes: differences in the mode of action of extracellular calcium and 1,25 dihydroxyvitamin D. J. Cell. Physiol. 146: 94-100, 1991.
    • (1991) J. Cell. Physiol. , vol.146 , pp. 94-100
    • Pillai, S.1    Bikle, D.D.2
  • 267
    • 3643140436 scopus 로고
    • Biological surprises and evolutionary links in the calcium field. Parathyroid hormone (PTH): Past, present and future
    • edited by T. Suda. Tokyo: Chugai
    • POTTS, J. T., JR. Biological surprises and evolutionary links in the calcium field. Parathyroid hormone (PTH): past, present and future. In: PTH and PTHrP, edited by T. Suda. Tokyo: Chugai, 1993, p. 6-11.
    • (1993) PTH and PTHrP , pp. 6-11
    • Potts Jr., J.T.1
  • 269
    • 0027459195 scopus 로고
    • In vivo metabolism of the vitamin D analog, dihydrotachysterol. Evidence for formation of 1,25- and 1,25-dihydroxy-dihydrotachysterol metabolites and studies of their biological activity
    • QAW, F., M. J. CALVERLEY, N. J. SCHROEDER, D. J. H. TRAFFORD, H. L. J. MAKIN, AND G. JONES. In vivo metabolism of the vitamin D analog, dihydrotachysterol. Evidence for formation of 1,25- and 1,25-dihydroxy-dihydrotachysterol metabolites and studies of their biological activity. J. Biol. Chem. 268: 282-292, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 282-292
    • Qaw, F.1    Calverley, M.J.2    Schroeder, N.J.3    Trafford, D.J.H.4    Makin, H.L.J.5    Jones, G.6
  • 270
    • 0015514459 scopus 로고
    • 1,25-Dihydroxycholecalciferol: A potent stimulator of bone resorption in tissue culture
    • RAISZ, L. G., C. L. TRUMMEL, M. F. HOLICK, AND H. F. DELUCA. 1,25-Dihydroxycholecalciferol: a potent stimulator of bone resorption in tissue culture. Science 175: 768-769, 1972.
    • (1972) Science , vol.175 , pp. 768-769
    • Raisz, L.G.1    Trummel, C.L.2    Holick, M.F.3    Deluca, H.F.4
  • 273
    • 0029044997 scopus 로고
    • Structural determinants of nuclear receptor assembly on DNA direct repeats
    • RASTINEJAD, F., T. PERLMANN, R. M. EVANS, AND P. B. SIGLER. Structural determinants of nuclear receptor assembly on DNA direct repeats. Nature 375: 203-211, 1995.
    • (1995) Nature , vol.375 , pp. 203-211
    • Rastinejad, F.1    Perlmann, T.2    Evans, R.M.3    Sigler, P.B.4
  • 277
  • 279
    • 0024467451 scopus 로고
    • 3 metabolism limits receptor occupancy and target cell responsiveness
    • 3 metabolism limits receptor occupancy and target cell responsiveness. J. Biol. Chem. 264: 15917-15921, 1989.
    • (1989) J. Biol. Chem. , vol.264 , pp. 15917-15921
    • Reinhardt, T.A.1    Horst, R.L.2
  • 280
    • 0029643780 scopus 로고
    • Crystal structure of the RAR-γ ligand-binding domain bound to all-trans retinoic acid
    • RENAUD, J. P., N. ROCHEL, M. RUFF, V. VIVAT, P. CHAMBON, H. GRONEMEYER, AND D. MORAS. Crystal structure of the RAR-γ ligand-binding domain bound to all-trans retinoic acid. Nature 378: 681-689, 1995.
    • (1995) Nature , vol.378 , pp. 681-689
    • Renaud, J.P.1    Rochel, N.2    Ruff, M.3    Vivat, V.4    Chambon, P.5    Gronemeyer, H.6    Moras, D.7
  • 281
    • 0028983573 scopus 로고
    • TNF-α expression by resident microglia and infiltrating leukocytes in the central nervous system of mice with experimental allergic encephalomyelitis: Regulation by Th1 cytokines
    • RENNO, T., M. KRAKOWSKI, C. PICCIRILLO, J. LIN, AND T. OWENS. TNF-α expression by resident microglia and infiltrating leukocytes in the central nervous system of mice with experimental allergic encephalomyelitis: regulation by Th1 cytokines. J. Immunol. 154: 944-953, 1995.
    • (1995) J. Immunol. , vol.154 , pp. 944-953
    • Renno, T.1    Krakowski, M.2    Piccirillo, C.3    Lin, J.4    Owens, T.5
  • 287
    • 0028364080 scopus 로고
    • Alteration of a single amino acid residue in retinoic acid receptor causes a dominant negative phenotype
    • SAITOU, M., S. NARUMIYA, AND A. KAKIZUKA. Alteration of a single amino acid residue in retinoic acid receptor causes a dominant negative phenotype. J. Biol. Chem. 269: 19101-19107, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 19101-19107
    • Saitou, M.1    Narumiya, S.2    Kakizuka, A.3
  • 290
    • 0027261111 scopus 로고
    • Cloning and functional expression of a human parathyroid hormone receptor
    • SCHNEIDER, H., J. H. FEYEN, K. SEUWEN, AND N. R. MOVVA. Cloning and functional expression of a human parathyroid hormone receptor. Eur. J. Pharmacol. 246: 149-155, 1993.
    • (1993) Eur. J. Pharmacol. , vol.246 , pp. 149-155
    • Schneider, H.1    Feyen, J.H.2    Seuwen, K.3    Movva, N.R.4
  • 292
    • 0028022977 scopus 로고
    • Specificity and flexibility of vitamin D signalling
    • SCHRADER, M., K. M. MULLER, AND C. CARLBERG. Specificity and flexibility of vitamin D signalling. J. Biol. Chem. 269: 5501-5504, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 5501-5504
    • Schrader, M.1    Muller, K.M.2    Carlberg, C.3
  • 294
    • 0029083618 scopus 로고
    • Present and future of osteoporosis therapy
    • SEEMAN, E., C. TSALAMANDRIS, S. BASS, AND G. PEARCE. Present and future of osteoporosis therapy. Bone 17, Suppl.: 23S-29S, 1995.
    • (1995) Bone , vol.17 , Issue.SUPPL.
    • Seeman, E.1    Tsalamandris, C.2    Bass, S.3    Pearce, G.4
  • 301
    • 0022992997 scopus 로고
    • Parathyroid hormone stimulates dephosphorylation of the renodoxin component of the 25-hydroxyvitamin D3-1α-hydroxylase from rat renal cortex
    • SIEGAL, N., N. WOMGSURAWAT, AND H. J. ARMBRECHT. Parathyroid hormone stimulates dephosphorylation of the renodoxin component of the 25-hydroxyvitamin D3-1α-hydroxylase from rat renal cortex. J. Biol. Chem. 261: 16998-17003, 1986.
    • (1986) J. Biol. Chem. , vol.261 , pp. 16998-17003
    • Siegal, N.1    Womgsurawat, N.2    Armbrecht, H.J.3
  • 302
    • 0002637440 scopus 로고    scopus 로고
    • Parathyroid hormone - Molecular biology and regulation
    • edited by J. B. Bilezikian, L. G. Raisz, and G. A. Rodan. San Diego, CA: Academic, chapt. 24
    • SILVER, J., AND H. M. KRONENBERG. Parathyroid hormone - molecular biology and regulation. In: Principles of Bone Biology, edited by J. B. Bilezikian, L. G. Raisz, and G. A. Rodan. San Diego, CA: Academic, 1996, chapt. 24, p. 325-337.
    • (1996) Principles of Bone Biology , pp. 325-337
    • Silver, J.1    Kronenberg, H.M.2
  • 303
    • 0029774748 scopus 로고    scopus 로고
    • New insights into the regulation of parathyroid hormone synthesis and secretion in chronic renal failure
    • SILVER, J., E. MOALLEM, R. KILAV, E. EPSTEIN, A. SELA, AND T. NAVEH-MANY. New insights into the regulation of parathyroid hormone synthesis and secretion in chronic renal failure. Nephrol. Dial. Transplant. 11, Suppl. 3: 2-5, 1996.
    • (1996) Nephrol. Dial. Transplant. , vol.11 , Issue.3 SUPPL. , pp. 2-5
    • Silver, J.1    Moallem, E.2    Kilav, R.3    Epstein, E.4    Sela, A.5    Naveh-Many, T.6
  • 304
    • 0000751571 scopus 로고    scopus 로고
    • Vitamin D and the parathyroid glands
    • edited by D. Feldman, F. H. Glorieux, and J. W. Pike. San Diego, CA: Academic, chapt. 23
    • SILVER, J., AND T. NAVEH-MANY. Vitamin D and the parathyroid glands. In: Vitamin D, edited by D. Feldman, F. H. Glorieux, and J. W. Pike. San Diego, CA: Academic, 1997, chapt. 23, p. 353-367.
    • (1997) Vitamin D , pp. 353-367
    • Silver, J.1    Naveh-Many, T.2
  • 305
    • 0022971152 scopus 로고
    • Regulation by vitamin D metabolites of parathyroid hormone gene transcription in vivo in the rat
    • SILVER, J., T. NAVEH-MANY, H. MAYER, H. J. SCHMEIZER, AND M. M. POPVTZER. Regulation by vitamin D metabolites of parathyroid hormone gene transcription in vivo in the rat. J. Clin. Invest. 78: 1296-1301, 1986.
    • (1986) J. Clin. Invest. , vol.78 , pp. 1296-1301
    • Silver, J.1    Naveh-Many, T.2    Mayer, H.3    Schmeizer, H.J.4    Popvtzer, M.M.5
  • 309
    • 0021748474 scopus 로고
    • Marked suppression of secondary hyperparathyroidism by I.V. administration of 1,25-dihydroxycholecalciferol in uremic patients
    • SLATOPOLSKY, E., C. WEERTS, J. THIELAND, R. HORST, H. HARTER, AND K. MARTIN. Marked suppression of secondary hyperparathyroidism by I.V. administration of 1,25-dihydroxycholecalciferol in uremic patients. J. Clin. Invest. 74: 2136-2141, 1984.
    • (1984) J. Clin. Invest. , vol.74 , pp. 2136-2141
    • Slatopolsky, E.1    Weerts, C.2    Thieland, J.3    Horst, R.4    Harter, H.5    Martin, K.6
  • 310
    • 0022621042 scopus 로고
    • 3 on the morphologic and biochemical differentiation of cultured human epidermal keratinocytes grown in serum-free conditions
    • 3 on the morphologic and biochemical differentiation of cultured human epidermal keratinocytes grown in serum-free conditions. J. Invest. Dermatol. 86: 709-714, 1986.
    • (1986) J. Invest. Dermatol. , vol.86 , pp. 709-714
    • Smith, E.L.1    Walworth, N.C.2    Holick, M.F.3
  • 311
    • 0025724977 scopus 로고
    • A 55-kilodalton accessory factor facilitates vitamin D receptor binding
    • SONE, T., K. OZONO, AND J. W. PIKE. A 55-kilodalton accessory factor facilitates vitamin D receptor binding. Mol. Endocrinol. 5: 1578-1586, 1991.
    • (1991) Mol. Endocrinol. , vol.5 , pp. 1578-1586
    • Sone, T.1    Ozono, K.2    Pike, J.W.3
  • 313
    • 0017853252 scopus 로고
    • The relationship between vitamin D-stimulated calcium transport and intestinal calcium-binding protein in the chicken
    • SPENCER, R., M. CHARMAN, P. W. WILSON, AND D. E. M. LAWSON. The relationship between vitamin D-stimulated calcium transport and intestinal
    • (1978) Biochem. J. , vol.170 , pp. 93-102
    • Spencer, R.1    Charman, M.2    Wilson, P.W.3    Lawson, D.E.M.4
  • 314
    • 0000485717 scopus 로고    scopus 로고
    • Abnormal bone development in mice deficient for the vitamin D 24-hydroxylase gene
    • ST. ARNAUD, R., A. ARABIAN, AND F. H. GLORIEUX. Abnormal bone development in mice deficient for the vitamin D 24-hydroxylase gene (Abstract). J. Bone Miner. Res. 11: S126, 1996.
    • (1996) J. Bone Miner. Res. , vol.11
    • St Arnaud, R.1    Arabian, A.2    Glorieux, F.H.3
  • 316
    • 3643142469 scopus 로고    scopus 로고
    • Abnormal intramembranous ossification in mice deficient for the vitamin D 24-hydroxylase gene
    • edited by A. W. Norman, R. Bouillon, and M. Thomasset. Riverside: Univ. of California
    • ST. ARNAUD, R., A. ARABIAN, R. TRAVERS, AND F. H. GLORIEUX. Abnormal intramembranous ossification in mice deficient for the vitamin D 24-hydroxylase gene. In: Vitamin D. Chemistry, Biology and Clinical Applications of the Steroid Hormone, edited by A. W. Norman, R. Bouillon, and M. Thomasset. Riverside: Univ. of California, 1997, p. 635-639.
    • (1997) Vitamin D. Chemistry, Biology and Clinical Applications of the Steroid Hormone , pp. 635-639
    • St Arnaud, R.1    Arabian, A.2    Travers, R.3    Glorieux, F.H.4
  • 317
    • 0001196827 scopus 로고    scopus 로고
    • The 25-hydroxyvitamin D 1α-hydroxylase gene maps to the pseudovitamin D-deficiency rickets (PDDR) disease locus
    • ST. ARNAUD, R., S. MESSERLIAN, J. M. MOIR, J. L. OMDAHL, AND F. H. GLORIEUX. The 25-hydroxyvitamin D 1α-hydroxylase gene maps to the pseudovitamin D-deficiency rickets (PDDR) disease locus. J. Bone Miner. Res. 12: 1552-1559, 1997.
    • (1997) J. Bone Miner. Res. , vol.12 , pp. 1552-1559
    • St Arnaud, R.1    Messerlian, S.2    Moir, J.M.3    Omdahl, J.L.4    Glorieux, F.H.5
  • 318
    • 0002303623 scopus 로고    scopus 로고
    • Mechanisms regulating osteoblast proliferation and differentiation
    • edited by J. P. Bilezekian, G. Raisz, and G. A. Rodan. San Diego, CA: Academic, chapt. 5
    • STEIN, G. S., J. B. LIAN, J. L. STEIN, A. J. VAN WIJNEN, B. FRENKEL, AND M. MONTECINO. Mechanisms regulating osteoblast proliferation and differentiation. In: Bone Biology, edited by J. P. Bilezekian, G. Raisz, and G. A. Rodan. San Diego, CA: Academic, 1996, chapt. 5, p. 69-86.
    • (1996) Bone Biology , pp. 69-86
    • Stein, G.S.1    Lian, J.B.2    Stein, J.L.3    Van Wijnen, A.J.4    Frenkel, B.5    Montecino, M.6
  • 319
    • 0019381680 scopus 로고
    • A monolog on analogs
    • STERN, P. A monolog on analogs. Calcif. Tissue Int. 33: 1-4, 1981.
    • (1981) Calcif. Tissue Int. , vol.33 , pp. 1-4
    • Stern, P.1
  • 320
    • 0008845527 scopus 로고    scopus 로고
    • 3 interactions with local factors in bone remodeling
    • edited by D. Feldman, F. H. Glorieux, and J. W. Pike. San Diego, CA: Academic, chapt. 22
    • 3 interactions with local factors in bone remodeling. In: Vitamin D, edited by D. Feldman, F. H. Glorieux, and J. W. Pike. San Diego, CA: Academic, 1997, chapt. 22, p. 341-352.
    • (1997) Vitamin D , pp. 341-352
    • Stern, P.H.1
  • 322
    • 0030956080 scopus 로고    scopus 로고
    • The vitamin D receptor-structure and transcriptional activation
    • STRUGNELL, S. A., AND H. F. DELUCA. The vitamin D receptor-structure and transcriptional activation. Proc. Soc. Exp. Biol. Med. 215: 223-228, 1997.
    • (1997) Proc. Soc. Exp. Biol. Med. , vol.215 , pp. 223-228
    • Strugnell, S.A.1    Deluca, H.F.2
  • 323
    • 0011096351 scopus 로고
    • Vitamin D receptor ligand-binding domain expressed as a fusion protein
    • STRUGNELL, S. A., B. A. WIEFLING, AND H. F. DELUCA. Vitamin D receptor ligand-binding domain expressed as a fusion protein (Abstract). J. Bone Miner. Res. 10: S396, 1995.
    • (1995) J. Bone Miner. Res. , vol.10
    • Strugnell, S.A.1    Wiefling, B.A.2    Deluca, H.F.3
  • 324
    • 0001848138 scopus 로고
    • 3 identified by thaw-mount autoradiography
    • edited by D. V. Cohn, R. V. Talmage, and J. L. Matthews. Amsterdam: Excerpta Medica
    • 3 identified by thaw-mount autoradiography. In: Hormonal Control of Calcium Metabolism, edited by D. V. Cohn, R. V. Talmage, and J. L. Matthews. Amsterdam: Excerpta Medica, 1981, p. 222-229.
    • (1981) Hormonal Control of Calcium Metabolism , pp. 222-229
    • Stumpf, W.E.1    Sar, M.2    Deluca, H.F.3
  • 328
    • 0038826379 scopus 로고    scopus 로고
    • Vitamin D and osteoclastogenesis
    • edited by D, Feldman, F. H. Glorieux, and J. W. Pike. San Diego, CA: Academic, chapt. 21
    • SUDA, T., AND N. TAKAHASHI. Vitamin D and osteoclastogenesis. In: Vitamin D, edited by D, Feldman, F. H. Glorieux, and J. W. Pike. San Diego, CA: Academic, 1997, chapt. 21, p. 329-340.
    • (1997) Vitamin D , pp. 329-340
    • Suda, T.1    Takahashi, N.2
  • 329
    • 0001137929 scopus 로고
    • Modulation of osteoclast differentiation: Update 1995
    • SUDA, T., N. TAKAHASHI, AND T. J. MARTIN. Modulation of osteoclast differentiation: update 1995. Endocr. Rev. 4: 266-270, 1995.
    • (1995) Endocr. Rev. , vol.4 , pp. 266-270
    • Suda, T.1    Takahashi, N.2    Martin, T.J.3
  • 333
    • 0014887364 scopus 로고
    • Morphological and physiological consideration in a new concept of calcium transport in bone
    • TALMAGE, R. V. Morphological and physiological consideration in a new concept of calcium transport in bone. Am. J. Anat. 129: 467-476, 1970.
    • (1970) Am. J. Anat. , vol.129 , pp. 467-476
    • Talmage, R.V.1
  • 334
    • 0020265220 scopus 로고
    • 1α,25-Dihydroxycholecalciferol and a human myeloid leukemia cell line (HL-60). The presence of a cytosol receptor and induction of differentiation
    • TANAKA, H., E. ABE, C. MIYAURA, T. KURIBAYASHI, K. KONNO, Y. NISHII, AND T. SUDA. 1α,25-Dihydroxycholecalciferol and a human myeloid leukemia cell line (HL-60). The presence of a cytosol receptor and induction of differentiation. Biochem. J. 204: 713-719, 1982.
    • (1982) Biochem. J. , vol.204 , pp. 713-719
    • Tanaka, H.1    Abe, E.2    Miyaura, C.3    Kuribayashi, T.4    Konno, K.5    Nishii, Y.6    Suda, T.7
  • 336
    • 0015583124 scopus 로고
    • The control of 25-hydroxyvitamin D metabolism by inorganic phosphorus
    • TANAKA, Y., AND H. F. DELUCA. The control of 25-hydroxyvitamin D metabolism by inorganic phosphorus. Arch. Biochem. Biophys. 154: 566-574, 1973.
    • (1973) Arch. Biochem. Biophys. , vol.154 , pp. 566-574
    • Tanaka, Y.1    Deluca, H.F.2
  • 342
    • 0000148691 scopus 로고    scopus 로고
    • 9K
    • edited by D. Feldman, F. H. Glorieux, and J. W. Pike. San Diego, CA: Academic, chapt. 14
    • 9K. In: Vitamin D, edited by D. Feldman, F. H. Glorieux, and J. W. Pike. San Diego, CA: Academic, 1997, chapt. 14, p. 223-232.
    • (1997) Vitamin D , pp. 223-232
    • Thomasset, M.1
  • 343
  • 344
    • 0025358395 scopus 로고
    • 3-24-hydroxylase activity in Caco-2 cells. An in vitro model of intestinal vitamin D catabolism
    • 3-24-hydroxylase activity in Caco-2 cells. An in vitro model of intestinal vitamin D catabolism. Endocrinology 126: 2868-2875, 1990.
    • (1990) Endocrinology , vol.126 , pp. 2868-2875
    • Tomon, M.1    Tenenhouse, H.S.2    Jones, G.3
  • 345
    • 0030912539 scopus 로고    scopus 로고
    • The transcriptional co-activator p/CIP binds CBP and mediates nuclear-receptor function
    • TORCHIA, J., D. W. ROSE, J. INOSTROZA, Y. KAMEL, S. WESTIN, C. K. GLASS, AND M. G. ROSENFELD. The transcriptional co-activator p/CIP binds CBP and mediates nuclear-receptor function. Nature 387: 677-684, 1997.
    • (1997) Nature , vol.387 , pp. 677-684
    • Torchia, J.1    Rose, D.W.2    Inostroza, J.3    Kamel, Y.4    Westin, S.5    Glass, C.K.6    Rosenfeld, M.G.7
  • 347
    • 0019193314 scopus 로고
    • In vitro synthesis of 1α,25-dihydroxycholecalciferol and 24,25-dihydroxycholecalciferol by isolated calvarial cells
    • TURNER, R. T., J. E. PUZAS, M. D. FORTE, G. E. LESTER, T. K. GRAY, G. A. HOWARD, AND D. J. BAYLINK. In vitro synthesis of 1α,25-dihydroxycholecalciferol and 24,25-dihydroxycholecalciferol by isolated calvarial cells. Proc. Natl. Acad. Sci. USA 77: 5720-5724, 1980.
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 5720-5724
    • Turner, R.T.1    Puzas, J.E.2    Forte, M.D.3    Lester, G.E.4    Gray, T.K.5    Howard, G.A.6    Baylink, D.J.7
  • 355
    • 0012316186 scopus 로고    scopus 로고
    • Differential ligand-dependent interactions between the AF-2 activating domain of nuclear receptors and the putative transcriptional intermediary factors mSUG1 and TIF1
    • VOM BAUR, E., C. ZECHEL, D. HEERY, M. J. S. HEINE, J. M. GARNIER, V. VIVAT, B. LE DOUARIN, H. GRONEMEYER, P. CHAMBON, AND R. LOSSON. Differential ligand-dependent interactions between the AF-2 activating domain of nuclear receptors and the putative transcriptional intermediary factors mSUG1 and TIF1. EMBO J. 15: 110-124, 1996.
    • (1996) EMBO J. , vol.15 , pp. 110-124
    • Vom Baur, E.1    Zechel, C.2    Heery, D.3    Heine, M.J.S.4    Garnier, J.M.5    Vivat, V.6    Le Douarin, B.7    Gronemeyer, H.8    Chambon, P.9    Losson, R.10
  • 357
    • 0003485986 scopus 로고
    • Vitamin D-dependent calcium-binding proteins
    • edited by R. H. Wasserman, R. A. Corradino, E. Carafoli, R. H. Kretsinger, D. H. MacLennan, and S. L. Siegel. New York: Elsevier/North-Holland
    • WASSERMAN, R. H., AND J. J. FEHER. Vitamin D-dependent calcium-binding proteins. In: Calcium Binding Proteins and Calcium Function, edited by R. H. Wasserman, R. A. Corradino, E. Carafoli, R. H. Kretsinger, D. H. MacLennan, and S. L. Siegel. New York: Elsevier/North-Holland, 1977, p. 292-302.
    • (1977) Calcium Binding Proteins and Calcium Function , pp. 292-302
    • Wasserman, R.H.1    Feher, J.J.2
  • 359
    • 0029123088 scopus 로고
    • A highly conserved region in the hormone-binding domain of the human vitamin D receptor contains residues vital for heterodimerization with retinoid X receptor and for transcriptional activation
    • WHITFIELD, G. K., J. C. HSIEH, S. NAKAJIMA, P. N. MACDONALD, P. D. THOMPSON, P. W. JURUTKA, C. A. HAUSSLER, AND M. R. HAUSSLER. A highly conserved region in the hormone-binding domain of the human vitamin D receptor contains residues vital for heterodimerization with retinoid X receptor and for transcriptional activation. Mol. Endocrinol. 9: 1166-1179, 1995.
    • (1995) Mol. Endocrinol. , vol.9 , pp. 1166-1179
    • Whitfield, G.K.1    Hsieh, J.C.2    Nakajima, S.3    Macdonald, P.N.4    Thompson, P.D.5    Jurutka, P.W.6    Haussler, C.A.7    Haussler, M.R.8
  • 361
    • 0001037347 scopus 로고    scopus 로고
    • 3-D model of the ligand-binding domain of the vitamin D receptor based on the crystal structure of holo-RAR
    • edited by A. W. Norman, R. Bouillon, and M. Thomasset. Riverside: Univ. of California
    • WURTZ, J.-M., B. GUILLOT, AND D. MORAS. 3-D model of the ligand-binding domain of the vitamin D receptor based on the crystal structure of holo-RAR. In: Vitamin D. Chemistry, Biology and Clinical Applications of the Steroid Hormone, edited by A. W. Norman, R. Bouillon, and M. Thomasset. Riverside: Univ. of California, 1997, p. 165-172.
    • (1997) Vitamin D. Chemistry, Biology and Clinical Applications of the Steroid Hormone , pp. 165-172
    • Wurtz, J.-M.1    Guillot, B.2    Moras, D.3
  • 363
    • 0027333285 scopus 로고
    • 2 suppress immunoglobulin production and thymic lymphocyte proliferation in vivo
    • 2 suppress immunoglobulin production and thymic lymphocyte proliferation in vivo. Biochim. Biophys. Acta 1158: 269-286, 1993.
    • (1993) Biochim. Biophys. Acta , vol.1158 , pp. 269-286
    • Yang, S.1    Smith, C.2    Deluca, H.F.3
  • 364
    • 0027176520 scopus 로고
    • Vitamin D deficiency suppresses cell-mediated immunity in vivo
    • YANG, S., C. SMITH, J. M. PRAHL, AND H. F. DELUCA. Vitamin D deficiency suppresses cell-mediated immunity in vivo. Arch. Biochem. Biophys. 303: 98-106, 1983.
    • (1983) Arch. Biochem. Biophys. , vol.303 , pp. 98-106
    • Yang, S.1    Smith, C.2    Prahl, J.M.3    Deluca, H.F.4
  • 366
    • 0028313996 scopus 로고
    • The dimerization interfaces formed between the DNA binding domains of RXR, RAR and TR determine the binding specificity and polarity of the full-length receptors to direct repeats
    • ZECHEL, C., X. Q. SHEN, J. Y. CHEN, Z. P. CHEN, P. CHAMBON, AND H. GRONEMEYER. The dimerization interfaces formed between the DNA binding domains of RXR, RAR and TR determine the binding specificity and polarity of the full-length receptors to direct repeats. EMBO J. 13: 1425-1433, 1994.
    • (1994) EMBO J. , vol.13 , pp. 1425-1433
    • Zechel, C.1    Shen, X.Q.2    Chen, J.Y.3    Chen, Z.P.4    Chambon, P.5    Gronemeyer, H.6
  • 368
    • 0028945042 scopus 로고
    • Two vitamin D response elements function in the rat 1,25-dihydroxyvitamin D 24-hydroxylase promoter
    • ZIEROLD, C., H. M. DARWISH, AND H. F. DELUCA. Two vitamin D response elements function in the rat 1,25-dihydroxyvitamin D 24-hydroxylase promoter. J. Biol. Chem. 270: 1675-1678, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 1675-1678
    • Zierold, C.1    Darwish, H.M.2    Deluca, H.F.3


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