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Volumn 250, Issue , 2006, Pages 109-174

Calcium Homeostasis in Human Placenta: Role of Calcium-Handling Proteins

Author keywords

Bone mineral content; Calcium channels; Calcium binding proteins; Calcium handling proteins; Human placenta; Syncytiotrophoblast

Indexed keywords

ADENOSINE TRIPHOSPHATASE (CALCIUM); AMINO ACID; CALBINDIN; CALCIUM; CALCIUM BINDING PROTEIN; CALCIUM CHANNEL; CALCIUM CHANNEL L TYPE; CALCIUM SENSING RECEPTOR; CALVASCULIN; ION; LIPID; NEUROTRANSMITTER; ONCOMODULIN; PROTEIN S 100; SODIUM CALCIUM EXCHANGE PROTEIN; TRANSIENT RECEPTOR POTENTIAL CHANNEL; TUMOR PROTEIN; VOLTAGE GATED CALCIUM CHANNEL;

EID: 33745993993     PISSN: 00747696     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0074-7696(06)50004-X     Document Type: Review
Times cited : (25)

References (426)
  • 2
    • 10044230497 scopus 로고    scopus 로고
    • S100B-stimulated NO production by BV-2 microglia is independent of RAGE transducing activity but dependent on RAGE extracellular domain
    • Adami C., Bianchi R., Pula G., and Donato R. S100B-stimulated NO production by BV-2 microglia is independent of RAGE transducing activity but dependent on RAGE extracellular domain. Biochim. Biophys. Acta 1742 (2004) 169-177
    • (2004) Biochim. Biophys. Acta , vol.1742 , pp. 169-177
    • Adami, C.1    Bianchi, R.2    Pula, G.3    Donato, R.4
  • 3
    • 0025319853 scopus 로고
    • Placental steroid hormone biosynthesis in primate pregnancy
    • Albrecht E.D., and Pepe G.J. Placental steroid hormone biosynthesis in primate pregnancy. Endocr. Rev. 11 (1990) 124-150
    • (1990) Endocr. Rev. , vol.11 , pp. 124-150
    • Albrecht, E.D.1    Pepe, G.J.2
  • 4
    • 1242337319 scopus 로고    scopus 로고
    • Correlation of c-erbB-2 and S-100 expression with the malignancy grading and anatomical site in oral squamous cell carcinoma
    • Albuquerque Jr. R.L., Miguel M.C., Costa A.L., and Souza L.B. Correlation of c-erbB-2 and S-100 expression with the malignancy grading and anatomical site in oral squamous cell carcinoma. Int. J. Exp. Pathol. 84 (2003) 259-265
    • (2003) Int. J. Exp. Pathol. , vol.84 , pp. 259-265
    • Albuquerque Jr., R.L.1    Miguel, M.C.2    Costa, A.L.3    Souza, L.B.4
  • 5
    • 0021042332 scopus 로고
    • Scanning electron microscopy of maternal blood cells and their surface relationship with the placenta
    • Al-Zuhair A.G., Ibrahim M.E., Mughal S., and Mohammed M.E. Scanning electron microscopy of maternal blood cells and their surface relationship with the placenta. Acta Obstet. Gynecol. Scand. 62 (1983) 493-498
    • (1983) Acta Obstet. Gynecol. Scand. , vol.62 , pp. 493-498
    • Al-Zuhair, A.G.1    Ibrahim, M.E.2    Mughal, S.3    Mohammed, M.E.4
  • 6
    • 0023639522 scopus 로고
    • Loss and regeneration of the microvilli of human placental syncytiotrophoblast
    • Al-Zuhair A.G., Ibrahim M.E., Mughal S., and Abdulla M.A. Loss and regeneration of the microvilli of human placental syncytiotrophoblast. Arch. Gynecol. 240 (1987) 147-151
    • (1987) Arch. Gynecol. , vol.240 , pp. 147-151
    • Al-Zuhair, A.G.1    Ibrahim, M.E.2    Mughal, S.3    Abdulla, M.A.4
  • 8
    • 1142297617 scopus 로고    scopus 로고
    • Complex regulation of calbindin-D(9k) in the mouse placenta and extra-embryonic membrane during mid- and late pregnancy
    • An B.S., Choi K.C., Lee G.S., Leung P.C., and Jeung E.B. Complex regulation of calbindin-D(9k) in the mouse placenta and extra-embryonic membrane during mid- and late pregnancy. Mol. Cell. Endocrinol. 214 (2004) 39-52
    • (2004) Mol. Cell. Endocrinol. , vol.214 , pp. 39-52
    • An, B.S.1    Choi, K.C.2    Lee, G.S.3    Leung, P.C.4    Jeung, E.B.5
  • 9
    • 0032969866 scopus 로고    scopus 로고
    • Expression of macrophage migration inhibitory factor transcript and protein by first-trimester human trophoblasts
    • Arcuri F., Cintorino M., Vatti R., Carducci A., Liberatori S., and Paulesu L. Expression of macrophage migration inhibitory factor transcript and protein by first-trimester human trophoblasts. Biol. Reprod. 60 (1999) 1299-1303
    • (1999) Biol. Reprod. , vol.60 , pp. 1299-1303
    • Arcuri, F.1    Cintorino, M.2    Vatti, R.3    Carducci, A.4    Liberatori, S.5    Paulesu, L.6
  • 10
    • 2942533913 scopus 로고    scopus 로고
    • Translationally controlled tumor protein (TCTP) in the human prostate and prostate cancer cells: Expression, distribution, and calcium binding activity
    • Arcuri F., Papa S., Carducci A., Romagnoli R., Liberatori S., Riparbelli M.G., Sanchez J.C., Tosi P., and del Vecchio M.T. Translationally controlled tumor protein (TCTP) in the human prostate and prostate cancer cells: Expression, distribution, and calcium binding activity. Prostate 60 (2004) 130-140
    • (2004) Prostate , vol.60 , pp. 130-140
    • Arcuri, F.1    Papa, S.2    Carducci, A.3    Romagnoli, R.4    Liberatori, S.5    Riparbelli, M.G.6    Sanchez, J.C.7    Tosi, P.8    del Vecchio, M.T.9
  • 12
    • 0030869241 scopus 로고    scopus 로고
    • Calcium-regulating hormones and parathyroid hormone-related peptide in normal human pregnancy and postpartum: A longitudinal study
    • Ardawi M.S., Nasrat H.A., and HS B.A.A. Calcium-regulating hormones and parathyroid hormone-related peptide in normal human pregnancy and postpartum: A longitudinal study. Eur. J. Endocrinol. 137 (1997) 402-409
    • (1997) Eur. J. Endocrinol. , vol.137 , pp. 402-409
    • Ardawi, M.S.1    Nasrat, H.A.2    HS, B.A.A.3
  • 13
    • 0016781259 scopus 로고
    • Radioimmunoassay studies of intestinal calcium-binding protein in the pig. II. The distribution of intestinal CaBP in pig tissues
    • Arnold B.M., Kuttner M., Willis D.M., Hitchman A.J., Harrison J.E., and Murray T.M. Radioimmunoassay studies of intestinal calcium-binding protein in the pig. II. The distribution of intestinal CaBP in pig tissues. Can. J. Physiol. Pharmacol. 53 (1975) 1135-1140
    • (1975) Can. J. Physiol. Pharmacol. , vol.53 , pp. 1135-1140
    • Arnold, B.M.1    Kuttner, M.2    Willis, D.M.3    Hitchman, A.J.4    Harrison, J.E.5    Murray, T.M.6
  • 16
    • 0006698180 scopus 로고    scopus 로고
    • Placental transfer and intrauterine growth restriction
    • Kingdom J., and Baker P. (Eds), Springer-Verlag, London
    • Ayuk P., Hughes J., and Sibley C. Placental transfer and intrauterine growth restriction. In: Kingdom J., and Baker P. (Eds). "Intrauterine Growth Restriction. Aetiology and Management" (2000), Springer-Verlag, London 167-186
    • (2000) "Intrauterine Growth Restriction. Aetiology and Management" , pp. 167-186
    • Ayuk, P.1    Hughes, J.2    Sibley, C.3
  • 17
    • 0029155743 scopus 로고
    • + exchanger NHE-1 isoform in osteoblastic cells (UMR-106) via a cAMP-dependent pathway
    • + exchanger NHE-1 isoform in osteoblastic cells (UMR-106) via a cAMP-dependent pathway. J. Biol. Chem. 270 (1995) 23166-23172
    • (1995) J. Biol. Chem. , vol.270 , pp. 23166-23172
    • Azarani, A.1    Orlowski, J.2    Goltzman, D.3
  • 18
    • 1442326052 scopus 로고    scopus 로고
    • Calcium-sensing receptor regulation of renal mineral ion transport
    • Ba J., and Friedman P.A. Calcium-sensing receptor regulation of renal mineral ion transport. Cell Calcium 35 (2004) 229-237
    • (2004) Cell Calcium , vol.35 , pp. 229-237
    • Ba, J.1    Friedman, P.A.2
  • 20
    • 0020085878 scopus 로고
    • Calcium-binding protein distribution in the rat brain
    • Baimbridge K.G., Miller J.J., and Parkes C.O. Calcium-binding protein distribution in the rat brain. Brain Res. 239 (1982) 519-525
    • (1982) Brain Res. , vol.239 , pp. 519-525
    • Baimbridge, K.G.1    Miller, J.J.2    Parkes, C.O.3
  • 21
    • 0025609868 scopus 로고
    • Permeability of the human placenta in vivo to four non-metabolized hydrophilic molecules
    • Bain M.D., Copas D.K., Taylor A., Landon M.J., and Stacey T.E. Permeability of the human placenta in vivo to four non-metabolized hydrophilic molecules. J. Physiol. 431 (1990) 505-513
    • (1990) J. Physiol. , vol.431 , pp. 505-513
    • Bain, M.D.1    Copas, D.K.2    Taylor, A.3    Landon, M.J.4    Stacey, T.E.5
  • 23
    • 0024411849 scopus 로고
    • Retroviral long terminal repeat is the promoter of the gene encoding the tumor-associated calcium-binding protein oncomodulin in the rat
    • Banville D., and Boie Y. Retroviral long terminal repeat is the promoter of the gene encoding the tumor-associated calcium-binding protein oncomodulin in the rat. J. Mol. Biol. 207 (1989) 481-490
    • (1989) J. Mol. Biol. , vol.207 , pp. 481-490
    • Banville, D.1    Boie, Y.2
  • 24
    • 33745985212 scopus 로고
    • Electron microscopic studies on the placental villi in man. (Remarks on the syncytium problem)
    • Bargmann W., and Knoop A. Electron microscopic studies on the placental villi in man. (Remarks on the syncytium problem). Z. Zellforsch. Mikrosk. Anat. 50 (1959) 472-493
    • (1959) Z. Zellforsch. Mikrosk. Anat. , vol.50 , pp. 472-493
    • Bargmann, W.1    Knoop, A.2
  • 26
    • 0028929758 scopus 로고
    • Voltage-gated calcium currents have two opposing effects on the secretion of aldosterone
    • Barrett P.Q., Ertel E.A., Smith M.M., Nee J.J., and Cohen C.J. Voltage-gated calcium currents have two opposing effects on the secretion of aldosterone. Am. J. Physiol. 268 (1995) C985-C992
    • (1995) Am. J. Physiol. , vol.268
    • Barrett, P.Q.1    Ertel, E.A.2    Smith, M.M.3    Nee, J.J.4    Cohen, C.J.5
  • 27
    • 0033555775 scopus 로고    scopus 로고
    • Receptor-activated Ca2+ inflow in animal cells: A variety of pathways tailored to meet different intracellular Ca2+ signalling requirements
    • Barritt G.J. Receptor-activated Ca2+ inflow in animal cells: A variety of pathways tailored to meet different intracellular Ca2+ signalling requirements. Biochem. J. 337 Pt. 2 (1999) 153-169
    • (1999) Biochem. J. , vol.337 , Issue.PART 2 , pp. 153-169
    • Barritt, G.J.1
  • 29
    • 0023881058 scopus 로고
    • Reinvestigation of the sulfhydryl reactivity in bovine brain S100b (beta beta) protein and the microtubule-associated tau proteins. Ca2+ stimulates disulfide cross-linking between the S100b beta-subunit and the microtubule-associated tau(2) protein
    • Baudier J., and Cole R.D. Reinvestigation of the sulfhydryl reactivity in bovine brain S100b (beta beta) protein and the microtubule-associated tau proteins. Ca2+ stimulates disulfide cross-linking between the S100b beta-subunit and the microtubule-associated tau(2) protein. Biochemistry 27 (1988) 2728-2736
    • (1988) Biochemistry , vol.27 , pp. 2728-2736
    • Baudier, J.1    Cole, R.D.2
  • 30
    • 0022973592 scopus 로고
    • Ions binding to S100 proteins. I. Calcium- and zinc-binding properties of bovine brain S100 alpha alpha, S100a (alpha beta), and S100b (beta beta) protein: Zn2+ regulates Ca2+ binding on S100b protein
    • Baudier J., Glasser N., and Gerard D. Ions binding to S100 proteins. I. Calcium- and zinc-binding properties of bovine brain S100 alpha alpha, S100a (alpha beta), and S100b (beta beta) protein: Zn2+ regulates Ca2+ binding on S100b protein. J. Biol. Chem. 261 (1986) 8192-8203
    • (1986) J. Biol. Chem. , vol.261 , pp. 8192-8203
    • Baudier, J.1    Glasser, N.2    Gerard, D.3
  • 31
    • 0026633683 scopus 로고
    • S100P, a novel Ca(2+)-binding protein from human placenta. cDNA cloning, recombinant protein expression and Ca2+ binding properties
    • Becker T., Gerke V., Kube E., and Weber K. S100P, a novel Ca(2+)-binding protein from human placenta. cDNA cloning, recombinant protein expression and Ca2+ binding properties. Eur. J. Biochem. 207 (1992) 541-547
    • (1992) Eur. J. Biochem. , vol.207 , pp. 541-547
    • Becker, T.1    Gerke, V.2    Kube, E.3    Weber, K.4
  • 32
    • 0037837178 scopus 로고    scopus 로고
    • Expression of calbindin-D28k (CaBP28k) in trophoblasts from human term placenta
    • Belkacemi L., Gariepy G., Mounier C., Simoneau L., and Lafond J. Expression of calbindin-D28k (CaBP28k) in trophoblasts from human term placenta. Biol. Reprod. 68 (2003) 1943-1950
    • (2003) Biol. Reprod. , vol.68 , pp. 1943-1950
    • Belkacemi, L.1    Gariepy, G.2    Mounier, C.3    Simoneau, L.4    Lafond, J.5
  • 33
    • 2442691472 scopus 로고    scopus 로고
    • Calbindin-D9k (CaBP9k) localization and levels of expression in trophoblast cells from human term placenta
    • Belkacemi L., Gariepy G., Mounier C., Simoneau L., and Lafond J. Calbindin-D9k (CaBP9k) localization and levels of expression in trophoblast cells from human term placenta. Cell Tissue Res. 315 (2004) 107-117
    • (2004) Cell Tissue Res. , vol.315 , pp. 107-117
    • Belkacemi, L.1    Gariepy, G.2    Mounier, C.3    Simoneau, L.4    Lafond, J.5
  • 34
    • 19444371147 scopus 로고    scopus 로고
    • Calbindin-D28k (CaBP28k) identification and regulation by 1,25-dihydroxyvitamin D(3) in human choriocarcinoma cell line JEG-3
    • Belkacemi L., Zuegel U., Steinmeyer A., Dion J.P., and Lafond J. Calbindin-D28k (CaBP28k) identification and regulation by 1,25-dihydroxyvitamin D(3) in human choriocarcinoma cell line JEG-3. Mol. Cell. Endocrinol. 236 (2005) 31-41
    • (2005) Mol. Cell. Endocrinol. , vol.236 , pp. 31-41
    • Belkacemi, L.1    Zuegel, U.2    Steinmeyer, A.3    Dion, J.P.4    Lafond, J.5
  • 36
    • 0027285585 scopus 로고
    • Evolution of EF-hand calcium-modulated proteins. V. The genes encoding EF-hand proteins are not clustered in mammalian genomes
    • Berchtold M.W. Evolution of EF-hand calcium-modulated proteins. V. The genes encoding EF-hand proteins are not clustered in mammalian genomes. J. Mol. Evol. 36 (1993) 489-496
    • (1993) J. Mol. Evol. , vol.36 , pp. 489-496
    • Berchtold, M.W.1
  • 38
    • 0033061835 scopus 로고    scopus 로고
    • Differential regulation of skeletal muscle L-type Ca2+ current and excitation-contraction coupling by the dihydropyridine receptor beta subunit
    • Beurg M., Sukhareva M., Ahern C.A., Conklin M.W., Perez-Reyes E., Powers P.A., Gregg R.G., and Coronado R. Differential regulation of skeletal muscle L-type Ca2+ current and excitation-contraction coupling by the dihydropyridine receptor beta subunit. Biophys. J. 76 (1999) 1744-1756
    • (1999) Biophys. J. , vol.76 , pp. 1744-1756
    • Beurg, M.1    Sukhareva, M.2    Ahern, C.A.3    Conklin, M.W.4    Perez-Reyes, E.5    Powers, P.A.6    Gregg, R.G.7    Coronado, R.8
  • 39
    • 0030872506 scopus 로고    scopus 로고
    • T-type calcium channels facilitate insulin secretion by enhancing general excitability in the insulin-secreting beta-cell line, INS-1
    • Bhattacharjee A., Whitehurst Jr. R.M., Zhang M., Wang L., and Li M. T-type calcium channels facilitate insulin secretion by enhancing general excitability in the insulin-secreting beta-cell line, INS-1. Endocrinology 138 (1997) 3735-3740
    • (1997) Endocrinology , vol.138 , pp. 3735-3740
    • Bhattacharjee, A.1    Whitehurst Jr., R.M.2    Zhang, M.3    Wang, L.4    Li, M.5
  • 42
    • 4243573750 scopus 로고    scopus 로고
    • Paracrine and autocrine regulators of trophoblast invasion-a review
    • Bischof P., Meisser A., and Campana A. Paracrine and autocrine regulators of trophoblast invasion-a review. Placenta 21 Suppl. A (2000) S55-S60
    • (2000) Placenta , vol.21 , Issue.SUPPL. A
    • Bischof, P.1    Meisser, A.2    Campana, A.3
  • 43
    • 0032801648 scopus 로고    scopus 로고
    • Sodium/calcium exchange: Its physiological implications
    • Blaustein M.P., and Lederer W.J. Sodium/calcium exchange: Its physiological implications. Physiol. Rev. 79 (1999) 763-854
    • (1999) Physiol. Rev. , vol.79 , pp. 763-854
    • Blaustein, M.P.1    Lederer, W.J.2
  • 44
    • 0028936338 scopus 로고
    • Glial fibrillary acidic protein in the cerebrospinal fluid: A possible indicator of prognosis in full-term asphyxiated newborn infants?
    • Blennow M., Hagberg H., and Rosengren L. Glial fibrillary acidic protein in the cerebrospinal fluid: A possible indicator of prognosis in full-term asphyxiated newborn infants?. Pediatr. Res. 37 (1995) 260-264
    • (1995) Pediatr. Res. , vol.37 , pp. 260-264
    • Blennow, M.1    Hagberg, H.2    Rosengren, L.3
  • 45
    • 0024417982 scopus 로고
    • The growth-related protein P23 of the Ehrlich ascites tumor: Translational control, cloning and primary structure
    • Bohm H., Benndorf R., Gaestel M., Gross B., Nurnberg P., Kraft R., Otto A., and Bielka H. The growth-related protein P23 of the Ehrlich ascites tumor: Translational control, cloning and primary structure. Biochem. Int. 19 (1989) 277-286
    • (1989) Biochem. Int. , vol.19 , pp. 277-286
    • Bohm, H.1    Benndorf, R.2    Gaestel, M.3    Gross, B.4    Nurnberg, P.5    Kraft, R.6    Otto, A.7    Bielka, H.8
  • 46
    • 0347480218 scopus 로고    scopus 로고
    • The translationally controlled tumour protein (TCTP)
    • Bommer U.A., and Thiele B.J. The translationally controlled tumour protein (TCTP). Int. J. Biochem. Cell Biol. 36 (2004) 379-385
    • (2004) Int. J. Biochem. Cell Biol. , vol.36 , pp. 379-385
    • Bommer, U.A.1    Thiele, B.J.2
  • 48
    • 0013925257 scopus 로고
    • Electron microscopic observations on the cytotrophoblast contribution to the syncytium in the human placenta
    • Boyd J.D., and Hamilton W.J. Electron microscopic observations on the cytotrophoblast contribution to the syncytium in the human placenta. J. Anat. 100 (1966) 535-548
    • (1966) J. Anat. , vol.100 , pp. 535-548
    • Boyd, J.D.1    Hamilton, W.J.2
  • 50
    • 0014261698 scopus 로고
    • The surface of the syncytium of the human chorionic villus
    • Boyd J.D., Hamilton W.J., and Boyd C.A. The surface of the syncytium of the human chorionic villus. J. Anat. 102 (1968) 553-563
    • (1968) J. Anat. , vol.102 , pp. 553-563
    • Boyd, J.D.1    Hamilton, W.J.2    Boyd, C.A.3
  • 53
    • 0034282412 scopus 로고    scopus 로고
    • Regulation of 25-hydroxyvitamin D3 1alpha-hydroxylase gene expression by parathyroid hormone and 1,25-dihydroxyvitamin D3
    • Brenza H.L., and DeLuca H.F. Regulation of 25-hydroxyvitamin D3 1alpha-hydroxylase gene expression by parathyroid hormone and 1,25-dihydroxyvitamin D3. Arch. Biochem. Biophys. 381 (2000) 143-152
    • (2000) Arch. Biochem. Biophys. , vol.381 , pp. 143-152
    • Brenza, H.L.1    DeLuca, H.F.2
  • 54
    • 0022349457 scopus 로고
    • Localization and synthesis of the tumor protein oncomodulin in extraembryonic tissues of the fetal rat
    • Brewer L.M., and MacManus J.P. Localization and synthesis of the tumor protein oncomodulin in extraembryonic tissues of the fetal rat. Dev. Biol. 112 (1985) 49-58
    • (1985) Dev. Biol. , vol.112 , pp. 49-58
    • Brewer, L.M.1    MacManus, J.P.2
  • 55
    • 0023281267 scopus 로고
    • Detection of oncomodulin, an oncodevelopmental protein in human placenta and choriocarcinoma cell lines
    • Brewer L.M., and MacManus J.P. Detection of oncomodulin, an oncodevelopmental protein in human placenta and choriocarcinoma cell lines. Placenta 8 (1987) 351-363
    • (1987) Placenta , vol.8 , pp. 351-363
    • Brewer, L.M.1    MacManus, J.P.2
  • 56
    • 0037406261 scopus 로고    scopus 로고
    • S100 protein subcellular localization during epidermal differentiation and psoriasis
    • Broome A.M., Ryan D., and Eckert R.L. S100 protein subcellular localization during epidermal differentiation and psoriasis. J. Histochem. Cytochem. 51 (2003) 675-685
    • (2003) J. Histochem. Cytochem. , vol.51 , pp. 675-685
    • Broome, A.M.1    Ryan, D.2    Eckert, R.L.3
  • 60
    • 0017857618 scopus 로고
    • Placental calcium binding protein in rats. Apparent identity with vitamin D-dependent calcium binding protein from rat intestine
    • Bruns M.E., Fausto A., and Avioli L.V. Placental calcium binding protein in rats. Apparent identity with vitamin D-dependent calcium binding protein from rat intestine. J. Biol. Chem. 253 (1978) 3186-3190
    • (1978) J. Biol. Chem. , vol.253 , pp. 3186-3190
    • Bruns, M.E.1    Fausto, A.2    Avioli, L.V.3
  • 61
    • 0020052117 scopus 로고
    • Regulation of calcium-binding protein in mouse placenta and intestine
    • Bruns M.E., Wallshein V., and Bruns D.E. Regulation of calcium-binding protein in mouse placenta and intestine. Am. J. Physiol. 242 (1982) E47-E52
    • (1982) Am. J. Physiol. , vol.242
    • Bruns, M.E.1    Wallshein, V.2    Bruns, D.E.3
  • 62
    • 0021269071 scopus 로고
    • Identification of calmodulin-binding proteins in chicken embryo fibroblasts
    • Burgess W.H., Watterson D.M., and Van Eldik L.J. Identification of calmodulin-binding proteins in chicken embryo fibroblasts. J. Cell Biol. 99 (1984) 550-557
    • (1984) J. Cell Biol. , vol.99 , pp. 550-557
    • Burgess, W.H.1    Watterson, D.M.2    Van Eldik, L.J.3
  • 63
    • 0032876371 scopus 로고    scopus 로고
    • Maternal arterial connections to the placental intervillous space during the first trimester of human pregnancy: The Boyd collection revisited
    • Burton G.J., Jauniaux E., and Watson A.L. Maternal arterial connections to the placental intervillous space during the first trimester of human pregnancy: The Boyd collection revisited. Am. J. Obstet. Gynecol. 181 (1999) 718-724
    • (1999) Am. J. Obstet. Gynecol. , vol.181 , pp. 718-724
    • Burton, G.J.1    Jauniaux, E.2    Watson, A.L.3
  • 64
    • 0022993464 scopus 로고
    • Molecular cloning of the cDNA for a growth factor-inducible gene with strong homology to S-100, a calcium-binding protein
    • Calabretta B., Battini R., Kaczmarek L., de Riel J.K., and Baserga R. Molecular cloning of the cDNA for a growth factor-inducible gene with strong homology to S-100, a calcium-binding protein. J. Biol. Chem. 261 (1986) 12628-12632
    • (1986) J. Biol. Chem. , vol.261 , pp. 12628-12632
    • Calabretta, B.1    Battini, R.2    Kaczmarek, L.3    de Riel, J.K.4    Baserga, R.5
  • 65
    • 0036544601 scopus 로고    scopus 로고
    • Regulation of calbindin-D9k expression by 1,25-dihydroxyvitamin D(3) and parathyroid hormone in mouse primary renal tubular cells
    • Cao L.P., Bolt M.J., Wei M., Sitrin M.D., and Chun Li Y. Regulation of calbindin-D9k expression by 1,25-dihydroxyvitamin D(3) and parathyroid hormone in mouse primary renal tubular cells. Arch. Biochem. Biophys. 400 (2002) 118-124
    • (2002) Arch. Biochem. Biophys. , vol.400 , pp. 118-124
    • Cao, L.P.1    Bolt, M.J.2    Wei, M.3    Sitrin, M.D.4    Chun Li, Y.5
  • 66
    • 0023069451 scopus 로고
    • Intracellular calcium homeostasis
    • Carafoli E. Intracellular calcium homeostasis. Annu. Rev. Biochem. 56 (1987) 395-433
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 395-433
    • Carafoli, E.1
  • 67
    • 0026074512 scopus 로고
    • Calcium pump of the plasma membrane
    • Carafoli E. Calcium pump of the plasma membrane. Physiol. Rev. 71 (1991) 129-153
    • (1991) Physiol. Rev. , vol.71 , pp. 129-153
    • Carafoli, E.1
  • 68
    • 0033520919 scopus 로고    scopus 로고
    • The rate of activation by calmodulin of isoform 4 of the plasma membrane Ca(2+) pump is slow and is changed by alternative splicing
    • Caride A.J., Elwess N.L., Verma A.K., Filoteo A.G., Enyedi A., Bajzer Z., and Penniston J.T. The rate of activation by calmodulin of isoform 4 of the plasma membrane Ca(2+) pump is slow and is changed by alternative splicing. J. Biol. Chem. 274 (1999) 35227-35232
    • (1999) J. Biol. Chem. , vol.274 , pp. 35227-35232
    • Caride, A.J.1    Elwess, N.L.2    Verma, A.K.3    Filoteo, A.G.4    Enyedi, A.5    Bajzer, Z.6    Penniston, J.T.7
  • 69
    • 0142089028 scopus 로고    scopus 로고
    • Preeclampsia and calcium-ATPase activity of plasma membranes from human myometrium and placental trophoblast
    • Carrera F., Casart Y.C., Proverbio T., Proverbio F., and Marin R. Preeclampsia and calcium-ATPase activity of plasma membranes from human myometrium and placental trophoblast. Hypertens. Pregnancy 22 (2003) 295-304
    • (2003) Hypertens. Pregnancy , vol.22 , pp. 295-304
    • Carrera, F.1    Casart, Y.C.2    Proverbio, T.3    Proverbio, F.4    Marin, R.5
  • 70
    • 0035165353 scopus 로고    scopus 로고
    • Comparative study of the calcium adenosine triphosphatase of basal membranes of human placental trophoblasts from normotensive and preeclamptic pregnant women
    • Casart Y., Proverbio T., Marin R., and Proverbio F. Comparative study of the calcium adenosine triphosphatase of basal membranes of human placental trophoblasts from normotensive and preeclamptic pregnant women. Gynecol. Obstet. Invest. 51 (2001) 28-31
    • (2001) Gynecol. Obstet. Invest. , vol.51 , pp. 28-31
    • Casart, Y.1    Proverbio, T.2    Marin, R.3    Proverbio, F.4
  • 71
    • 0031783082 scopus 로고    scopus 로고
    • Identification of L-type calcium channels associated with kappa opioid receptors in human placenta
    • Cemerikic B., Zamah R., and Ahmed M.S. Identification of L-type calcium channels associated with kappa opioid receptors in human placenta. J. Mol. Neurosci. 10 (1998) 261-272
    • (1998) J. Mol. Neurosci. , vol.10 , pp. 261-272
    • Cemerikic, B.1    Zamah, R.2    Ahmed, M.S.3
  • 72
    • 0029796174 scopus 로고    scopus 로고
    • The calcium-sensing receptor: A window into the physiology and pathophysiology of mineral ion metabolism
    • Chattopadhyay N., Mithal A., and Brown E.M. The calcium-sensing receptor: A window into the physiology and pathophysiology of mineral ion metabolism. Endocr. Rev. 17 (1996) 289-307
    • (1996) Endocr. Rev. , vol.17 , pp. 289-307
    • Chattopadhyay, N.1    Mithal, A.2    Brown, E.M.3
  • 73
    • 0034739871 scopus 로고    scopus 로고
    • The Na+-Ca2+ exchanger is essential for embryonic heart development in mice
    • Cho C.H., Kim S.S., Jeong M.J., Lee C.O., and Shin H.S. The Na+-Ca2+ exchanger is essential for embryonic heart development in mice. Mol. Cells 10 (2000) 712-722
    • (2000) Mol. Cells , vol.10 , pp. 712-722
    • Cho, C.H.1    Kim, S.S.2    Jeong, M.J.3    Lee, C.O.4    Shin, H.S.5
  • 74
    • 0038823690 scopus 로고    scopus 로고
    • Partial rescue of the Na+-Ca2+ exchanger (NCX1) knock-out mouse by transgenic expression of NCX1
    • Cho C.H., Lee S.Y., Shin H.S., Philipson K.D., and Lee C.O. Partial rescue of the Na+-Ca2+ exchanger (NCX1) knock-out mouse by transgenic expression of NCX1. Exp. Mol. Med. 35 (2003) 125-135
    • (2003) Exp. Mol. Med. , vol.35 , pp. 125-135
    • Cho, C.H.1    Lee, S.Y.2    Shin, H.S.3    Philipson, K.D.4    Lee, C.O.5
  • 75
    • 0018198094 scopus 로고
    • Vitamin D3-induced calcium binding protein in bone tissue
    • Christakos S., and Norman A.W. Vitamin D3-induced calcium binding protein in bone tissue. Science 202 (1978) 70-71
    • (1978) Science , vol.202 , pp. 70-71
    • Christakos, S.1    Norman, A.W.2
  • 76
    • 0024344467 scopus 로고
    • Vitamin D-dependent calcium binding proteins: Chemistry, distribution, functional considerations, and molecular biology
    • Christakos S., Gabrielides C., and Rhoten W.B. Vitamin D-dependent calcium binding proteins: Chemistry, distribution, functional considerations, and molecular biology. Endocr. Rev. 10 (1989) 3-26
    • (1989) Endocr. Rev. , vol.10 , pp. 3-26
    • Christakos, S.1    Gabrielides, C.2    Rhoten, W.B.3
  • 77
    • 0038455890 scopus 로고    scopus 로고
    • Store-operated Ca2+ entry in first trimester and term human placenta
    • Clarson L.H., Roberts V.H., Hamark B., Elliott A.C., and Powell T. Store-operated Ca2+ entry in first trimester and term human placenta. J. Physiol. 550 (2003) 515-528
    • (2003) J. Physiol. , vol.550 , pp. 515-528
    • Clarson, L.H.1    Roberts, V.H.2    Hamark, B.3    Elliott, A.C.4    Powell, T.5
  • 78
    • 0036017357 scopus 로고    scopus 로고
    • The effect of smoking on bone metabolism: Maternal and cord blood bone marker levels
    • Colak O., Alatas O., Aydogdu S., and Uslu S. The effect of smoking on bone metabolism: Maternal and cord blood bone marker levels. Clin. Biochem. 35 (2002) 247-250
    • (2002) Clin. Biochem. , vol.35 , pp. 247-250
    • Colak, O.1    Alatas, O.2    Aydogdu, S.3    Uslu, S.4
  • 79
    • 0029133887 scopus 로고
    • Long-term effects of calcium availability on prolactin and protein synthesis in human decidual cells
    • Couderc B., Dufy-Barbe L., and Sartor P. Long-term effects of calcium availability on prolactin and protein synthesis in human decidual cells. Placenta 16 (1995) 527-537
    • (1995) Placenta , vol.16 , pp. 527-537
    • Couderc, B.1    Dufy-Barbe, L.2    Sartor, P.3
  • 81
    • 0028618660 scopus 로고
    • Implantation and the placenta: Key pieces of the development puzzle
    • Cross J.C., Werb Z., and Fisher S.J. Implantation and the placenta: Key pieces of the development puzzle. Science 266 (1994) 1508-1518
    • (1994) Science , vol.266 , pp. 1508-1518
    • Cross, J.C.1    Werb, Z.2    Fisher, S.J.3
  • 82
    • 0028840178 scopus 로고
    • Calcium homeostasis and bone metabolism during pregnancy, lactation, and postweaning: A longitudinal study
    • Cross N.A., Hillman L.S., Allen S.H., Krause G.F., and Vieira N.E. Calcium homeostasis and bone metabolism during pregnancy, lactation, and postweaning: A longitudinal study. Am. J. Clin. Nutr. 61 (1995) 514-523
    • (1995) Am. J. Clin. Nutr. , vol.61 , pp. 514-523
    • Cross, N.A.1    Hillman, L.S.2    Allen, S.H.3    Krause, G.F.4    Vieira, N.E.5
  • 83
    • 0026569632 scopus 로고
    • Identification of a 1,25-dihydroxyvitamin D3-response element in the 5′-flanking region of the rat calbindin D-9k gene
    • Darwish H.M., and DeLuca H.F. Identification of a 1,25-dihydroxyvitamin D3-response element in the 5′-flanking region of the rat calbindin D-9k gene. Proc. Natl. Acad. Sci. USA 89 (1992) 603-607
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 603-607
    • Darwish, H.M.1    DeLuca, H.F.2
  • 84
    • 0019862289 scopus 로고
    • Calcium-ion-binding activity in human small-intestinal mucosal cytosol. Purification of two proteins and interrelationship of calcium-binding fractions
    • Davie M. Calcium-ion-binding activity in human small-intestinal mucosal cytosol. Purification of two proteins and interrelationship of calcium-binding fractions. Biochem. J. 197 (1981) 55-65
    • (1981) Biochem. J. , vol.197 , pp. 55-65
    • Davie, M.1
  • 85
    • 18544388495 scopus 로고    scopus 로고
    • Apoptosis and human placenta: Expression of proteins belonging to different apoptotic pathways during pregnancy
    • De Falco M., Penta R., Laforgia V., Cobellis L., and De Luca A. Apoptosis and human placenta: Expression of proteins belonging to different apoptotic pathways during pregnancy. J. Exp. Clin. Cancer Res. 24 (2005) 25-33
    • (2005) J. Exp. Clin. Cancer Res. , vol.24 , pp. 25-33
    • De Falco, M.1    Penta, R.2    Laforgia, V.3    Cobellis, L.4    De Luca, A.5
  • 87
    • 0020552568 scopus 로고
    • In rat uterus 17 beta-estradiol stimulates a calcium-binding protein similar to the duodenal vitamin D-dependent calcium-binding protein
    • Delorme A.C., Danan J.L., Acker M.G., Ripoche M.A., and Mathieu H. In rat uterus 17 beta-estradiol stimulates a calcium-binding protein similar to the duodenal vitamin D-dependent calcium-binding protein. Endocrinology 113 (1983) 1340-1347
    • (1983) Endocrinology , vol.113 , pp. 1340-1347
    • Delorme, A.C.1    Danan, J.L.2    Acker, M.G.3    Ripoche, M.A.4    Mathieu, H.5
  • 88
    • 0019958747 scopus 로고
    • Control of vitamin D metabolism in preterm infants: Feto-maternal relationships
    • Delvin E.E., Glorieux F.H., Salle B.L., David L., and Varenne J.P. Control of vitamin D metabolism in preterm infants: Feto-maternal relationships. Arch. Dis. Child 57 (1982) 754-757
    • (1982) Arch. Dis. Child , vol.57 , pp. 754-757
    • Delvin, E.E.1    Glorieux, F.H.2    Salle, B.L.3    David, L.4    Varenne, J.P.5
  • 89
    • 0029019032 scopus 로고
    • Evidence of increased intrauterine bone resorption in term infants of mothers with insulin-dependent diabetes
    • Demarini S., Specker B.L., Sierra R.I., Miodovnik M., and Tsang R.C. Evidence of increased intrauterine bone resorption in term infants of mothers with insulin-dependent diabetes. J. Pediatr. 126 (1995) 796-798
    • (1995) J. Pediatr. , vol.126 , pp. 796-798
    • Demarini, S.1    Specker, B.L.2    Sierra, R.I.3    Miodovnik, M.4    Tsang, R.C.5
  • 90
    • 0036345262 scopus 로고    scopus 로고
    • Expression and activity of 25-hydroxyvitamin D-1 alpha-hydroxylase are restricted in cultures of human syncytiotrophoblast cells from preeclamptic pregnancies
    • Diaz L., Arranz C., Avila E., Halhali A., Vilchis F., and Larrea F. Expression and activity of 25-hydroxyvitamin D-1 alpha-hydroxylase are restricted in cultures of human syncytiotrophoblast cells from preeclamptic pregnancies. J. Clin. Endocrinol. Metab. 87 (2002) 3876-3882
    • (2002) J. Clin. Endocrinol. Metab. , vol.87 , pp. 3876-3882
    • Diaz, L.1    Arranz, C.2    Avila, E.3    Halhali, A.4    Vilchis, F.5    Larrea, F.6
  • 91
    • 0032983595 scopus 로고    scopus 로고
    • Functional roles of S100 proteins, calcium-binding proteins of the EF-hand type
    • Donato R. Functional roles of S100 proteins, calcium-binding proteins of the EF-hand type. Biochim. Biophys. Acta 1450 (1999) 191-231
    • (1999) Biochim. Biophys. Acta , vol.1450 , pp. 191-231
    • Donato, R.1
  • 92
    • 0034995073 scopus 로고    scopus 로고
    • S100: A multigenic family of calcium-modulated proteins of the EF-hand type with intracellular and extracellular functional roles
    • Donato R. S100: A multigenic family of calcium-modulated proteins of the EF-hand type with intracellular and extracellular functional roles. Int. J. Biochem. Cell Biol. 33 (2001) 637-668
    • (2001) Int. J. Biochem. Cell Biol. , vol.33 , pp. 637-668
    • Donato, R.1
  • 93
    • 0024359664 scopus 로고
    • Molecular interaction of S-100 proteins with microtubule proteins in vitro
    • Donato R., Giambanco I., and Aisa M.C. Molecular interaction of S-100 proteins with microtubule proteins in vitro. J. Neurochem. 53 (1989) 566-571
    • (1989) J. Neurochem. , vol.53 , pp. 566-571
    • Donato, R.1    Giambanco, I.2    Aisa, M.C.3
  • 94
    • 0016810103 scopus 로고
    • Primary hyperparathyroidism during the third trimester of pregnancy
    • Dorey L.G., and Gell J.W. Primary hyperparathyroidism during the third trimester of pregnancy. Obstet. Gynecol. 45 (1975) 469-472
    • (1975) Obstet. Gynecol. , vol.45 , pp. 469-472
    • Dorey, L.G.1    Gell, J.W.2
  • 95
    • 0030472423 scopus 로고    scopus 로고
    • Mechanisms of maternofetal chloride transfer across the human placenta perfused in vitro
    • Doughty I.M., Glazier J.D., Greenwood S.L., Boyd R.D., and Sibley C.P. Mechanisms of maternofetal chloride transfer across the human placenta perfused in vitro. Am. J. Physiol. 271 (1996) R1701-R1706
    • (1996) Am. J. Physiol. , vol.271
    • Doughty, I.M.1    Glazier, J.D.2    Greenwood, S.L.3    Boyd, R.D.4    Sibley, C.P.5
  • 96
    • 0026447131 scopus 로고
    • Calbindin-D9K gene expression in the lung of the rat. Absence of regulation by 1,25-dihydroxyvitamin D3 and estrogen
    • Dupret J.M., L'Horset F., Perret C., Bernaudin J.F., and Thomasset M. Calbindin-D9K gene expression in the lung of the rat. Absence of regulation by 1,25-dihydroxyvitamin D3 and estrogen. Endocrinology 131 (1992) 2643-2648
    • (1992) Endocrinology , vol.131 , pp. 2643-2648
    • Dupret, J.M.1    L'Horset, F.2    Perret, C.3    Bernaudin, J.F.4    Thomasset, M.5
  • 97
    • 0027401833 scopus 로고
    • Paracellular permeability pathways in the human placenta: A quantitative and morphological study of maternal-fetal transfer of horseradish peroxidase
    • Edwards D., Jones C.J., Sibley C.P., and Nelson D.M. Paracellular permeability pathways in the human placenta: A quantitative and morphological study of maternal-fetal transfer of horseradish peroxidase. Placenta 14 (1993) 63-73
    • (1993) Placenta , vol.14 , pp. 63-73
    • Edwards, D.1    Jones, C.J.2    Sibley, C.P.3    Nelson, D.M.4
  • 100
    • 0030610570 scopus 로고    scopus 로고
    • Plasma membrane Ca2+ pump isoforms 2a and 2b are unusually responsive to calmodulin and Ca2+
    • Elwess N.L., Filoteo A.G., Enyedi A., and Penniston J.T. Plasma membrane Ca2+ pump isoforms 2a and 2b are unusually responsive to calmodulin and Ca2+. J. Biol. Chem. 272 (1997) 17981-17986
    • (1997) J. Biol. Chem. , vol.272 , pp. 17981-17986
    • Elwess, N.L.1    Filoteo, A.G.2    Enyedi, A.3    Penniston, J.T.4
  • 102
    • 0026600297 scopus 로고
    • Purification and characterization of a new member of the S-100 protein family from human placenta
    • Emoto Y., Kobayashi R., Akatsuka H., and Hidaka H. Purification and characterization of a new member of the S-100 protein family from human placenta. Biochem. Biophys. Res. Commun. 182 (1992) 1246-1253
    • (1992) Biochem. Biophys. Res. Commun. , vol.182 , pp. 1246-1253
    • Emoto, Y.1    Kobayashi, R.2    Akatsuka, H.3    Hidaka, H.4
  • 104
    • 0022517564 scopus 로고
    • Fetal nutrition: Supply, combustion, interconversion, and deposition
    • Faber J.J., and Thornburg K.L. Fetal nutrition: Supply, combustion, interconversion, and deposition. Fed. Proc. 45 (1986) 2502-2507
    • (1986) Fed. Proc. , vol.45 , pp. 2502-2507
    • Faber, J.J.1    Thornburg, K.L.2
  • 105
    • 0031877854 scopus 로고    scopus 로고
    • Calcyclin in the mouse decidua: Expression and effects on placental lactogen secretion
    • Farnsworth R.L., and Talamantes F. Calcyclin in the mouse decidua: Expression and effects on placental lactogen secretion. Biol. Reprod. 59 (1998) 546-552
    • (1998) Biol. Reprod. , vol.59 , pp. 546-552
    • Farnsworth, R.L.1    Talamantes, F.2
  • 106
    • 0033835040 scopus 로고    scopus 로고
    • Parathyroid hormone(1-34) and parathyroid hormone-related protein(1-34) stimulate calcium release from human syncytiotrophoblast basal membranes via a common receptor
    • Farrugia W., de Gooyer T., Rice G.E., Moseley J.M., and Wlodek M.E. Parathyroid hormone(1-34) and parathyroid hormone-related protein(1-34) stimulate calcium release from human syncytiotrophoblast basal membranes via a common receptor. J. Endocrinol. 166 (2000) 689-695
    • (2000) J. Endocrinol. , vol.166 , pp. 689-695
    • Farrugia, W.1    de Gooyer, T.2    Rice, G.E.3    Moseley, J.M.4    Wlodek, M.E.5
  • 108
    • 0028278291 scopus 로고
    • Expression of parathyroid hormone-related protein and its receptor in human umbilical cord: Evidence for a paracrine system involving umbilical vessels
    • discussion: 1024-1026.
    • Ferguson J.E., Seaner II R., Bruns D.E., Redick J.A., Mills S.E., Juppner H., Segre G.V., and Bruns M.E. Expression of parathyroid hormone-related protein and its receptor in human umbilical cord: Evidence for a paracrine system involving umbilical vessels. Am. J. Obstet. Gynecol. 170 (1994) 1018-1024 discussion: 1024-1026.
    • (1994) Am. J. Obstet. Gynecol. , vol.170 , pp. 1018-1024
    • Ferguson, J.E.1    Seaner II, R.2    Bruns, D.E.3    Redick, J.A.4    Mills, S.E.5    Juppner, H.6    Segre, G.V.7    Bruns, M.E.8
  • 109
    • 0023106598 scopus 로고
    • ATP-dependent calcium transport across basal plasma membranes of human placental trophoblast
    • Fisher G.J., Kelley L.K., and Smith C.H. ATP-dependent calcium transport across basal plasma membranes of human placental trophoblast. Am. J. Physiol. 252 (1987) C38-C46
    • (1987) Am. J. Physiol. , vol.252
    • Fisher, G.J.1    Kelley, L.K.2    Smith, C.H.3
  • 112
    • 0018653936 scopus 로고
    • Indirect immunofluorescent localization of prolactin to the cytoplasm of decidua and trophoblast cells in human placental membranes at term
    • Frame L.T., Wiley L., and Rogol A.D. Indirect immunofluorescent localization of prolactin to the cytoplasm of decidua and trophoblast cells in human placental membranes at term. J. Clin. Endocrinol. Metab. 49 (1979) 435-437
    • (1979) J. Clin. Endocrinol. Metab. , vol.49 , pp. 435-437
    • Frame, L.T.1    Wiley, L.2    Rogol, A.D.3
  • 115
    • 0034089471 scopus 로고    scopus 로고
    • Myeloid-related proteins 8 and 14 are specifically secreted during interaction of phagocytes and activated endothelium and are useful markers for monitoring disease activity in pauciarticular-onset juvenile rheumatoid arthritis
    • Frosch M., Strey A., Vogl T., Wulffraat N.M., Kuis W., Sunderkotter C., Harms E., Sorg C., and Roth J. Myeloid-related proteins 8 and 14 are specifically secreted during interaction of phagocytes and activated endothelium and are useful markers for monitoring disease activity in pauciarticular-onset juvenile rheumatoid arthritis. Arthritis Rheum. 43 (2000) 628-637
    • (2000) Arthritis Rheum. , vol.43 , pp. 628-637
    • Frosch, M.1    Strey, A.2    Vogl, T.3    Wulffraat, N.M.4    Kuis, W.5    Sunderkotter, C.6    Harms, E.7    Sorg, C.8    Roth, J.9
  • 117
    • 0030580082 scopus 로고    scopus 로고
    • Characterization of type III intermediate filament regulatory protein target epitopes: S-100 (beta and/or alpha) binds the N-terminal head domain; annexin II2-p11(2) binds the rod domain
    • Garbuglia M., Verzini M., Dimlich R.V., Jamieson Jr. G.A., and Donato R. Characterization of type III intermediate filament regulatory protein target epitopes: S-100 (beta and/or alpha) binds the N-terminal head domain; annexin II2-p11(2) binds the rod domain. Biochim. Biophys. Acta 1313 (1996) 268-276
    • (1996) Biochim. Biophys. Acta , vol.1313 , pp. 268-276
    • Garbuglia, M.1    Verzini, M.2    Dimlich, R.V.3    Jamieson Jr., G.A.4    Donato, R.5
  • 118
    • 0017115884 scopus 로고
    • Calcium metabolism in newborn animals: The interrelationship of calcium, magnesium, and inorganic phosphorus in newborn rats, foals, lambs, and calves
    • Garel J.M., and Barlet J.P. Calcium metabolism in newborn animals: The interrelationship of calcium, magnesium, and inorganic phosphorus in newborn rats, foals, lambs, and calves. Pediatr. Res. 10 (1976) 749-754
    • (1976) Pediatr. Res. , vol.10 , pp. 749-754
    • Garel, J.M.1    Barlet, J.P.2
  • 119
    • 0029994295 scopus 로고    scopus 로고
    • The role of the placenta in fetal nutrition and growth
    • Garnica A.D., and Chan W.Y. The role of the placenta in fetal nutrition and growth. J. Am. Coll. Nutr. 15 (1996) 206-222
    • (1996) J. Am. Coll. Nutr. , vol.15 , pp. 206-222
    • Garnica, A.D.1    Chan, W.Y.2
  • 121
    • 0032716073 scopus 로고    scopus 로고
    • Elevated S100 blood level as an early indicator of intraventricular hemorrhage in preterm infants. Correlation with cerebral Doppler velocimetry
    • Gazzolo D., Vinesi P., Bartocci M., Geloso M.C., Bonacci W., Serra G., Haglid K.G., and Michetti F. Elevated S100 blood level as an early indicator of intraventricular hemorrhage in preterm infants. Correlation with cerebral Doppler velocimetry. J. Neurol. Sci. 170 (1999) 32-35
    • (1999) J. Neurol. Sci. , vol.170 , pp. 32-35
    • Gazzolo, D.1    Vinesi, P.2    Bartocci, M.3    Geloso, M.C.4    Bonacci, W.5    Serra, G.6    Haglid, K.G.7    Michetti, F.8
  • 123
    • 0022157945 scopus 로고
    • The regulatory chain in the p36-kd substrate complex of viral tyrosine-specific protein kinases is related in sequence to the S-100 protein of glial cells
    • Gerke V., and Weber K. The regulatory chain in the p36-kd substrate complex of viral tyrosine-specific protein kinases is related in sequence to the S-100 protein of glial cells. EMBO J. 4 (1985) 2917-2920
    • (1985) EMBO J. , vol.4 , pp. 2917-2920
    • Gerke, V.1    Weber, K.2
  • 124
    • 0033152603 scopus 로고    scopus 로고
    • Current modulation and membrane targeting of the calcium channel alpha1C subunit are independent functions of the beta subunit
    • Gerster U., Neuhuber B., Groschner K., Striessnig J., and Flucher B.E. Current modulation and membrane targeting of the calcium channel alpha1C subunit are independent functions of the beta subunit. J. Physiol. 517 Pt. 2 (1999) 353-368
    • (1999) J. Physiol. , vol.517 , Issue.PART 2 , pp. 353-368
    • Gerster, U.1    Neuhuber, B.2    Groschner, K.3    Striessnig, J.4    Flucher, B.E.5
  • 126
    • 0023944134 scopus 로고
    • Varying oncomodulin mRNA abundance in developing placenta and solid tumors
    • Gillen M.F., Brewer L.M., and MacManus J.P. Varying oncomodulin mRNA abundance in developing placenta and solid tumors. Cancer Lett. 40 (1988) 151-160
    • (1988) Cancer Lett. , vol.40 , pp. 151-160
    • Gillen, M.F.1    Brewer, L.M.2    MacManus, J.P.3
  • 128
    • 0016734270 scopus 로고
    • Voltage clamp analysis of two inward current mechanisms in the egg cell membrane of a starfish
    • Hagiwara S., Ozawa S., and Sand O. Voltage clamp analysis of two inward current mechanisms in the egg cell membrane of a starfish. J. Gen. Physiol. 65 (1975) 617-644
    • (1975) J. Gen. Physiol. , vol.65 , pp. 617-644
    • Hagiwara, S.1    Ozawa, S.2    Sand, O.3
  • 129
    • 0034989086 scopus 로고    scopus 로고
    • Calcitonin gene- and parathyroid hormone-related peptides in preeclampsia: Effects of magnesium sulfate
    • Halhali A., Wimalawansa S.J., Berentsen V., Avila E., Thota C.S., and Larrea F. Calcitonin gene- and parathyroid hormone-related peptides in preeclampsia: Effects of magnesium sulfate. Obstet. Gynecol. 97 (2001) 893-897
    • (2001) Obstet. Gynecol. , vol.97 , pp. 893-897
    • Halhali, A.1    Wimalawansa, S.J.2    Berentsen, V.3    Avila, E.4    Thota, C.S.5    Larrea, F.6
  • 132
    • 0016609868 scopus 로고
    • Intestinal calcium-binding protein in animals fed normal and rachitogenic diets: I. Rat studies
    • Harrison J.E., Hitchman A.J., and Tam C.S. Intestinal calcium-binding protein in animals fed normal and rachitogenic diets: I. Rat studies. Can. J. Physiol. Pharmacol. 53 (1975) 137-143
    • (1975) Can. J. Physiol. Pharmacol. , vol.53 , pp. 137-143
    • Harrison, J.E.1    Hitchman, A.J.2    Tam, C.S.3
  • 133
    • 0034177642 scopus 로고    scopus 로고
    • From worm to man: Three subfamilies of TRP channels
    • Harteneck C., Plant T.D., and Schultz G. From worm to man: Three subfamilies of TRP channels. Trends Neurosci. 23 (2000) 159-166
    • (2000) Trends Neurosci. , vol.23 , pp. 159-166
    • Harteneck, C.1    Plant, T.D.2    Schultz, G.3
  • 134
    • 0028032390 scopus 로고
    • Placental transport of nutrients to the fetus
    • Hay Jr. W.W. Placental transport of nutrients to the fetus. Horm. Res. 42 (1994) 215-222
    • (1994) Horm. Res. , vol.42 , pp. 215-222
    • Hay Jr., W.W.1
  • 135
    • 0029927951 scopus 로고    scopus 로고
    • Disparate effects of calcium antagonists on renal microcirculation
    • Hayashi K., Nagahama T., Oka K., Epstein M., and Saruta T. Disparate effects of calcium antagonists on renal microcirculation. Hypertens. Res. 19 (1996) 31-36
    • (1996) Hypertens. Res. , vol.19 , pp. 31-36
    • Hayashi, K.1    Nagahama, T.2    Oka, K.3    Epstein, M.4    Saruta, T.5
  • 136
    • 28044448714 scopus 로고    scopus 로고
    • Pathophysiological significance of T-type Ca(2+) channels: Role of T-type Ca(2+) channels in renal microcirculation
    • Hayashi K., Wakino S., Homma K., Sugano N., and Saruta T. Pathophysiological significance of T-type Ca(2+) channels: Role of T-type Ca(2+) channels in renal microcirculation. J. Pharmacol. Sci. 99 (2005) 221-227
    • (2005) J. Pharmacol. Sci. , vol.99 , pp. 221-227
    • Hayashi, K.1    Wakino, S.2    Homma, K.3    Sugano, N.4    Saruta, T.5
  • 138
    • 0032588099 scopus 로고    scopus 로고
    • Ca2+-binding S100 proteins in the central nervous system
    • Heizmann C.W. Ca2+-binding S100 proteins in the central nervous system. Neurochem. Res. 24 (1999) 1097-1100
    • (1999) Neurochem. Res. , vol.24 , pp. 1097-1100
    • Heizmann, C.W.1
  • 139
    • 0025978546 scopus 로고
    • Intracellular calcium-binding proteins: More sites than insights
    • Heizmann C.W., and Hunziker W. Intracellular calcium-binding proteins: More sites than insights. Trends. Biochem. Sci. 16 (1991) 98-103
    • (1991) Trends. Biochem. Sci. , vol.16 , pp. 98-103
    • Heizmann, C.W.1    Hunziker, W.2
  • 140
    • 0014904364 scopus 로고
    • Microvill osities on the surface of chorionic villi of the human placenta
    • Herbst R., and Multier A.M. Microvill osities on the surface of chorionic villi of the human placenta. Gynecol. Obstet. (Paris) 69 Suppl. 5 (1970) 609+
    • (1970) Gynecol. Obstet. (Paris) , vol.69 , Issue.SUPPL. 5
    • Herbst, R.1    Multier, A.M.2
  • 141
    • 0016633403 scopus 로고
    • Vitamin D-dependent calcium-binding protein from rat kidney
    • Hermsdorf C.L., and Bronner F. Vitamin D-dependent calcium-binding protein from rat kidney. Biochim. Biophys. Acta 379 (1975) 553-561
    • (1975) Biochim. Biophys. Acta , vol.379 , pp. 553-561
    • Hermsdorf, C.L.1    Bronner, F.2
  • 142
    • 0032126724 scopus 로고    scopus 로고
    • Placental 57-kDa Ca(2+)-binding protein: Regulation of expression and function in trophoblast calcium transport
    • Hershberger M.E., and Tuan R.S. Placental 57-kDa Ca(2+)-binding protein: Regulation of expression and function in trophoblast calcium transport. Dev. Biol. 199 (1998) 80-92
    • (1998) Dev. Biol. , vol.199 , pp. 80-92
    • Hershberger, M.E.1    Tuan, R.S.2
  • 143
    • 0033231413 scopus 로고    scopus 로고
    • Functional analysis of placental 57-kDa Ca(2+)-binding protein: Overexpression and downregulation in a trophoblastic cell line
    • Hershberger M.E., and Tuan R.S. Functional analysis of placental 57-kDa Ca(2+)-binding protein: Overexpression and downregulation in a trophoblastic cell line. Dev. Biol. 215 (1999) 107-117
    • (1999) Dev. Biol. , vol.215 , pp. 107-117
    • Hershberger, M.E.1    Tuan, R.S.2
  • 145
    • 0028116583 scopus 로고
    • Cloning and expression of isoform 2 of the human plasma membrane Ca2+ ATPase. Functional properties of the enzyme and its splicing products
    • Hilfiker H., Guerini D., and Carafoli E. Cloning and expression of isoform 2 of the human plasma membrane Ca2+ ATPase. Functional properties of the enzyme and its splicing products. J. Biol. Chem. 269 (1994) 26178-26183
    • (1994) J. Biol. Chem. , vol.269 , pp. 26178-26183
    • Hilfiker, H.1    Guerini, D.2    Carafoli, E.3
  • 149
  • 150
    • 0036720339 scopus 로고    scopus 로고
    • Modulation of renal Ca2+ transport protein genes by dietary Ca2+ and 1,25-dihydroxyvitamin D3 in 25-hydroxyvitamin D3-1alpha-hydroxylase knockout mice
    • Hoenderop J.G., Dardenne O., Van Abel M., Van Der Kemp A.W., Van Os C.H., St -Arnaud R., and Bindels R.J. Modulation of renal Ca2+ transport protein genes by dietary Ca2+ and 1,25-dihydroxyvitamin D3 in 25-hydroxyvitamin D3-1alpha-hydroxylase knockout mice. FASEB J. 16 (2002) 1398-1406
    • (2002) FASEB J. , vol.16 , pp. 1398-1406
    • Hoenderop, J.G.1    Dardenne, O.2    Van Abel, M.3    Van Der Kemp, A.W.4    Van Os, C.H.5    St -Arnaud, R.6    Bindels, R.J.7
  • 151
    • 0036194384 scopus 로고    scopus 로고
    • Molecular mechanism of active Ca2+ reabsorption in the distal nephron
    • Hoenderop J.G., Nilius B., and Bindels R.J. Molecular mechanism of active Ca2+ reabsorption in the distal nephron. Annu. Rev. Physiol. 64 (2002) 529-549
    • (2002) Annu. Rev. Physiol. , vol.64 , pp. 529-549
    • Hoenderop, J.G.1    Nilius, B.2    Bindels, R.J.3
  • 152
    • 0037450768 scopus 로고    scopus 로고
    • Homo- and heterotetrameric architecture of the epithelial Ca2+ channels TRPV5 and TRPV6
    • Hoenderop J.G., Voets T., Hoefs S., Weidema F., Prenen J., Nilius B., and Bindels R.J. Homo- and heterotetrameric architecture of the epithelial Ca2+ channels TRPV5 and TRPV6. EMBO J. 22 (2003) 776-785
    • (2003) EMBO J. , vol.22 , pp. 776-785
    • Hoenderop, J.G.1    Voets, T.2    Hoefs, S.3    Weidema, F.4    Prenen, J.5    Nilius, B.6    Bindels, R.J.7
  • 153
    • 0037188517 scopus 로고    scopus 로고
    • Subunit composition of mammalian transient receptor potential channels in living cells
    • Hofmann T., Schaefer M., Schultz G., and Gudermann T. Subunit composition of mammalian transient receptor potential channels in living cells. Proc. Natl. Acad. Sci. USA 99 (2002) 7461-7466
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 7461-7466
    • Hofmann, T.1    Schaefer, M.2    Schultz, G.3    Gudermann, T.4
  • 154
    • 0345707679 scopus 로고    scopus 로고
    • Maternal-fetal transfer of endocrine disruptors in the induction of calbindin-D9k mRNA and protein during pregnancy in rat model
    • Hong E.J., Choi K.C., and Jeung E.B. Maternal-fetal transfer of endocrine disruptors in the induction of calbindin-D9k mRNA and protein during pregnancy in rat model. Mol. Cell. Endocrinol. 212 (2003) 63-72
    • (2003) Mol. Cell. Endocrinol. , vol.212 , pp. 63-72
    • Hong, E.J.1    Choi, K.C.2    Jeung, E.B.3
  • 155
    • 0029948937 scopus 로고    scopus 로고
    • Calcium homeostasis in pregnancy
    • Hosking D.J. Calcium homeostasis in pregnancy. Clin. Endocrinol. (Oxf.) 45 (1996) 1-6
    • (1996) Clin. Endocrinol. (Oxf.) , vol.45 , pp. 1-6
    • Hosking, D.J.1
  • 156
    • 0026594980 scopus 로고
    • Depletion of intracellular calcium stores activates a calcium current in mast cells
    • Hoth M., and Penner R. Depletion of intracellular calcium stores activates a calcium current in mast cells. Nature 355 (1992) 353-356
    • (1992) Nature , vol.355 , pp. 353-356
    • Hoth, M.1    Penner, R.2
  • 157
    • 0026524991 scopus 로고
    • Plasma membrane calcium pump expression in human placenta and small intestine
    • Howard A., Legon S., and Walters J.R. Plasma membrane calcium pump expression in human placenta and small intestine. Biochem. Biophys. Res. Commun. 183 (1992) 499-505
    • (1992) Biochem. Biophys. Res. Commun. , vol.183 , pp. 499-505
    • Howard, A.1    Legon, S.2    Walters, J.R.3
  • 158
    • 0032213510 scopus 로고    scopus 로고
    • Low-voltage-activated (T-type) calcium-channel genes identified
    • Huguenard J.R. Low-voltage-activated (T-type) calcium-channel genes identified. Trends Neurosci. 21 (1998) 451-452
    • (1998) Trends Neurosci. , vol.21 , pp. 451-452
    • Huguenard, J.R.1
  • 159
    • 0033048814 scopus 로고    scopus 로고
    • The apoptosis cascade3/4morphological and immunohistochemical methods for its visualization
    • Huppertz B., Frank H.G., and Kaufmann P. The apoptosis cascade3/4morphological and immunohistochemical methods for its visualization. Anat. Embryol. (Berl.) 200 (1999) 1-18
    • (1999) Anat. Embryol. (Berl.) , vol.200 , pp. 1-18
    • Huppertz, B.1    Frank, H.G.2    Kaufmann, P.3
  • 160
    • 0026748482 scopus 로고
    • Mineral transport across the placenta
    • Husain S.M., and Mughal M.Z. Mineral transport across the placenta. Arch. Dis. Child 67 (1992) 874-878
    • (1992) Arch. Dis. Child , vol.67 , pp. 874-878
    • Husain, S.M.1    Mughal, M.Z.2
  • 161
    • 0028084911 scopus 로고
    • Effect of diabetes mellitus on maternofetal flux of calcium and magnesium and calbindin9K mRNA expression in rat placenta
    • Husain S.M., Birdsey T.J., Glazier J.D., Mughal M.Z., Garland H.O., and Sibley C.P. Effect of diabetes mellitus on maternofetal flux of calcium and magnesium and calbindin9K mRNA expression in rat placenta. Pediatr. Res. 35 (1994) 376-381
    • (1994) Pediatr. Res. , vol.35 , pp. 376-381
    • Husain, S.M.1    Birdsey, T.J.2    Glazier, J.D.3    Mughal, M.Z.4    Garland, H.O.5    Sibley, C.P.6
  • 162
    • 0347060616 scopus 로고
    • The maternotrophoblastics interface: Uteroplacental blood flow
    • Barnea E.R., Hustin J., and Jauniaux E. (Eds), Springer-Verlag, Berlin
    • Hustin J. The maternotrophoblastics interface: Uteroplacental blood flow. In: Barnea E.R., Hustin J., and Jauniaux E. (Eds). "The First Twelve Weeks of Pregnancy" (1992), Springer-Verlag, Berlin 97-110
    • (1992) "The First Twelve Weeks of Pregnancy" , pp. 97-110
    • Hustin, J.1
  • 163
    • 0025202599 scopus 로고
    • Histological study of the materno-embryonic interface in spontaneous abortion
    • Hustin J., Jauniaux E., and Schaaps J.P. Histological study of the materno-embryonic interface in spontaneous abortion. Placenta 11 (1990) 477-486
    • (1990) Placenta , vol.11 , pp. 477-486
    • Hustin, J.1    Jauniaux, E.2    Schaaps, J.P.3
  • 164
    • 0035964811 scopus 로고    scopus 로고
    • Polyvalent cation-sensing mechanism increased Na(+)-independent Mg(2+) transport in renal epithelial cells
    • Ikari A., Nakajima K., Kawano K., and Suketa Y. Polyvalent cation-sensing mechanism increased Na(+)-independent Mg(2+) transport in renal epithelial cells. Biochem. Biophys. Res. Commun. 287 (2001) 671-674
    • (2001) Biochem. Biophys. Res. Commun. , vol.287 , pp. 671-674
    • Ikari, A.1    Nakajima, K.2    Kawano, K.3    Suketa, Y.4
  • 165
    • 0033575899 scopus 로고    scopus 로고
    • Human S100A11 exhibits differential steady-state RNA levels in various tissues and a distinct subcellular localization
    • Inada H., Naka M., Tanaka T., Davey G.E., and Heizmann C.W. Human S100A11 exhibits differential steady-state RNA levels in various tissues and a distinct subcellular localization. Biochem. Biophys. Res. Commun. 263 (1999) 135-138
    • (1999) Biochem. Biophys. Res. Commun. , vol.263 , pp. 135-138
    • Inada, H.1    Naka, M.2    Tanaka, T.3    Davey, G.E.4    Heizmann, C.W.5
  • 166
    • 0027323865 scopus 로고
    • 22-Oxacalcitriol, a noncalcemic analogue of calcitriol, suppresses both cell proliferation and parathyroid hormone-related peptide gene expression in human T cell lymphotrophic virus, type I-infected T cells
    • Inoue D., Matsumoto T., Ogata E., and Ikeda K. 22-Oxacalcitriol, a noncalcemic analogue of calcitriol, suppresses both cell proliferation and parathyroid hormone-related peptide gene expression in human T cell lymphotrophic virus, type I-infected T cells. J. Biol. Chem. 268 (1993) 16730-16736
    • (1993) J. Biol. Chem. , vol.268 , pp. 16730-16736
    • Inoue, D.1    Matsumoto, T.2    Ogata, E.3    Ikeda, K.4
  • 167
    • 0015086181 scopus 로고
    • A study of synthesis and secretion of HCG in trophoblastic culture
    • Ishimaru T. A study of synthesis and secretion of HCG in trophoblastic culture. Acta Obstet. Gynaecol. Jpn. 18 (1971) 172-180
    • (1971) Acta Obstet. Gynaecol. Jpn. , vol.18 , pp. 172-180
    • Ishimaru, T.1
  • 168
    • 0017857916 scopus 로고
    • The amino-acid sequence of S-100 protein (PAP I-b protein) and its relation to the calcium-binding proteins
    • Isobe T., and Okuyama T. The amino-acid sequence of S-100 protein (PAP I-b protein) and its relation to the calcium-binding proteins. Eur. J. Biochem. 89 (1978) 379-388
    • (1978) Eur. J. Biochem. , vol.89 , pp. 379-388
    • Isobe, T.1    Okuyama, T.2
  • 169
    • 0031816393 scopus 로고    scopus 로고
    • Differential inhibition of Na+/Ca2+ exchanger isoforms by divalent cations and isothiourea derivative
    • Iwamoto T., and Shigekawa M. Differential inhibition of Na+/Ca2+ exchanger isoforms by divalent cations and isothiourea derivative. Am. J. Physiol. 275 (1998) C423-C430
    • (1998) Am. J. Physiol. , vol.275
    • Iwamoto, T.1    Shigekawa, M.2
  • 170
    • 0023664898 scopus 로고
    • A growth-related mRNA in cultured mouse cells encodes a placental calcium binding protein
    • Jackson-Grusby L.L., Swiergiel J., and Linzer D.I. A growth-related mRNA in cultured mouse cells encodes a placental calcium binding protein. Nucleic Acids Res. 15 (1987) 6677-6690
    • (1987) Nucleic Acids Res. , vol.15 , pp. 6677-6690
    • Jackson-Grusby, L.L.1    Swiergiel, J.2    Linzer, D.I.3
  • 171
    • 0028921581 scopus 로고
    • Calmodulin-binding domains: Just two faced or multi-faceted?
    • James P., Vorherr T., and Carafoli E. Calmodulin-binding domains: Just two faced or multi-faceted?. Trends Biochem. Sci. 20 (1995) 38-42
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 38-42
    • James, P.1    Vorherr, T.2    Carafoli, E.3
  • 173
  • 174
    • 22244478077 scopus 로고    scopus 로고
    • Structure and physiologic function of the low-density lipoprotein receptor
    • Jeon H., and Blacklow S.C. Structure and physiologic function of the low-density lipoprotein receptor. Annu. Rev. Biochem. 74 (2005) 535-562
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 535-562
    • Jeon, H.1    Blacklow, S.C.2
  • 175
    • 0026671206 scopus 로고
    • Cloning of the porcine calbindin-D9k complementary deoxyribonucleic acid by anchored polymerase chain reaction technique
    • Jeung E.B., Krisinger J., Dann J.L., and Leung P.C. Cloning of the porcine calbindin-D9k complementary deoxyribonucleic acid by anchored polymerase chain reaction technique. Biol. Reprod. 47 (1992) 503-508
    • (1992) Biol. Reprod. , vol.47 , pp. 503-508
    • Jeung, E.B.1    Krisinger, J.2    Dann, J.L.3    Leung, P.C.4
  • 176
    • 0026695055 scopus 로고
    • Molecular cloning of the full-length cDNA encoding the human calbindin-D9k
    • Jeung E.B., Krisinger J., Dann J.L., and Leung P.C. Molecular cloning of the full-length cDNA encoding the human calbindin-D9k. FEBS Lett. 307 (1992) 224-228
    • (1992) FEBS Lett. , vol.307 , pp. 224-228
    • Jeung, E.B.1    Krisinger, J.2    Dann, J.L.3    Leung, P.C.4
  • 177
    • 0028180374 scopus 로고
    • The human calbindin-D9k gene. Complete structure and implications on steroid hormone regulation
    • Jeung E.B., Leung P.C., and Krisinger J. The human calbindin-D9k gene. Complete structure and implications on steroid hormone regulation. J. Mol. Biol. 235 (1994) 1231-1238
    • (1994) J. Mol. Biol. , vol.235 , pp. 1231-1238
    • Jeung, E.B.1    Leung, P.C.2    Krisinger, J.3
  • 178
    • 0344875984 scopus 로고    scopus 로고
    • Characterization of the tissue-specific expression of the s100P gene which encodes an EF-hand Ca2+-binding protein
    • Jin G., Wang S., Hu X., Jing Z., Chen J., Ying K., Xie Y., and Mao Y. Characterization of the tissue-specific expression of the s100P gene which encodes an EF-hand Ca2+-binding protein. Mol. Biol. Rep. 30 (2003) 243-248
    • (2003) Mol. Biol. Rep. , vol.30 , pp. 243-248
    • Jin, G.1    Wang, S.2    Hu, X.3    Jing, Z.4    Chen, J.5    Ying, K.6    Xie, Y.7    Mao, Y.8
  • 179
    • 0032918344 scopus 로고    scopus 로고
    • Maternal smoking during pregnancy, growth, and bone mass in prepubertal children
    • Jones G., Riley M., and Dwyer T. Maternal smoking during pregnancy, growth, and bone mass in prepubertal children. J. Bone Miner. Res. 14 (1999) 146-151
    • (1999) J. Bone Miner. Res. , vol.14 , pp. 146-151
    • Jones, G.1    Riley, M.2    Dwyer, T.3
  • 180
    • 0029845505 scopus 로고    scopus 로고
    • Increased content of annexin II (p36) and p11 in human placenta brush-border membrane vesicles during syncytiotrophoblast maturation and differentiation
    • Kaczan-Bourgois D., Salles J.P., Hullin F., Fauvel J., Moisand A., Duga-Neulat I., Berrebi A., Campistron G., and Chap H. Increased content of annexin II (p36) and p11 in human placenta brush-border membrane vesicles during syncytiotrophoblast maturation and differentiation. Placenta 17 (1996) 669-676
    • (1996) Placenta , vol.17 , pp. 669-676
    • Kaczan-Bourgois, D.1    Salles, J.P.2    Hullin, F.3    Fauvel, J.4    Moisand, A.5    Duga-Neulat, I.6    Berrebi, A.7    Campistron, G.8    Chap, H.9
  • 181
    • 0028170227 scopus 로고
    • Na+/Ca2+ exchange, Ca2+ binding, and electrogenic Ca2+ transport in plasma membranes of human placental syncytiotrophoblast
    • Kamath S.G., and Smith C.H. Na+/Ca2+ exchange, Ca2+ binding, and electrogenic Ca2+ transport in plasma membranes of human placental syncytiotrophoblast. Pediatr. Res. 36 (1994) 461-467
    • (1994) Pediatr. Res. , vol.36 , pp. 461-467
    • Kamath, S.G.1    Smith, C.H.2
  • 182
    • 0030090294 scopus 로고    scopus 로고
    • Structure, function and expression of Ca2+ channels
    • Kameyama A., and Kameyama M. Structure, function and expression of Ca2+ channels. Nippon Rinsho 54 (1996) 672-678
    • (1996) Nippon Rinsho , vol.54 , pp. 672-678
    • Kameyama, A.1    Kameyama, M.2
  • 183
    • 0029833887 scopus 로고    scopus 로고
    • Parathyroid hormone related peptide mRNA expression during murine postimplantation development: Evidence for involvement in multiple differentiation processes
    • Karperien M., Lanser P., de Laat S.W., Boonstra J., and Defize L.H. Parathyroid hormone related peptide mRNA expression during murine postimplantation development: Evidence for involvement in multiple differentiation processes. Int. J. Dev. Biol. 40 (1996) 599-608
    • (1996) Int. J. Dev. Biol. , vol.40 , pp. 599-608
    • Karperien, M.1    Lanser, P.2    de Laat, S.W.3    Boonstra, J.4    Defize, L.H.5
  • 184
    • 0005322689 scopus 로고    scopus 로고
    • Placental development
    • Polin R.A., and Fox W.W. (Eds), W. B. Saunders, Philadelphia, PA
    • Kaufmann P., and Scheffen I. Placental development. In: Polin R.A., and Fox W.W. (Eds). "Fetal and Neonatal Physiology" Vol. 1 (1998), W. B. Saunders, Philadelphia, PA
    • (1998) "Fetal and Neonatal Physiology" , vol.1
    • Kaufmann, P.1    Scheffen, I.2
  • 185
    • 0032454584 scopus 로고    scopus 로고
    • Classification and evolution of EF-hand proteins
    • Kawasaki H., Nakayama S., and Kretsinger R.H. Classification and evolution of EF-hand proteins. Biometals 11 (1998) 277-295
    • (1998) Biometals , vol.11 , pp. 277-295
    • Kawasaki, H.1    Nakayama, S.2    Kretsinger, R.H.3
  • 186
    • 0029911275 scopus 로고    scopus 로고
    • Effect of maternal ethanol consumption on maternal and fetal calcium metabolism
    • Keiver K., Herbert L., and Weinberg J. Effect of maternal ethanol consumption on maternal and fetal calcium metabolism. Alcohol Clin. Exp. Res. 20 (1996) 1305-1312
    • (1996) Alcohol Clin. Exp. Res. , vol.20 , pp. 1305-1312
    • Keiver, K.1    Herbert, L.2    Weinberg, J.3
  • 187
    • 0031459011 scopus 로고    scopus 로고
    • Effect of prenatal ethanol exposure on fetal calcium metabolism
    • Keiver K., Ellis L., Anzarut A., and Weinberg J. Effect of prenatal ethanol exposure on fetal calcium metabolism. Alcohol Clin. Exp. Res. 21 (1997) 1612-1618
    • (1997) Alcohol Clin. Exp. Res. , vol.21 , pp. 1612-1618
    • Keiver, K.1    Ellis, L.2    Anzarut, A.3    Weinberg, J.4
  • 188
    • 0034573075 scopus 로고    scopus 로고
    • Identification of the calcium binding sites in translationally controlled tumor protein
    • Kim M., Jung Y., Lee K., and Kim C. Identification of the calcium binding sites in translationally controlled tumor protein. Arch. Pharm. Res. 23 (2000) 633-636
    • (2000) Arch. Pharm. Res. , vol.23 , pp. 633-636
    • Kim, M.1    Jung, Y.2    Lee, K.3    Kim, C.4
  • 189
    • 33745248179 scopus 로고    scopus 로고
    • Placental development in normal and IUGR pregnancies
    • Kingdom J.C.P., Jauniaux E., and O'Brien S. (Eds), RCOG Press, London
    • Kingdom J.C.P., and Kaufmann P.H.U. Placental development in normal and IUGR pregnancies. In: Kingdom J.C.P., Jauniaux E., and O'Brien S. (Eds). "The Placenta: Basic Science and Clinical Practice" (2000), RCOG Press, London 375
    • (2000) "The Placenta: Basic Science and Clinical Practice" , pp. 375
    • Kingdom, J.C.P.1    Kaufmann, P.H.U.2
  • 190
    • 0033179431 scopus 로고    scopus 로고
    • Fatty acids, diacylglycerol, Ins(1,4,5)P3 receptors and Ca2+ influx
    • Kiselyov K., and Muallem S. Fatty acids, diacylglycerol, Ins(1,4,5)P3 receptors and Ca2+ influx. Trends Neurosci. 22 (1999) 334-337
    • (1999) Trends Neurosci. , vol.22 , pp. 334-337
    • Kiselyov, K.1    Muallem, S.2
  • 195
    • 0033233479 scopus 로고    scopus 로고
    • Comparison of the Ca2+ currents induced by expression of three cloned alpha1 subunits, alpha1G, alpha1H and alpha1I, of low-voltage-activated T-type Ca2+ channels
    • Klockner U., Lee J.H., Cribbs L.L., Daud A., Hescheler J., Pereverzev A., Perez-Reyes E., and Schneider T. Comparison of the Ca2+ currents induced by expression of three cloned alpha1 subunits, alpha1G, alpha1H and alpha1I, of low-voltage-activated T-type Ca2+ channels. Eur. J. Neurosci. 11 (1999) 4171-4178
    • (1999) Eur. J. Neurosci. , vol.11 , pp. 4171-4178
    • Klockner, U.1    Lee, J.H.2    Cribbs, L.L.3    Daud, A.4    Hescheler, J.5    Pereverzev, A.6    Perez-Reyes, E.7    Schneider, T.8
  • 196
    • 0027062745 scopus 로고
    • Expression of the Na-Ca exchanger in diverse tissues: A study using the cloned human cardiac Na-Ca exchanger
    • Kofuji P., Hadley R.W., Kieval R.S., Lederer W.J., and Schulze D.H. Expression of the Na-Ca exchanger in diverse tissues: A study using the cloned human cardiac Na-Ca exchanger. Am. J. Physiol. 263 (1992) C1241-C1249
    • (1992) Am. J. Physiol. , vol.263
    • Kofuji, P.1    Hadley, R.W.2    Kieval, R.S.3    Lederer, W.J.4    Schulze, D.H.5
  • 197
    • 0033536038 scopus 로고    scopus 로고
    • Molecular cloning, characterization, and promoter analysis of the human 25-hydroxyvitamin D3-1alpha-hydroxylase gene
    • Kong X.F., Zhu X.H., Pei Y.L., Jackson D.M., and Holick M.F. Molecular cloning, characterization, and promoter analysis of the human 25-hydroxyvitamin D3-1alpha-hydroxylase gene. Proc. Natl. Acad. Sci. USA 96 (1999) 6988-6993
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 6988-6993
    • Kong, X.F.1    Zhu, X.H.2    Pei, Y.L.3    Jackson, D.M.4    Holick, M.F.5
  • 198
    • 0035349728 scopus 로고    scopus 로고
    • Targeted inactivation of the sodium-calcium exchanger (Ncx1) results in the lack of a heartbeat and abnormal myofibrillar organization
    • Koushik S.V., Wang J., Rogers R., Moskophidis D., Lambert N.A., Creazzo T.L., and Conway S.J. Targeted inactivation of the sodium-calcium exchanger (Ncx1) results in the lack of a heartbeat and abnormal myofibrillar organization. FASEB J. 15 (2001) 1209-1211
    • (2001) FASEB J. , vol.15 , pp. 1209-1211
    • Koushik, S.V.1    Wang, J.2    Rogers, R.3    Moskophidis, D.4    Lambert, N.A.5    Creazzo, T.L.6    Conway, S.J.7
  • 199
    • 33746006622 scopus 로고
    • PTHrP gene knock out mouse have placental calcium transport severely impaired
    • Kovacs C.S. PTHrP gene knock out mouse have placental calcium transport severely impaired. J. Bone Miner. Res 10 (1995) 73
    • (1995) J. Bone Miner. Res , vol.10 , pp. 73
    • Kovacs, C.S.1
  • 200
    • 0031471679 scopus 로고    scopus 로고
    • Maternal-fetal calcium and bone metabolism during pregnancy, puerperium, and lactation
    • Kovacs C.S., and Kronenberg H.M. Maternal-fetal calcium and bone metabolism during pregnancy, puerperium, and lactation. Endocr. Rev. 18 (1997) 832-872
    • (1997) Endocr. Rev. , vol.18 , pp. 832-872
    • Kovacs, C.S.1    Kronenberg, H.M.2
  • 201
    • 0030465408 scopus 로고    scopus 로고
    • Parathyroid hormone-related peptide (PTHrP) regulates fetal-placental calcium transport through a receptor distinct from the PTH/PTHrP receptor
    • Kovacs C.S., Lanske B., Hunzelman J.L., Guo J., Karaplis A.C., and Kronenberg H.M. Parathyroid hormone-related peptide (PTHrP) regulates fetal-placental calcium transport through a receptor distinct from the PTH/PTHrP receptor. Proc. Natl. Acad. Sci. USA 93 (1996) 15233-15238
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 15233-15238
    • Kovacs, C.S.1    Lanske, B.2    Hunzelman, J.L.3    Guo, J.4    Karaplis, A.C.5    Kronenberg, H.M.6
  • 204
    • 0034752132 scopus 로고    scopus 로고
    • PTH regulates fetal blood calcium and skeletal mineralization independently of PTHrP
    • Kovacs C.S., Chafe L.L., Fudge N.J., Friel J.K., and Manley N.R. PTH regulates fetal blood calcium and skeletal mineralization independently of PTHrP. Endocrinology 142 (2001) 4983-4993
    • (2001) Endocrinology , vol.142 , pp. 4983-4993
    • Kovacs, C.S.1    Chafe, L.L.2    Fudge, N.J.3    Friel, J.K.4    Manley, N.R.5
  • 206
    • 21044451621 scopus 로고    scopus 로고
    • The vitamin D receptor is not required for fetal mineral homeostasis or for the regulation of placental calcium transfer in mice
    • Kovacs C.S., Woodland M.L., Fudge N.J., and Friel J.K. The vitamin D receptor is not required for fetal mineral homeostasis or for the regulation of placental calcium transfer in mice. Am. J. Physiol. Endocrinol. Metab. 289 (2005) E133-E144
    • (2005) Am. J. Physiol. Endocrinol. Metab. , vol.289
    • Kovacs, C.S.1    Woodland, M.L.2    Fudge, N.J.3    Friel, J.K.4
  • 208
    • 0018816959 scopus 로고
    • Structure and evolution of calcium-modulated proteins
    • Kretsinger R.H. Structure and evolution of calcium-modulated proteins. CRC Crit. Rev. Biochem. 8 (1980) 119-174
    • (1980) CRC Crit. Rev. Biochem. , vol.8 , pp. 119-174
    • Kretsinger, R.H.1
  • 209
    • 0020024904 scopus 로고
    • Placenta as a source of 'brain' and 'pituitary' hormones
    • Krieger D.T. Placenta as a source of 'brain' and 'pituitary' hormones. Biol. Reprod. 26 (1982) 55-71
    • (1982) Biol. Reprod. , vol.26 , pp. 55-71
    • Krieger, D.T.1
  • 210
    • 0027338439 scopus 로고
    • Calbindin-D9k gene expression during the perinatal period in the rat: Correlation to estrogen receptor expression in uterus
    • Krisinger J., Dann J.L., Applegarth O., Currie W.D., Jeung E.B., Staun M., and Leung P.C. Calbindin-D9k gene expression during the perinatal period in the rat: Correlation to estrogen receptor expression in uterus. Mol. Cell. Endocrinol. 97 (1993) 61-69
    • (1993) Mol. Cell. Endocrinol. , vol.97 , pp. 61-69
    • Krisinger, J.1    Dann, J.L.2    Applegarth, O.3    Currie, W.D.4    Jeung, E.B.5    Staun, M.6    Leung, P.C.7
  • 211
    • 17444366177 scopus 로고    scopus 로고
    • S100A10, annexin A2, and annexin a2 heterotetramer as candidate plasminogen receptors
    • Kwon M., MacLeod T.J., Zhang Y., and Waisman D.M. S100A10, annexin A2, and annexin a2 heterotetramer as candidate plasminogen receptors. Front. Biosci. 10 (2005) 300-325
    • (2005) Front. Biosci. , vol.10 , pp. 300-325
    • Kwon, M.1    MacLeod, T.J.2    Zhang, Y.3    Waisman, D.M.4
  • 212
    • 0026699628 scopus 로고
    • Purification and structural analysis of a murine chemotactic cytokine (CP-10) with sequence homology to S100 proteins
    • Lackmann M., Cornish C.J., Simpson R.J., Moritz R.L., and Geczy C.L. Purification and structural analysis of a murine chemotactic cytokine (CP-10) with sequence homology to S100 proteins. J. Biol. Chem. 267 (1992) 7499-7504
    • (1992) J. Biol. Chem. , vol.267 , pp. 7499-7504
    • Lackmann, M.1    Cornish, C.J.2    Simpson, R.J.3    Moritz, R.L.4    Geczy, C.L.5
  • 214
    • 0025851350 scopus 로고
    • Characterization of calcium transport by basal plasma membranes from human placental syncytiotrophoblast
    • Lafond J., Leclerc M., and Brunette M.G. Characterization of calcium transport by basal plasma membranes from human placental syncytiotrophoblast. J. Cell Physiol. 148 (1991) 17-23
    • (1991) J. Cell Physiol. , vol.148 , pp. 17-23
    • Lafond, J.1    Leclerc, M.2    Brunette, M.G.3
  • 215
    • 0028151336 scopus 로고
    • Linoleic acid transport by human placental syncytiotrophoblast membranes
    • Lafond J., Simoneau L., Savard R., and Gagnon M.C. Linoleic acid transport by human placental syncytiotrophoblast membranes. Eur. J. Biochem. 226 (1994) 707-713
    • (1994) Eur. J. Biochem. , vol.226 , pp. 707-713
    • Lafond, J.1    Simoneau, L.2    Savard, R.3    Gagnon, M.C.4
  • 216
    • 0033824458 scopus 로고    scopus 로고
    • Implication of ATP and sodium in arachidonic acid incorporation by placental syncytiotrophoblast brush border and basal plasma membranes in the human
    • Lafond J., Moukdar F., Rioux A., Ech-Chadli H., Brissette L., Robidoux J., Masse A., and Simoneau L. Implication of ATP and sodium in arachidonic acid incorporation by placental syncytiotrophoblast brush border and basal plasma membranes in the human. Placenta 21 (2000) 661-669
    • (2000) Placenta , vol.21 , pp. 661-669
    • Lafond, J.1    Moukdar, F.2    Rioux, A.3    Ech-Chadli, H.4    Brissette, L.5    Robidoux, J.6    Masse, A.7    Simoneau, L.8
  • 217
    • 0029845504 scopus 로고    scopus 로고
    • Growth factors, proteases and protease inhibitors in the maternal-fetal dialogue
    • Lala P.K., and Hamilton G.S. Growth factors, proteases and protease inhibitors in the maternal-fetal dialogue. Placenta 17 (1996) 545-555
    • (1996) Placenta , vol.17 , pp. 545-555
    • Lala, P.K.1    Hamilton, G.S.2
  • 218
    • 0032795085 scopus 로고    scopus 로고
    • Nickel block of three cloned T-type calcium channels: Low concentrations selectively block alpha1H
    • Lee J.H., Gomora J.C., Cribbs L.L., and Perez-Reyes E. Nickel block of three cloned T-type calcium channels: Low concentrations selectively block alpha1H. Biophys. J. 77 (1999) 3034-3042
    • (1999) Biophys. J. , vol.77 , pp. 3034-3042
    • Lee, J.H.1    Gomora, J.C.2    Cribbs, L.L.3    Perez-Reyes, E.4
  • 220
    • 0028030681 scopus 로고
    • Placental structure: In a comparative aspect
    • Leiser R., and Kaufmann P. Placental structure: In a comparative aspect. Exp. Clin. Endocrinol. 102 (1994) 122-134
    • (1994) Exp. Clin. Endocrinol. , vol.102 , pp. 122-134
    • Leiser, R.1    Kaufmann, P.2
  • 221
    • 0019436236 scopus 로고
    • Immunocytological evidence for parathyroid hormone in human fetal parathyroid glands
    • Leroyer-Alizon E., David L., Anast C.S., and Dubois P.M. Immunocytological evidence for parathyroid hormone in human fetal parathyroid glands. J. Clin. Endocrinol. Metab. 52 (1981) 513-516
    • (1981) J. Clin. Endocrinol. Metab. , vol.52 , pp. 513-516
    • Leroyer-Alizon, E.1    David, L.2    Anast, C.S.3    Dubois, P.M.4
  • 222
    • 0028038204 scopus 로고
    • Identification of the high affinity Ca(2+)-binding domain of the cardiac Na(+)-Ca2+ exchanger
    • Levitsky D.O., Nicoll D.A., and Philipson K.D. Identification of the high affinity Ca(2+)-binding domain of the cardiac Na(+)-Ca2+ exchanger. J. Biol. Chem. 269 (1994) 22847-22852
    • (1994) J. Biol. Chem. , vol.269 , pp. 22847-22852
    • Levitsky, D.O.1    Nicoll, D.A.2    Philipson, K.D.3
  • 223
    • 0027954370 scopus 로고
    • Calbindin-D9k gene expression in the uterus: Study of the two messenger ribonucleic acid species and analysis of an imperfect estrogen-responsive element
    • L'Horset F., Blin C., Colnot S., Lambert M., Thomasset M., and Perret C. Calbindin-D9k gene expression in the uterus: Study of the two messenger ribonucleic acid species and analysis of an imperfect estrogen-responsive element. Endocrinology 134 (1994) 11-18
    • (1994) Endocrinology , vol.134 , pp. 11-18
    • L'Horset, F.1    Blin, C.2    Colnot, S.3    Lambert, M.4    Thomasset, M.5    Perret, C.6
  • 224
    • 0035861647 scopus 로고    scopus 로고
    • Characterization of fortilin, a novel antiapoptotic protein
    • Li F., Zhang D., and Fujise K. Characterization of fortilin, a novel antiapoptotic protein. J. Biol. Chem. 276 (2001) 47542-47549
    • (2001) J. Biol. Chem. , vol.276 , pp. 47542-47549
    • Li, F.1    Zhang, D.2    Fujise, K.3
  • 225
    • 0025819897 scopus 로고
    • Differential regulation by 1,25-dihydroxyvitamin D3 of calbindin-D9k and calbindin-D28k gene expression in mouse kidney
    • Li H., and Christakos S. Differential regulation by 1,25-dihydroxyvitamin D3 of calbindin-D9k and calbindin-D28k gene expression in mouse kidney. Endocrinology 128 (1991) 2844-2852
    • (1991) Endocrinology , vol.128 , pp. 2844-2852
    • Li, H.1    Christakos, S.2
  • 227
    • 0034830518 scopus 로고    scopus 로고
    • Effects of vitamin D receptor inactivation on the expression of calbindins and calcium metabolism
    • Li Y.C., Bolt M.J., Cao L.P., and Sitrin M.D. Effects of vitamin D receptor inactivation on the expression of calbindins and calcium metabolism. Am. J. Physiol. Endocrinol. Metab. 281 (2001) E558-E564
    • (2001) Am. J. Physiol. Endocrinol. Metab. , vol.281
    • Li, Y.C.1    Bolt, M.J.2    Cao, L.P.3    Sitrin, M.D.4
  • 228
    • 3042594296 scopus 로고    scopus 로고
    • Vitamin D: A negative endocrine regulator of the renin-angiotensin system and blood pressure
    • Li Y.C., Qiao G., Uskokovic M., Xiang W., Zheng W., and Kong J. Vitamin D: A negative endocrine regulator of the renin-angiotensin system and blood pressure. J. Steroid Biochem. Mol. Biol. 89-90 (2004) 387-392
    • (2004) J. Steroid Biochem. Mol. Biol. , vol.89-90 , pp. 387-392
    • Li, Y.C.1    Qiao, G.2    Uskokovic, M.3    Xiang, W.4    Zheng, W.5    Kong, J.6
  • 231
    • 0031935069 scopus 로고    scopus 로고
    • Functional comparison of the three isoforms of the Na+/Ca2+ exchanger (NCX1, NCX2, NCX3)
    • Linck B., Qiu Z., He Z., Tong Q., Hilgemann D.W., and Philipson K.D. Functional comparison of the three isoforms of the Na+/Ca2+ exchanger (NCX1, NCX2, NCX3). Am. J. Physiol. 274 (1998) C415-C423
    • (1998) Am. J. Physiol. , vol.274
    • Linck, B.1    Qiu, Z.2    He, Z.3    Tong, Q.4    Hilgemann, D.W.5    Philipson, K.D.6
  • 233
    • 0033811624 scopus 로고    scopus 로고
    • A homolog of voltage-gated Ca(2+) channels stimulated by depletion of secretory Ca(2+) in yeast
    • Locke E.G., Bonilla M., Liang L., Takita Y., and Cunningham K.W. A homolog of voltage-gated Ca(2+) channels stimulated by depletion of secretory Ca(2+) in yeast. Mol. Cell. Biol. 20 (2000) 6686-6694
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 6686-6694
    • Locke, E.G.1    Bonilla, M.2    Liang, L.3    Takita, Y.4    Cunningham, K.W.5
  • 235
    • 1842351052 scopus 로고    scopus 로고
    • Effect of physiologic perfusion-fixation on the morphometrically evaluated dimensions of the term placental cotyledon
    • Luckhardt M., Leiser R., Kingdom J., Malek A., Sager R., Kaisig C., and Schneider H. Effect of physiologic perfusion-fixation on the morphometrically evaluated dimensions of the term placental cotyledon. J. Soc. Gynecol. Investig. 3 (1996) 166-171
    • (1996) J. Soc. Gynecol. Investig. , vol.3 , pp. 166-171
    • Luckhardt, M.1    Leiser, R.2    Kingdom, J.3    Malek, A.4    Sager, R.5    Kaisig, C.6    Schneider, H.7
  • 236
    • 0034009899 scopus 로고    scopus 로고
    • Requirement of the inositol trisphosphate receptor for activation of store-operated Ca2+ channels
    • Ma H.T., Patterson R.L., van Rossum D.B., Birnbaumer L., Mikoshiba K., and Gill D.L. Requirement of the inositol trisphosphate receptor for activation of store-operated Ca2+ channels. Science 287 (2000) 1647-1651
    • (2000) Science , vol.287 , pp. 1647-1651
    • Ma, H.T.1    Patterson, R.L.2    van Rossum, D.B.3    Birnbaumer, L.4    Mikoshiba, K.5    Gill, D.L.6
  • 237
    • 0028982775 scopus 로고
    • Molecular identification of an IgE-dependent histamine-releasing factor
    • MacDonald S.M., Rafnar T., Langdon J., and Lichtenstein L.M. Molecular identification of an IgE-dependent histamine-releasing factor. Science 269 (1995) 688-690
    • (1995) Science , vol.269 , pp. 688-690
    • MacDonald, S.M.1    Rafnar, T.2    Langdon, J.3    Lichtenstein, L.M.4
  • 238
    • 0018765536 scopus 로고
    • Occurrence of a low-molecular-weight calcium-binding protein in neoplastic liver
    • MacManus J.P. Occurrence of a low-molecular-weight calcium-binding protein in neoplastic liver. Cancer Res. 39 (1979) 3000-3005
    • (1979) Cancer Res. , vol.39 , pp. 3000-3005
    • MacManus, J.P.1
  • 239
    • 0022262385 scopus 로고
    • The widely-distributed tumour protein, oncomodulin, is a normal constituent of human and rodent placentas
    • MacManus J.P., Brewer L.M., and Whitfield J.F. The widely-distributed tumour protein, oncomodulin, is a normal constituent of human and rodent placentas. Cancer Lett. 27 (1985) 145-151
    • (1985) Cancer Lett. , vol.27 , pp. 145-151
    • MacManus, J.P.1    Brewer, L.M.2    Whitfield, J.F.3
  • 241
    • 0030052283 scopus 로고    scopus 로고
    • Calcium-dependent binding of S100C to the N-terminal domain of annexin I
    • Mailliard W.S., Haigler H.T., and Schlaepfer D.D. Calcium-dependent binding of S100C to the N-terminal domain of annexin I. J. Biol. Chem. 271 (1996) 719-725
    • (1996) J. Biol. Chem. , vol.271 , pp. 719-725
    • Mailliard, W.S.1    Haigler, H.T.2    Schlaepfer, D.D.3
  • 242
    • 9744278277 scopus 로고    scopus 로고
    • Parathyroid hormone-related protein in preeclampsia: A linkage between maternal and fetal failures
    • Maioli E., Fortino V., and Pacini A. Parathyroid hormone-related protein in preeclampsia: A linkage between maternal and fetal failures. Biol. Reprod. 71 (2004) 1779-1784
    • (2004) Biol. Reprod. , vol.71 , pp. 1779-1784
    • Maioli, E.1    Fortino, V.2    Pacini, A.3
  • 243
    • 0034850713 scopus 로고    scopus 로고
    • Morphological variability and placental function
    • Malassine A. Morphological variability and placental function. Gynecol. Obstet. Fertil. 29 (2001) 489-496
    • (2001) Gynecol. Obstet. Fertil. , vol.29 , pp. 489-496
    • Malassine, A.1
  • 244
    • 0036822271 scopus 로고    scopus 로고
    • Hormones and human trophoblast differentiation: A review
    • Malassine A., and Cronier L. Hormones and human trophoblast differentiation: A review. Endocrine 19 (2002) 3-11
    • (2002) Endocrine , vol.19 , pp. 3-11
    • Malassine, A.1    Cronier, L.2
  • 245
    • 0031870090 scopus 로고    scopus 로고
    • Distinct subcellular localization of calcium binding S100 proteins in human smooth muscle cells and their relocation in response to rises in intracellular calcium
    • Mandinova A., Atar D., Schafer B.W., Spiess M., Aebi U., and Heizmann C.W. Distinct subcellular localization of calcium binding S100 proteins in human smooth muscle cells and their relocation in response to rises in intracellular calcium. J. Cell Sci. 111 Pt. 14 (1998) 2043-2054
    • (1998) J. Cell Sci. , vol.111 , Issue.PART 14 , pp. 2043-2054
    • Mandinova, A.1    Atar, D.2    Schafer, B.W.3    Spiess, M.4    Aebi, U.5    Heizmann, C.W.6
  • 246
    • 0037275686 scopus 로고    scopus 로고
    • Neurodevelopmental and cognitive assessment of children born growth restricted to mothers with and without preeclampsia
    • Many A., Fattal A., Leitner Y., Kupferminc M.J., Harel S., and Jaffa A. Neurodevelopmental and cognitive assessment of children born growth restricted to mothers with and without preeclampsia. Hypertens. Pregnancy 22 (2003) 25-29
    • (2003) Hypertens. Pregnancy , vol.22 , pp. 25-29
    • Many, A.1    Fattal, A.2    Leitner, Y.3    Kupferminc, M.J.4    Harel, S.5    Jaffa, A.6
  • 247
    • 4444371768 scopus 로고    scopus 로고
    • S100 proteins in mouse and man: From evolution to function and pathology (including an update of the nomenclature)
    • Marenholz I., Heizmann C.W., and Fritz G. S100 proteins in mouse and man: From evolution to function and pathology (including an update of the nomenclature). Biochem. Biophys. Res. Commun. 322 (2004) 1111-1122
    • (2004) Biochem. Biophys. Res. Commun. , vol.322 , pp. 1111-1122
    • Marenholz, I.1    Heizmann, C.W.2    Fritz, G.3
  • 249
    • 0027453984 scopus 로고
    • A prospective study of several potential biologic markers for early prediction of the development of preeclampsia
    • Masse J., Forest J.C., Moutquin J.M., Marcoux S., Brideau N.A., and Belanger M. A prospective study of several potential biologic markers for early prediction of the development of preeclampsia. Am. J. Obstet. Gynecol. 169 (1993) 501-508
    • (1993) Am. J. Obstet. Gynecol. , vol.169 , pp. 501-508
    • Masse, J.1    Forest, J.C.2    Moutquin, J.M.3    Marcoux, S.4    Brideau, N.A.5    Belanger, M.6
  • 251
    • 0028965584 scopus 로고
    • Regulation of the cardiac Na(+)-Ca2+ exchanger by Ca2+. Mutational analysis of the Ca(2+)-binding domain
    • Matsuoka S., Nicoll D.A., Hryshko L.V., Levitsky D.O., Weiss J.N., and Philipson K.D. Regulation of the cardiac Na(+)-Ca2+ exchanger by Ca2+. Mutational analysis of the Ca(2+)-binding domain. J. Gen. Physiol. 105 (1995) 403-420
    • (1995) J. Gen. Physiol. , vol.105 , pp. 403-420
    • Matsuoka, S.1    Nicoll, D.A.2    Hryshko, L.V.3    Levitsky, D.O.4    Weiss, J.N.5    Philipson, K.D.6
  • 253
    • 0028179048 scopus 로고
    • Ca2+ entry through L-type voltage-sensitive Ca2+ channels stimulates the release of human chorionic gonadotrophin and placental lactogen by placental explants
    • Meuris S., Polliotti B., Robyn C., and Lebrun P. Ca2+ entry through L-type voltage-sensitive Ca2+ channels stimulates the release of human chorionic gonadotrophin and placental lactogen by placental explants. Biochim. Biophys. Acta 1220 (1994) 101-106
    • (1994) Biochim. Biophys. Acta , vol.1220 , pp. 101-106
    • Meuris, S.1    Polliotti, B.2    Robyn, C.3    Lebrun, P.4
  • 254
    • 0036251217 scopus 로고    scopus 로고
    • Parathyroid hormone is essential for normal fetal bone formation
    • Miao D., He B., Karaplis A.C., and Goltzman D. Parathyroid hormone is essential for normal fetal bone formation. J. Clin. Invest. 109 (2002) 1173-1182
    • (2002) J. Clin. Invest. , vol.109 , pp. 1173-1182
    • Miao, D.1    He, B.2    Karaplis, A.C.3    Goltzman, D.4
  • 256
    • 0025311949 scopus 로고
    • Evolution of EF-hand calcium-modulated proteins. I. Relationships based on amino acid sequences
    • Moncrief N.D., Kretsinger R.H., and Goodman M. Evolution of EF-hand calcium-modulated proteins. I. Relationships based on amino acid sequences. J. Mol. Evol. 30 (1990) 522-562
    • (1990) J. Mol. Evol. , vol.30 , pp. 522-562
    • Moncrief, N.D.1    Kretsinger, R.H.2    Goodman, M.3
  • 258
    • 0034758366 scopus 로고    scopus 로고
    • Characteristics of calcium uptake by BeWo cells, a human trophoblast cell line
    • Moreau R., Simoneau L., and Lafond J. Characteristics of calcium uptake by BeWo cells, a human trophoblast cell line. Placenta 22 (2001) 768-775
    • (2001) Placenta , vol.22 , pp. 768-775
    • Moreau, R.1    Simoneau, L.2    Lafond, J.3
  • 259
    • 0036838842 scopus 로고    scopus 로고
    • Expression of calcium channels along the differentiation of cultured trophoblast cells from human term placenta
    • Moreau R., Hamel A., Daoud G., Simoneau L., and Lafond J. Expression of calcium channels along the differentiation of cultured trophoblast cells from human term placenta. Biol. Reprod. 67 (2002) 1473-1479
    • (2002) Biol. Reprod. , vol.67 , pp. 1473-1479
    • Moreau, R.1    Hamel, A.2    Daoud, G.3    Simoneau, L.4    Lafond, J.5
  • 260
    • 0037206124 scopus 로고    scopus 로고
    • Calcium uptake and calcium transporter expression by trophoblast cells from human term placenta
    • Moreau R., Daoud G., Bernatchez R., Simoneau L., Masse A., and Lafond J. Calcium uptake and calcium transporter expression by trophoblast cells from human term placenta. Biochim. Biophys. Acta 1564 (2002) 325-332
    • (2002) Biochim. Biophys. Acta , vol.1564 , pp. 325-332
    • Moreau, R.1    Daoud, G.2    Bernatchez, R.3    Simoneau, L.4    Masse, A.5    Lafond, J.6
  • 261
    • 0037295799 scopus 로고    scopus 로고
    • Calcium fluxes in human trophoblast (BeWo) cells: Calcium channels, calcium-ATPase, and sodium-calcium exchanger expression
    • Moreau R., Simoneau L., and Lafond J. Calcium fluxes in human trophoblast (BeWo) cells: Calcium channels, calcium-ATPase, and sodium-calcium exchanger expression. Mol. Reprod. Dev. 64 (2003) 189-198
    • (2003) Mol. Reprod. Dev. , vol.64 , pp. 189-198
    • Moreau, R.1    Simoneau, L.2    Lafond, J.3
  • 262
    • 0038689302 scopus 로고    scopus 로고
    • Expression and role of calcium-ATPase pump and sodium-calcium exchanger in differentiated trophoblasts from human term placenta
    • Moreau R., Daoud G., Masse A., Simoneau L., and Lafond J. Expression and role of calcium-ATPase pump and sodium-calcium exchanger in differentiated trophoblasts from human term placenta. Mol. Reprod. Dev. 65 (2003) 283-288
    • (2003) Mol. Reprod. Dev. , vol.65 , pp. 283-288
    • Moreau, R.1    Daoud, G.2    Masse, A.3    Simoneau, L.4    Lafond, J.5
  • 263
    • 0030972615 scopus 로고    scopus 로고
    • Genetic regulation of placental function: A quantitative in situ hybridization study of calcium binding protein (calbindin-D9k) and calcium ATPase mRNAs in sheep placenta
    • Morgan G., Wooding F.B., Care A.D., and Jones G.V. Genetic regulation of placental function: A quantitative in situ hybridization study of calcium binding protein (calbindin-D9k) and calcium ATPase mRNAs in sheep placenta. Placenta 18 (1997) 211-218
    • (1997) Placenta , vol.18 , pp. 211-218
    • Morgan, G.1    Wooding, F.B.2    Care, A.D.3    Jones, G.V.4
  • 264
    • 0034856576 scopus 로고    scopus 로고
    • Life and death in the placenta: New peptides and genes regulating human syncytiotrophoblast and extravillous cytotrophoblast lineage formation and renewal
    • Morrish D.W., Dakour J., and Li H. Life and death in the placenta: New peptides and genes regulating human syncytiotrophoblast and extravillous cytotrophoblast lineage formation and renewal. Curr. Protein Pept. Sci. 2 (2001) 245-259
    • (2001) Curr. Protein Pept. Sci. , vol.2 , pp. 245-259
    • Morrish, D.W.1    Dakour, J.2    Li, H.3
  • 269
    • 0024430881 scopus 로고
    • The effects of maternal caffeine intake during pregnancy on mineral contents of fetal rat bone
    • Nakamoto T., Grant S., and Yazdani M. The effects of maternal caffeine intake during pregnancy on mineral contents of fetal rat bone. Res. Exp. Med. (Berl.) 189 (1989) 275-280
    • (1989) Res. Exp. Med. (Berl.) , vol.189 , pp. 275-280
    • Nakamoto, T.1    Grant, S.2    Yazdani, M.3
  • 270
    • 0027433880 scopus 로고
    • Cloning of the rat aortic smooth muscle Na+/Ca2+ exchanger and tissue-specific expression of isoforms
    • Nakasaki Y., Iwamoto T., Hanada H., Imagawa T., and Shigekawa M. Cloning of the rat aortic smooth muscle Na+/Ca2+ exchanger and tissue-specific expression of isoforms. J. Biochem. (Tokyo) 114 (1993) 528-534
    • (1993) J. Biochem. (Tokyo) , vol.114 , pp. 528-534
    • Nakasaki, Y.1    Iwamoto, T.2    Hanada, H.3    Imagawa, T.4    Shigekawa, M.5
  • 271
    • 0027269620 scopus 로고
    • Evolution of EF-hand calcium-modulated proteins. III. Exon sequences confirm most dendrograms based on protein sequences: Calmodulin dendrograms show significant lack of parallelism
    • Nakayama S., and Kretsinger R.H. Evolution of EF-hand calcium-modulated proteins. III. Exon sequences confirm most dendrograms based on protein sequences: Calmodulin dendrograms show significant lack of parallelism. J. Mol. Evol. 36 (1993) 458-576
    • (1993) J. Mol. Evol. , vol.36 , pp. 458-576
    • Nakayama, S.1    Kretsinger, R.H.2
  • 273
    • 0037505657 scopus 로고    scopus 로고
    • Bone in the pregnant mother and newborn at birth
    • Namgung R., and Tsang R.C. Bone in the pregnant mother and newborn at birth. Clin. Chim. Acta 333 (2003) 1-11
    • (2003) Clin. Chim. Acta , vol.333 , pp. 1-11
    • Namgung, R.1    Tsang, R.C.2
  • 275
    • 0027472228 scopus 로고
    • Reduced serum osteocalcin and 1,25-dihydroxyvitamin D concentrations and low bone mineral content in small for gestational age infants: Evidence of decreased bone formation rates
    • Namgung R., Tsang R.C., Specker B.L., Sierra R.I., and Ho M.L. Reduced serum osteocalcin and 1,25-dihydroxyvitamin D concentrations and low bone mineral content in small for gestational age infants: Evidence of decreased bone formation rates. J. Pediatr. 122 (1993) 269-275
    • (1993) J. Pediatr. , vol.122 , pp. 269-275
    • Namgung, R.1    Tsang, R.C.2    Specker, B.L.3    Sierra, R.I.4    Ho, M.L.5
  • 276
    • 0027958982 scopus 로고
    • Low bone mineral content and high serum osteocalcin and 1,25-dihydroxyvitamin D in summer- versus winter-born newborn infants: An early fetal effect?
    • Namgung R., Tsang R.C., Specker B.L., Sierra R.I., and Ho M.L. Low bone mineral content and high serum osteocalcin and 1,25-dihydroxyvitamin D in summer- versus winter-born newborn infants: An early fetal effect?. J. Pediatr. Gastroenterol. Nutr. 19 (1994) 220-227
    • (1994) J. Pediatr. Gastroenterol. Nutr. , vol.19 , pp. 220-227
    • Namgung, R.1    Tsang, R.C.2    Specker, B.L.3    Sierra, R.I.4    Ho, M.L.5
  • 277
    • 0029816583 scopus 로고    scopus 로고
    • Normal serum indices of bone collagen biosynthesis and degradation in small for gestational age infants
    • Namgung R., Tsang R.C., Sierra R.I., and Ho M.L. Normal serum indices of bone collagen biosynthesis and degradation in small for gestational age infants. J. Pediatr. Gastroenterol. Nutr. 23 (1996) 224-228
    • (1996) J. Pediatr. Gastroenterol. Nutr. , vol.23 , pp. 224-228
    • Namgung, R.1    Tsang, R.C.2    Sierra, R.I.3    Ho, M.L.4
  • 278
    • 0031941893 scopus 로고    scopus 로고
    • Low total body bone mineral content and high bone resorption in Korean winter-born versus summer-born newborn infants
    • Namgung R., Tsang R.C., Lee C., Han D.G., Ho M.L., and Sierra R.I. Low total body bone mineral content and high bone resorption in Korean winter-born versus summer-born newborn infants. J. Pediatr. 132 (1998) 421-425
    • (1998) J. Pediatr. , vol.132 , pp. 421-425
    • Namgung, R.1    Tsang, R.C.2    Lee, C.3    Han, D.G.4    Ho, M.L.5    Sierra, R.I.6
  • 279
    • 0025243512 scopus 로고
    • Molecular cloning and functional expression of the cardiac sarcolemmal Na(+)-Ca2+ exchanger
    • Nicoll D.A., Longoni S., and Philipson K.D. Molecular cloning and functional expression of the cardiac sarcolemmal Na(+)-Ca2+ exchanger. Science 250 (1990) 562-565
    • (1990) Science , vol.250 , pp. 562-565
    • Nicoll, D.A.1    Longoni, S.2    Philipson, K.D.3
  • 281
    • 0035853086 scopus 로고    scopus 로고
    • Competitive regulation of CaT-like-mediated Ca2+ entry by protein kinase C and calmodulin
    • Niemeyer B.A., Bergs C., Wissenbach U., Flockerzi V., and Trost C. Competitive regulation of CaT-like-mediated Ca2+ entry by protein kinase C and calmodulin. Proc. Natl. Acad. Sci. USA 98 (2001) 3600-3605
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 3600-3605
    • Niemeyer, B.A.1    Bergs, C.2    Wissenbach, U.3    Flockerzi, V.4    Trost, C.5
  • 282
    • 0031924373 scopus 로고    scopus 로고
    • Immunocytochemical and in situ hybridization studies of the distribution of calbindin D9k in the bovine placenta throughout pregnancy
    • Nikitenko L., Morgan G., Kolesnikov S.I., and Wooding F.B. Immunocytochemical and in situ hybridization studies of the distribution of calbindin D9k in the bovine placenta throughout pregnancy. J. Histochem. Cytochem. 46 (1998) 679-688
    • (1998) J. Histochem. Cytochem. , vol.46 , pp. 679-688
    • Nikitenko, L.1    Morgan, G.2    Kolesnikov, S.I.3    Wooding, F.B.4
  • 283
    • 0035847013 scopus 로고    scopus 로고
    • The single pore residue Asp542 determines Ca2+ permeation and Mg2+ block of the epithelial Ca2+ channel
    • Nilius B., Vennekens R., Prenen J., Hoenderop J.G., Droogmans G., and Bindels R.J. The single pore residue Asp542 determines Ca2+ permeation and Mg2+ block of the epithelial Ca2+ channel. J. Biol. Chem. 276 (2001) 1020-1025
    • (2001) J. Biol. Chem. , vol.276 , pp. 1020-1025
    • Nilius, B.1    Vennekens, R.2    Prenen, J.3    Hoenderop, J.G.4    Droogmans, G.5    Bindels, R.J.6
  • 284
    • 0032079521 scopus 로고    scopus 로고
    • A negative vitamin D response DNA element in the human parathyroid hormone-related peptide gene binds to vitamin D receptor along with Ku antigen to mediate negative gene regulation by vitamin D
    • Nishishita T., Okazaki T., Ishikawa T., Igarashi T., Hata K., Ogata E., and Fujita T. A negative vitamin D response DNA element in the human parathyroid hormone-related peptide gene binds to vitamin D receptor along with Ku antigen to mediate negative gene regulation by vitamin D. J. Biol. Chem. 273 (1998) 10901-10907
    • (1998) J. Biol. Chem. , vol.273 , pp. 10901-10907
    • Nishishita, T.1    Okazaki, T.2    Ishikawa, T.3    Igarashi, T.4    Hata, K.5    Ogata, E.6    Fujita, T.7
  • 285
    • 0034891331 scopus 로고    scopus 로고
    • Calcium metabolism in pregnancy: Disturbed calcium homeostasis in diabetic pregnancy and preeclampsia
    • Ohara N. Calcium metabolism in pregnancy: Disturbed calcium homeostasis in diabetic pregnancy and preeclampsia. Clin. Exp. Obstet. Gynecol. 28 (2001) 133-141
    • (2001) Clin. Exp. Obstet. Gynecol. , vol.28 , pp. 133-141
    • Ohara, N.1
  • 286
    • 4043055834 scopus 로고    scopus 로고
    • Targeted ablation of plasma membrane Ca2+-ATPase (PMCA) 1 and 4 indicates a major housekeeping function for PMCA1 and a critical role in hyperactivated sperm motility and male fertility for PMCA4
    • Okunade G.W., Miller M.L., Pyne G.J., Sutliff R.L., O'Connor K.T., Neumann J.C., Andringa A., Miller D.A., Prasad V., Doetschman T., Paul R.J., and Shull G.E. Targeted ablation of plasma membrane Ca2+-ATPase (PMCA) 1 and 4 indicates a major housekeeping function for PMCA1 and a critical role in hyperactivated sperm motility and male fertility for PMCA4. J. Biol. Chem. 279 (2004) 33742-33750
    • (2004) J. Biol. Chem. , vol.279 , pp. 33742-33750
    • Okunade, G.W.1    Miller, M.L.2    Pyne, G.J.3    Sutliff, R.L.4    O'Connor, K.T.5    Neumann, J.C.6    Andringa, A.7    Miller, D.A.8    Prasad, V.9    Doetschman, T.10    Paul, R.J.11    Shull, G.E.12
  • 287
    • 0030810066 scopus 로고    scopus 로고
    • Store depletion and calcium influx
    • Parekh A.B., and Penner R. Store depletion and calcium influx. Physiol. Rev. 77 (1997) 901-930
    • (1997) Physiol. Rev. , vol.77 , pp. 901-930
    • Parekh, A.B.1    Penner, R.2
  • 288
    • 15544368216 scopus 로고    scopus 로고
    • Store-operated calcium channels
    • Parekh A.B., and Putney Jr. J.W. Store-operated calcium channels. Physiol. Rev. 85 (2005) 757-810
    • (2005) Physiol. Rev. , vol.85 , pp. 757-810
    • Parekh, A.B.1    Putney Jr., J.W.2
  • 289
    • 0028589615 scopus 로고
    • The calcium current activated by T cell receptor and store depletion in human lymphocytes is absent in a primary immunodeficiency
    • Partiseti M., Le Deist F., Hivroz C., Fischer A., Korn H., and Choquet D. The calcium current activated by T cell receptor and store depletion in human lymphocytes is absent in a primary immunodeficiency. J. Biol. Chem. 269 (1994) 32327-32335
    • (1994) J. Biol. Chem. , vol.269 , pp. 32327-32335
    • Partiseti, M.1    Le Deist, F.2    Hivroz, C.3    Fischer, A.4    Korn, H.5    Choquet, D.6
  • 290
    • 0033566735 scopus 로고    scopus 로고
    • A null mutation in the inflammation-associated S100 protein S100A8 causes early resorption of the mouse embryo
    • Passey R.J., Williams E., Lichanska A.M., Wells C., Hu S., Geczy C.L., Little M.H., and Hume D.A. A null mutation in the inflammation-associated S100 protein S100A8 causes early resorption of the mouse embryo. J. Immunol. 163 (1999) 2209-2216
    • (1999) J. Immunol. , vol.163 , pp. 2209-2216
    • Passey, R.J.1    Williams, E.2    Lichanska, A.M.3    Wells, C.4    Hu, S.5    Geczy, C.L.6    Little, M.H.7    Hume, D.A.8
  • 291
    • 0036489419 scopus 로고    scopus 로고
    • Plasma membrane Ca2+ATPase isoform 4b is cleaved and activated by caspase-3 during the early phase of apoptosis
    • Paszty K., Verma A.K., Padanyi R., Filoteo A.G., Penniston J.T., and Enyedi A. Plasma membrane Ca2+ATPase isoform 4b is cleaved and activated by caspase-3 during the early phase of apoptosis. J. Biol. Chem. 277 (2002) 6822-6829
    • (2002) J. Biol. Chem. , vol.277 , pp. 6822-6829
    • Paszty, K.1    Verma, A.K.2    Padanyi, R.3    Filoteo, A.G.4    Penniston, J.T.5    Enyedi, A.6
  • 292
    • 0030577844 scopus 로고    scopus 로고
    • The Ca2+(-)binding proteins parvalbumin and oncomodulin and their genes: New structural and functional findings
    • Pauls T.L., Cox J.A., and Berchtold M.W. The Ca2+(-)binding proteins parvalbumin and oncomodulin and their genes: New structural and functional findings. Biochim. Biophys. Acta 1306 (1996) 39-54
    • (1996) Biochim. Biophys. Acta , vol.1306 , pp. 39-54
    • Pauls, T.L.1    Cox, J.A.2    Berchtold, M.W.3
  • 293
    • 0033529713 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a channel-like transporter mediating intestinal calcium absorption
    • Peng J.B., Chen X.Z., Berger U.V., Vassilev P.M., Tsukaguchi H., Brown E.M., and Hediger M.A. Molecular cloning and characterization of a channel-like transporter mediating intestinal calcium absorption. J. Biol. Chem. 274 (1999) 22739-22746
    • (1999) J. Biol. Chem. , vol.274 , pp. 22739-22746
    • Peng, J.B.1    Chen, X.Z.2    Berger, U.V.3    Vassilev, P.M.4    Tsukaguchi, H.5    Brown, E.M.6    Hediger, M.A.7
  • 295
    • 0035878469 scopus 로고    scopus 로고
    • Structural conservation of the genes encoding CaT1, CaT2, and related cation channels
    • Peng J.B., Brown E.M., and Hediger M.A. Structural conservation of the genes encoding CaT1, CaT2, and related cation channels. Genomics 76 (2001) 99-109
    • (2001) Genomics , vol.76 , pp. 99-109
    • Peng, J.B.1    Brown, E.M.2    Hediger, M.A.3
  • 297
    • 0042422130 scopus 로고    scopus 로고
    • Apical entry channels in calcium-transporting epithelia
    • Peng J.B., Brown E.M., and Hediger M.A. Apical entry channels in calcium-transporting epithelia. News Physiol. Sci. 18 (2003) 158-163
    • (2003) News Physiol. Sci. , vol.18 , pp. 158-163
    • Peng, J.B.1    Brown, E.M.2    Hediger, M.A.3
  • 298
    • 0035185591 scopus 로고    scopus 로고
    • Characterization of the deafwaddler mutant of the rat plasma membrane calcium-ATPase 2
    • Penheiter A.R., Filoteo A.G., Croy C.L., and Penniston J.T. Characterization of the deafwaddler mutant of the rat plasma membrane calcium-ATPase 2. Hear. Res. 162 (2001) 19-28
    • (2001) Hear. Res. , vol.162 , pp. 19-28
    • Penheiter, A.R.1    Filoteo, A.G.2    Croy, C.L.3    Penniston, J.T.4
  • 299
    • 0032530540 scopus 로고    scopus 로고
    • Modulation of the plasma membrane Ca2+ pump
    • Penniston J.T., and Enyedi A. Modulation of the plasma membrane Ca2+ pump. J. Membr. Biol. 165 (1998) 101-109
    • (1998) J. Membr. Biol. , vol.165 , pp. 101-109
    • Penniston, J.T.1    Enyedi, A.2
  • 300
    • 0037207469 scopus 로고    scopus 로고
    • Molecular physiology of low-voltage-activated t-type calcium channels
    • Perez-Reyes E. Molecular physiology of low-voltage-activated t-type calcium channels. Physiol. Rev. 83 (2003) 117-161
    • (2003) Physiol. Rev. , vol.83 , pp. 117-161
    • Perez-Reyes, E.1
  • 301
    • 0029134828 scopus 로고
    • Molecular biology of calcium channels
    • Perez-Reyes E., and Schneider T. Molecular biology of calcium channels. Kidney Int. 48 (1995) 1111-1124
    • (1995) Kidney Int. , vol.48 , pp. 1111-1124
    • Perez-Reyes, E.1    Schneider, T.2
  • 303
    • 0029049786 scopus 로고
    • Stimulation of intracellular calcium concentration by adenosine triphosphate and uridine 5′-triphosphate in human term placental cells: Evidence for purinergic receptors
    • Petit A., and Belisle S. Stimulation of intracellular calcium concentration by adenosine triphosphate and uridine 5′-triphosphate in human term placental cells: Evidence for purinergic receptors. J. Clin. Endocrinol. Metab. 80 (1995) 1809-1815
    • (1995) J. Clin. Endocrinol. Metab. , vol.80 , pp. 1809-1815
    • Petit, A.1    Belisle, S.2
  • 305
    • 25144454969 scopus 로고    scopus 로고
    • The Na+-Ca2+ exchanger: Molecular aspects
    • Morad, M., Ebashi S., Trautwein W., and Kurachi Y. (Eds), Kluwer Academic Publishers, Boston, MA
    • Philipson K.D. The Na+-Ca2+ exchanger: Molecular aspects. In: Morad, M., Ebashi S., Trautwein W., and Kurachi Y. (Eds). "Molecular Physiology and Pharmacology of Cardiac Ion Channels and Transporters" (1996), Kluwer Academic Publishers, Boston, MA 435-445
    • (1996) "Molecular Physiology and Pharmacology of Cardiac Ion Channels and Transporters" , pp. 435-445
    • Philipson, K.D.1
  • 306
    • 0027272471 scopus 로고
    • Molecular and kinetic aspects of sodium-calcium exchange
    • Philipson K.D., and Nicoll D.A. Molecular and kinetic aspects of sodium-calcium exchange. Int. Rev. Cytol. 137C (1993) 199-227
    • (1993) Int. Rev. Cytol. , vol.137 C , pp. 199-227
    • Philipson, K.D.1    Nicoll, D.A.2
  • 307
  • 308
    • 0019378232 scopus 로고
    • Review article: Trophoblast invasion and the establishment of haemochorial placentation in man and laboratory animals
    • Pijnenborg R., Robertson W.B., Brosens I., and Dixon G. Review article: Trophoblast invasion and the establishment of haemochorial placentation in man and laboratory animals. Placenta 2 (1981) 71-91
    • (1981) Placenta , vol.2 , pp. 71-91
    • Pijnenborg, R.1    Robertson, W.B.2    Brosens, I.3    Dixon, G.4
  • 309
    • 0020603626 scopus 로고
    • Uteroplacental arterial changes related to interstitial trophoblast migration in early human pregnancy
    • Pijnenborg R., Bland J.M., Robertson W.B., and Brosens I. Uteroplacental arterial changes related to interstitial trophoblast migration in early human pregnancy. Placenta 4 (1983) 397-413
    • (1983) Placenta , vol.4 , pp. 397-413
    • Pijnenborg, R.1    Bland, J.M.2    Robertson, W.B.3    Brosens, I.4
  • 310
    • 0021068167 scopus 로고
    • Endocrine regulation of calcium homeostasis during pregnancy
    • Pitkin R.M. Endocrine regulation of calcium homeostasis during pregnancy. Clin. Perinatol. 10 (1983) 575-592
    • (1983) Clin. Perinatol. , vol.10 , pp. 575-592
    • Pitkin, R.M.1
  • 311
    • 0030003266 scopus 로고    scopus 로고
    • Expression and functional characterization of isoforms 4 of the plasma membrane calcium pump
    • Preiano B.S., Guerini D., and Carafoli E. Expression and functional characterization of isoforms 4 of the plasma membrane calcium pump. Biochemistry 35 (1996) 7946-7953
    • (1996) Biochemistry , vol.35 , pp. 7946-7953
    • Preiano, B.S.1    Guerini, D.2    Carafoli, E.3
  • 312
    • 0033826761 scopus 로고    scopus 로고
    • Calcium in pregnancy and lactation
    • Prentice A. Calcium in pregnancy and lactation. Annu. Rev. Nutr. 20 (2000) 249-272
    • (2000) Annu. Rev. Nutr. , vol.20 , pp. 249-272
    • Prentice, A.1
  • 313
    • 0035810178 scopus 로고    scopus 로고
    • Cell biology. Channelling calcium
    • Putney Jr. J.W. Cell biology. Channelling calcium. Nature 410 (2001) 648-649
    • (2001) Nature , vol.410 , pp. 648-649
    • Putney Jr., J.W.1
  • 314
    • 26444509424 scopus 로고    scopus 로고
    • Physiological mechanisms of TRPC activation
    • Putney J.W. Physiological mechanisms of TRPC activation. Pflugers Arch. 451 (2005) 29-34
    • (2005) Pflugers Arch. , vol.451 , pp. 29-34
    • Putney, J.W.1
  • 315
    • 0027422088 scopus 로고
    • The signal for capacitative calcium entry
    • Putney Jr. J.W., and Bird G.S. The signal for capacitative calcium entry. Cell 75 (1993) 199-201
    • (1993) Cell , vol.75 , pp. 199-201
    • Putney Jr., J.W.1    Bird, G.S.2
  • 316
    • 7644223075 scopus 로고    scopus 로고
    • Functional characterisation and genomic analysis of an epithelial calcium channel (ECaC) from pufferfish, Fugu rubripes
    • Qiu A., and Hogstrand C. Functional characterisation and genomic analysis of an epithelial calcium channel (ECaC) from pufferfish, Fugu rubripes. Gene 342 (2004) 113-123
    • (2004) Gene , vol.342 , pp. 113-123
    • Qiu, A.1    Hogstrand, C.2
  • 317
    • 0030912068 scopus 로고    scopus 로고
    • Tissue specificity and alternative splicing of the Na+/Ca2+ exchanger isoforms NCX1, NCX2, and NCX3 in rat
    • Quednau B.D., Nicoll D.A., and Philipson K.D. Tissue specificity and alternative splicing of the Na+/Ca2+ exchanger isoforms NCX1, NCX2, and NCX3 in rat. Am. J. Physiol. 272 (1997) C1250-C1261
    • (1997) Am. J. Physiol. , vol.272
    • Quednau, B.D.1    Nicoll, D.A.2    Philipson, K.D.3
  • 318
    • 0037163041 scopus 로고    scopus 로고
    • Cloning and characterization of a calcium-binding, histamine-releasing protein from Schistosoma mansoni
    • Rao K.V., Chen L., Gnanasekar M., and Ramaswamy K. Cloning and characterization of a calcium-binding, histamine-releasing protein from Schistosoma mansoni. J. Biol. Chem. 277 (2002) 31207-31213
    • (2002) J. Biol. Chem. , vol.277 , pp. 31207-31213
    • Rao, K.V.1    Chen, L.2    Gnanasekar, M.3    Ramaswamy, K.4
  • 320
    • 0028978651 scopus 로고
    • Calbindin-D9k expression in the pregnant cow uterus and placenta
    • Reiswig J.D., Frazer G.S., and Inpanbutr N. Calbindin-D9k expression in the pregnant cow uterus and placenta. Histochem. Cell Biol. 104 (1995) 169-174
    • (1995) Histochem. Cell Biol. , vol.104 , pp. 169-174
    • Reiswig, J.D.1    Frazer, G.S.2    Inpanbutr, N.3
  • 322
    • 0020693764 scopus 로고
    • Calcium channel modulation by neurotransmitters, enzymes and drugs
    • Reuter H. Calcium channel modulation by neurotransmitters, enzymes and drugs. Nature 301 (1983) 569-574
    • (1983) Nature , vol.301 , pp. 569-574
    • Reuter, H.1
  • 324
    • 0028924833 scopus 로고
    • Cloning and functional expression of a rat kidney extracellular calcium/polyvalent cation-sensing receptor
    • Riccardi D., Park J., Lee W.S., Gamba G., Brown E.M., and Hebert S.C. Cloning and functional expression of a rat kidney extracellular calcium/polyvalent cation-sensing receptor. Proc. Natl. Acad. Sci. USA 92 (1995) 131-135
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 131-135
    • Riccardi, D.1    Park, J.2    Lee, W.S.3    Gamba, G.4    Brown, E.M.5    Hebert, S.C.6
  • 326
    • 1842267369 scopus 로고
    • Studies of placental morphogenesis. I. Radioautographic studies of human placenta utilizing tritiated thymidine
    • Richart R. Studies of placental morphogenesis. I. Radioautographic studies of human placenta utilizing tritiated thymidine. Proc. Soc. Exp. Biol. Med. 106 (1961) 829-831
    • (1961) Proc. Soc. Exp. Biol. Med. , vol.106 , pp. 829-831
    • Richart, R.1
  • 327
    • 0034060702 scopus 로고    scopus 로고
    • Dietary calcium and pregnancy-induced hypertension: Is there a relation?
    • Ritchie L.D., and King J.C. Dietary calcium and pregnancy-induced hypertension: Is there a relation?. Am. J. Clin. Nutr. 71 (2000) 1371S-1374S
    • (2000) Am. J. Clin. Nutr. , vol.71
    • Ritchie, L.D.1    King, J.C.2
  • 328
    • 0034465231 scopus 로고    scopus 로고
    • Characterization of neuropeptide Y-mediated corticotropin-releasing factor synthesis and release from human placental trophoblasts
    • Robidoux J., Simoneau L., St-Pierre S., Masse A., and Lafond J. Characterization of neuropeptide Y-mediated corticotropin-releasing factor synthesis and release from human placental trophoblasts. Endocrinology 141 (2000) 2795-2804
    • (2000) Endocrinology , vol.141 , pp. 2795-2804
    • Robidoux, J.1    Simoneau, L.2    St-Pierre, S.3    Masse, A.4    Lafond, J.5
  • 329
    • 0033709496 scopus 로고    scopus 로고
    • Activation of L-type calcium channels induces corticotropin-releasing factor secretion from human placental trophoblasts
    • Robidoux J., Simoneau L., Masse A., and Lafond J. Activation of L-type calcium channels induces corticotropin-releasing factor secretion from human placental trophoblasts. J. Clin. Endocrinol. Metab. 85 (2000) 3356-3364
    • (2000) J. Clin. Endocrinol. Metab. , vol.85 , pp. 3356-3364
    • Robidoux, J.1    Simoneau, L.2    Masse, A.3    Lafond, J.4
  • 330
    • 0022493076 scopus 로고
    • Localization of vitamin D-dependent active Ca2+ transport in rat duodenum and relation to CaBP
    • Roche C., Bellaton C., Pansu D., Miller III A., and Bronner F. Localization of vitamin D-dependent active Ca2+ transport in rat duodenum and relation to CaBP. Am. J. Physiol. 251 (1986) G314-G320
    • (1986) Am. J. Physiol. , vol.251
    • Roche, C.1    Bellaton, C.2    Pansu, D.3    Miller III, A.4    Bronner, F.5
  • 331
    • 1842264105 scopus 로고
    • Parathyroid hormone-related protein (PTHrP): An oncofetal protein contributing to placental calicium transport
    • Brennecke S.P., and Rice G.E. (Eds), CRC Press, Boca Raton, FL
    • Rodda C.P., and Moseley J.M. Parathyroid hormone-related protein (PTHrP): An oncofetal protein contributing to placental calicium transport. In: Brennecke S.P., and Rice G.E. (Eds). "Molecular Aspects of Placental and Fetal Membrane Autocoids" (1993), CRC Press, Boca Raton, FL 209-238
    • (1993) "Molecular Aspects of Placental and Fetal Membrane Autocoids" , pp. 209-238
    • Rodda, C.P.1    Moseley, J.M.2
  • 332
    • 0023944150 scopus 로고
    • Evidence for a novel parathyroid hormone-related protein in fetal lamb parathyroid glands and sheep placenta: Comparisons with a similar protein implicated in humoral hypercalcaemia of malignancy
    • Rodda C.P., Kubota M., Heath J.A., Ebeling P.R., Moseley J.M., Care A.D., Caple I.W., and Martin T.J. Evidence for a novel parathyroid hormone-related protein in fetal lamb parathyroid glands and sheep placenta: Comparisons with a similar protein implicated in humoral hypercalcaemia of malignancy. J. Endocrinol. 117 (1988) 261-271
    • (1988) J. Endocrinol. , vol.117 , pp. 261-271
    • Rodda, C.P.1    Kubota, M.2    Heath, J.A.3    Ebeling, P.R.4    Moseley, J.M.5    Care, A.D.6    Caple, I.W.7    Martin, T.J.8
  • 333
    • 0028955536 scopus 로고
    • Calcium sensing receptor: Molecular cloning in rat and localization to nerve terminals
    • Ruat M., Molliver M.E., Snowman A.M., and Snyder S.H. Calcium sensing receptor: Molecular cloning in rat and localization to nerve terminals. Proc. Natl. Acad. Sci. USA 92 (1995) 3161-3165
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 3161-3165
    • Ruat, M.1    Molliver, M.E.2    Snowman, A.M.3    Snyder, S.H.4
  • 337
    • 0033173667 scopus 로고    scopus 로고
    • Tissue expression of the S100 protein family-related MRP8 gene in human chorionic villi by in situ hybridization techniques
    • Sato N., Isono K., Ishiwata I., Nakai M., and Kami K. Tissue expression of the S100 protein family-related MRP8 gene in human chorionic villi by in situ hybridization techniques. Okajimas Folia Anat. Jpn. 76 (1999) 123-129
    • (1999) Okajimas Folia Anat. Jpn. , vol.76 , pp. 123-129
    • Sato, N.1    Isono, K.2    Ishiwata, I.3    Nakai, M.4    Kami, K.5
  • 338
    • 0032127218 scopus 로고    scopus 로고
    • Urinary calcium/creatinine ratio as a predictor of preeclampsia
    • Saudan P.J., Shaw L., and Brown M.A. Urinary calcium/creatinine ratio as a predictor of preeclampsia. Am. J. Hypertens. 11 (1998) 839-843
    • (1998) Am. J. Hypertens. , vol.11 , pp. 839-843
    • Saudan, P.J.1    Shaw, L.2    Brown, M.A.3
  • 339
    • 0029669991 scopus 로고    scopus 로고
    • The S100 family of EF-hand calcium-binding proteins: Functions and pathology
    • Schafer B.W., and Heizmann C.W. The S100 family of EF-hand calcium-binding proteins: Functions and pathology. Trends Biochem. Sci. 21 (1996) 134-140
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 134-140
    • Schafer, B.W.1    Heizmann, C.W.2
  • 340
    • 0028987554 scopus 로고
    • Isolation of a YAC clone covering a cluster of nine S100 genes on human chromosome 1q21: Rationale for a new nomenclature of the S100 calcium-binding protein family
    • Schafer B.W., Wicki R., Engelkamp D., Mattei M.G., and Heizmann C.W. Isolation of a YAC clone covering a cluster of nine S100 genes on human chromosome 1q21: Rationale for a new nomenclature of the S100 calcium-binding protein family. Genomics 25 (1995) 638-643
    • (1995) Genomics , vol.25 , pp. 638-643
    • Schafer, B.W.1    Wicki, R.2    Engelkamp, D.3    Mattei, M.G.4    Heizmann, C.W.5
  • 342
    • 0025794369 scopus 로고
    • The role of the placenta in nutrition of the human fetus
    • Schneider H. The role of the placenta in nutrition of the human fetus. Am. J. Obstet. Gynecol. 164 (1991) 967-973
    • (1991) Am. J. Obstet. Gynecol. , vol.164 , pp. 967-973
    • Schneider, H.1
  • 344
    • 0026767069 scopus 로고
    • Lower serum ionized calcium and abnormal calciotropic hormone levels in preeclampsia
    • Seely E.W., Wood R.J., Brown E.M., and Graves S.W. Lower serum ionized calcium and abnormal calciotropic hormone levels in preeclampsia. J. Clin. Endocrinol. Metab. 74 (1992) 1436-1440
    • (1992) J. Clin. Endocrinol. Metab. , vol.74 , pp. 1436-1440
    • Seely, E.W.1    Wood, R.J.2    Brown, E.M.3    Graves, S.W.4
  • 345
    • 0029360340 scopus 로고
    • Effects of tobacco smoke inhalation on the developing mouse embryo and fetus
    • Seller M.J., and Bnait K.S. Effects of tobacco smoke inhalation on the developing mouse embryo and fetus. Reprod. Toxicol. 9 (1995) 449-459
    • (1995) Reprod. Toxicol. , vol.9 , pp. 449-459
    • Seller, M.J.1    Bnait, K.S.2
  • 347
    • 0025829956 scopus 로고
    • Expression of parathyroid hormone-related protein mRNA in the rat before birth: Demonstration by hybridization histochemistry
    • Senior P.V., Heath D.A., and Beck F. Expression of parathyroid hormone-related protein mRNA in the rat before birth: Demonstration by hybridization histochemistry. J. Mol. Endocrinol. 6 (1991) 281-290
    • (1991) J. Mol. Endocrinol. , vol.6 , pp. 281-290
    • Senior, P.V.1    Heath, D.A.2    Beck, F.3
  • 349
    • 0026591411 scopus 로고
    • Mapping of the gene for the cardiac sarcolemmal Na(+)-Ca2+ exchanger to human chromosome 2p21-p23
    • Shieh B.H., Xia Y., Sparkes R.S., Klisak I., Lusis A.J., Nicoll D.A., and Philipson K.D. Mapping of the gene for the cardiac sarcolemmal Na(+)-Ca2+ exchanger to human chromosome 2p21-p23. Genomics 12 (1992) 616-617
    • (1992) Genomics , vol.12 , pp. 616-617
    • Shieh, B.H.1    Xia, Y.2    Sparkes, R.S.3    Klisak, I.4    Lusis, A.J.5    Nicoll, D.A.6    Philipson, K.D.7
  • 350
    • 0002343679 scopus 로고
    • The ultrastructural basis of the nutritional transfer: Evidence of different patterns in the plasma membranes of the multilayered placental barrier
    • Sideri M., de Vergiliis G., Trainoldi R., and Remotti G. The ultrastructural basis of the nutritional transfer: Evidence of different patterns in the plasma membranes of the multilayered placental barrier. Trophoblast Res. 1 (1983) 15-26
    • (1983) Trophoblast Res. , vol.1 , pp. 15-26
    • Sideri, M.1    de Vergiliis, G.2    Trainoldi, R.3    Remotti, G.4
  • 351
    • 0026653769 scopus 로고
    • Nutrient transport pathways across the epithelium of the placenta
    • Smith C.H., Moe A.J., and Ganapathy V. Nutrient transport pathways across the epithelium of the placenta. Annu. Rev. Nutr. 12 (1992) 183-206
    • (1992) Annu. Rev. Nutr. , vol.12 , pp. 183-206
    • Smith, C.H.1    Moe, A.J.2    Ganapathy, V.3
  • 352
    • 0028043535 scopus 로고
    • Signal transduction and regulation in smooth muscle
    • Somlyo A.P., and Somlyo A.V. Signal transduction and regulation in smooth muscle. Nature 372 (1994) 231-236
    • (1994) Nature , vol.372 , pp. 231-236
    • Somlyo, A.P.1    Somlyo, A.V.2
  • 353
    • 0041419383 scopus 로고    scopus 로고
    • Calcium transporter 1 and epithelial calcium channel messenger ribonucleic acid are differentially regulated by 1,25 dihydroxyvitamin D3 in the intestine and kidney of mice
    • Song Y., Peng X., Porta A., Takanaga H., Peng J.B., Hediger M.A., Fleet J.C., and Christakos S. Calcium transporter 1 and epithelial calcium channel messenger ribonucleic acid are differentially regulated by 1,25 dihydroxyvitamin D3 in the intestine and kidney of mice. Endocrinology 144 (2003) 3885-3894
    • (2003) Endocrinology , vol.144 , pp. 3885-3894
    • Song, Y.1    Peng, X.2    Porta, A.3    Takanaga, H.4    Peng, J.B.5    Hediger, M.A.6    Fleet, J.C.7    Christakos, S.8
  • 354
    • 0033607686 scopus 로고    scopus 로고
    • Calbindin-D(28k) controls [Ca(2+)](i) and insulin release. Evidence obtained from calbindin-d(28k) knockout mice and beta cell lines
    • Sooy K., Schermerhorn T., Noda M., Surana M., Rhoten W.B., Meyer M., Fleischer N., Sharp G.W., and Christakos S. Calbindin-D(28k) controls [Ca(2+)](i) and insulin release. Evidence obtained from calbindin-d(28k) knockout mice and beta cell lines. J. Biol. Chem. 274 (1999) 34343-34349
    • (1999) J. Biol. Chem. , vol.274 , pp. 34343-34349
    • Sooy, K.1    Schermerhorn, T.2    Noda, M.3    Surana, M.4    Rhoten, W.B.5    Meyer, M.6    Fleischer, N.7    Sharp, G.W.8    Christakos, S.9
  • 355
    • 0033568165 scopus 로고    scopus 로고
    • Molecular cloning and characterization of TRPC5 (HTRP5), the human homologue of a mouse brain receptor-activated capacitative Ca2+ entry channel
    • Sossey-Alaoui K., Lyon J.A., Jones L., Abidi F.E., Hartung A.J., Hane B., Schwartz C.E., Stevenson R.E., and Srivastava A.K. Molecular cloning and characterization of TRPC5 (HTRP5), the human homologue of a mouse brain receptor-activated capacitative Ca2+ entry channel. Genomics 60 (1999) 330-340
    • (1999) Genomics , vol.60 , pp. 330-340
    • Sossey-Alaoui, K.1    Lyon, J.A.2    Jones, L.3    Abidi, F.E.4    Hartung, A.J.5    Hane, B.6    Schwartz, C.E.7    Stevenson, R.E.8    Srivastava, A.K.9
  • 356
    • 0027518196 scopus 로고
    • Quantitative analysis of alternative splicing options of human plasma membrane calcium pump genes
    • Stauffer T.P., Hilfiker H., Carafoli E., and Strehler E.E. Quantitative analysis of alternative splicing options of human plasma membrane calcium pump genes. J. Biol. Chem. 268 (1993) 25993-26003
    • (1993) J. Biol. Chem. , vol.268 , pp. 25993-26003
    • Stauffer, T.P.1    Hilfiker, H.2    Carafoli, E.3    Strehler, E.E.4
  • 357
    • 0029013891 scopus 로고
    • Tissue distribution of the four gene products of the plasma membrane Ca2+ pump. A study using specific antibodies
    • Stauffer T.P., Guerini D., and Carafoli E. Tissue distribution of the four gene products of the plasma membrane Ca2+ pump. A study using specific antibodies. J. Biol. Chem. 270 (1995) 12184-12190
    • (1995) J. Biol. Chem. , vol.270 , pp. 12184-12190
    • Stauffer, T.P.1    Guerini, D.2    Carafoli, E.3
  • 358
    • 0021288602 scopus 로고
    • Ca2+-binding protein from human kidney. Purification and properties
    • Staun M., Noren O., and Sjostrom H. Ca2+-binding protein from human kidney. Purification and properties. Biochem. J. 217 (1984) 229-237
    • (1984) Biochem. J. , vol.217 , pp. 229-237
    • Staun, M.1    Noren, O.2    Sjostrom, H.3
  • 359
    • 0028829062 scopus 로고
    • Determinants of PKC-dependent modulation of a family of neuronal calcium channels
    • Stea A., Soong T.W., and Snutch T.P. Determinants of PKC-dependent modulation of a family of neuronal calcium channels. Neuron 15 (1995) 929-940
    • (1995) Neuron , vol.15 , pp. 929-940
    • Stea, A.1    Soong, T.W.2    Snutch, T.P.3
  • 360
    • 0026098439 scopus 로고
    • Recent advances in the molecular characterization of plasma membrane Ca2+ pumps
    • Strehler E.E. Recent advances in the molecular characterization of plasma membrane Ca2+ pumps. J. Membr. Biol. 120 (1991) 1-15
    • (1991) J. Membr. Biol. , vol.120 , pp. 1-15
    • Strehler, E.E.1
  • 361
    • 0035137205 scopus 로고    scopus 로고
    • Role of alternative splicing in generating isoform diversity among plasma membrane calcium pumps
    • Strehler E.E., and Zacharias D.A. Role of alternative splicing in generating isoform diversity among plasma membrane calcium pumps. Physiol. Rev. 81 (2001) 21-50
    • (2001) Physiol. Rev. , vol.81 , pp. 21-50
    • Strehler, E.E.1    Zacharias, D.A.2
  • 362
    • 0033623836 scopus 로고    scopus 로고
    • ATP-dependent Ca2+ transport is up-regulated during third trimester in human syncytiotrophoblast basal membranes
    • Strid H., and Powell T.L. ATP-dependent Ca2+ transport is up-regulated during third trimester in human syncytiotrophoblast basal membranes. Pediatr. Res. 48 (2000) 58-63
    • (2000) Pediatr. Res. , vol.48 , pp. 58-63
    • Strid, H.1    Powell, T.L.2
  • 363
    • 18744399257 scopus 로고    scopus 로고
    • Parathyroid hormone-related peptide (38-94) amide stimulates ATP-dependent calcium transport in the basal plasma membrane of the human syncytiotrophoblast
    • Strid H., Care A., Jansson T., and Powell T. Parathyroid hormone-related peptide (38-94) amide stimulates ATP-dependent calcium transport in the basal plasma membrane of the human syncytiotrophoblast. J. Endocrinol. 175 (2002) 517-524
    • (2002) J. Endocrinol. , vol.175 , pp. 517-524
    • Strid, H.1    Care, A.2    Jansson, T.3    Powell, T.4
  • 364
    • 0141726747 scopus 로고    scopus 로고
    • ATP dependent Ca2+ transport across basal membrane of human syncytiotrophoblast in pregnancies complicated by intrauterine growth restriction or diabetes
    • Strid H., Bucht E., Jansson T., Wennergren M., and Powell T.L. ATP dependent Ca2+ transport across basal membrane of human syncytiotrophoblast in pregnancies complicated by intrauterine growth restriction or diabetes. Placenta 24 (2003) 445-452
    • (2003) Placenta , vol.24 , pp. 445-452
    • Strid, H.1    Bucht, E.2    Jansson, T.3    Wennergren, M.4    Powell, T.L.5
  • 365
    • 0028329449 scopus 로고
    • Parallel mechanisms of Ca++ transfer across the perfused human placental cotyledon
    • Stulc J., Stulcova B., Smid M., and Sach I. Parallel mechanisms of Ca++ transfer across the perfused human placental cotyledon. Am. J. Obstet. Gynecol. 170 (1994) 162-167
    • (1994) Am. J. Obstet. Gynecol. , vol.170 , pp. 162-167
    • Stulc, J.1    Stulcova, B.2    Smid, M.3    Sach, I.4
  • 366
    • 17544398505 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis: Disease stage related changes of tau protein and S100 beta in cerebrospinal fluid and creatine kinase in serum
    • Sussmuth S.D., Tumani H., Ecker D., and Ludolph A.C. Amyotrophic lateral sclerosis: Disease stage related changes of tau protein and S100 beta in cerebrospinal fluid and creatine kinase in serum. Neurosci. Lett. 353 (2003) 57-60
    • (2003) Neurosci. Lett. , vol.353 , pp. 57-60
    • Sussmuth, S.D.1    Tumani, H.2    Ecker, D.3    Ludolph, A.C.4
  • 367
    • 0029737042 scopus 로고    scopus 로고
    • The role of macrophage migration inhibitory factor in pregnancy and development of murine embryos
    • Suzuki H., Nishihira J., Koyama Y., and Kanagawa H. The role of macrophage migration inhibitory factor in pregnancy and development of murine embryos. Biochem. Mol. Biol. Int. 38 (1996) 409-416
    • (1996) Biochem. Mol. Biol. Int. , vol.38 , pp. 409-416
    • Suzuki, H.1    Nishihira, J.2    Koyama, Y.3    Kanagawa, H.4
  • 368
    • 0030184941 scopus 로고    scopus 로고
    • Evidence for the presence of macrophage migration inhibitory factor in murine reproductive organs and early embryos
    • Suzuki H., Kanagawa H., and Nishihira J. Evidence for the presence of macrophage migration inhibitory factor in murine reproductive organs and early embryos. Immunol. Lett. 51 (1996) 141-147
    • (1996) Immunol. Lett. , vol.51 , pp. 141-147
    • Suzuki, H.1    Kanagawa, H.2    Nishihira, J.3
  • 371
    • 0032903244 scopus 로고    scopus 로고
    • Expression of calcium binding protein D-9k messenger RNA in the mouse uterine endometrium during implantation
    • Tatsumi K., Higuchi T., Fujiwara H., Nakayama T., Itoh K., Mori T., Fujii S., and Fujita J. Expression of calcium binding protein D-9k messenger RNA in the mouse uterine endometrium during implantation. Mol. Hum. Reprod. 5 (1999) 153-161
    • (1999) Mol. Hum. Reprod. , vol.5 , pp. 153-161
    • Tatsumi, K.1    Higuchi, T.2    Fujiwara, H.3    Nakayama, T.4    Itoh, K.5    Mori, T.6    Fujii, S.7    Fujita, J.8
  • 372
    • 0017600786 scopus 로고
    • Chick brain calcium binding protein: Response to cholecalciferol and some developmental aspects
    • Taylor A.N. Chick brain calcium binding protein: Response to cholecalciferol and some developmental aspects. J. Nutr. 107 (1977) 480-486
    • (1977) J. Nutr. , vol.107 , pp. 480-486
    • Taylor, A.N.1
  • 373
    • 0022341613 scopus 로고
    • Morphometric evaluation of the microvillous surface enlargement factor in the human placenta from mid-gestation to term
    • Teasdale F., and Jean-Jacques G. Morphometric evaluation of the microvillous surface enlargement factor in the human placenta from mid-gestation to term. Placenta 6 (1985) 375-381
    • (1985) Placenta , vol.6 , pp. 375-381
    • Teasdale, F.1    Jean-Jacques, G.2
  • 374
    • 0022596470 scopus 로고
    • Morphometry of the microvillous membrane of the human placenta in maternal diabetes mellitus
    • Teasdale F., and Jean-Jacques G. Morphometry of the microvillous membrane of the human placenta in maternal diabetes mellitus. Placenta 7 (1986) 81-88
    • (1986) Placenta , vol.7 , pp. 81-88
    • Teasdale, F.1    Jean-Jacques, G.2
  • 375
    • 0022981962 scopus 로고
    • Translational control of mRNA expression during the early mitogenic response in Swiss mouse 3T3 cells: Identification of specific proteins
    • Thomas G., and Thomas G. Translational control of mRNA expression during the early mitogenic response in Swiss mouse 3T3 cells: Identification of specific proteins. J. Cell Biol. 103 (1986) 2137-2144
    • (1986) J. Cell Biol. , vol.103 , pp. 2137-2144
    • Thomas, G.1    Thomas, G.2
  • 376
    • 0020435560 scopus 로고
    • Rat calcium-binding proteins: Distribution, development, and vitamin D dependence
    • Thomasset M., Parkes C.O., and Cuisinier-Gleizes P. Rat calcium-binding proteins: Distribution, development, and vitamin D dependence. Am. J. Physiol. 243 (1982) E483-E488
    • (1982) Am. J. Physiol. , vol.243
    • Thomasset, M.1    Parkes, C.O.2    Cuisinier-Gleizes, P.3
  • 377
    • 0025939353 scopus 로고
    • Purification and characterization of mouse decidual calcyclin: A novel stimulator of mouse placental lactogen-II secretion
    • Thordarson G., Southard J.N., and Talamantes F. Purification and characterization of mouse decidual calcyclin: A novel stimulator of mouse placental lactogen-II secretion. Endocrinology 129 (1991) 1257-1265
    • (1991) Endocrinology , vol.129 , pp. 1257-1265
    • Thordarson, G.1    Southard, J.N.2    Talamantes, F.3
  • 379
    • 0026043539 scopus 로고
    • Purification, characterization, and partial sequence analysis of a newly identified EF-hand type 13-kDa Ca(2+)-binding protein from smooth muscle and non-muscle tissues
    • Todoroki H., Kobayashi R., Watanabe M., Minami H., and Hidaka H. Purification, characterization, and partial sequence analysis of a newly identified EF-hand type 13-kDa Ca(2+)-binding protein from smooth muscle and non-muscle tissues. J. Biol. Chem. 266 (1991) 18668-18673
    • (1991) J. Biol. Chem. , vol.266 , pp. 18668-18673
    • Todoroki, H.1    Kobayashi, R.2    Watanabe, M.3    Minami, H.4    Hidaka, H.5
  • 381
    • 0019970098 scopus 로고
    • Identification and characterization of a calcium-binding protein from human placenta
    • Tuan R.S. Identification and characterization of a calcium-binding protein from human placenta. Placenta 3 (1982) 145-158
    • (1982) Placenta , vol.3 , pp. 145-158
    • Tuan, R.S.1
  • 382
    • 0021893599 scopus 로고
    • Ca2+-binding protein of the human placenta. Characterization, immunohistochemical localization and functional involvement in Ca2+ transport
    • Tuan R.S. Ca2+-binding protein of the human placenta. Characterization, immunohistochemical localization and functional involvement in Ca2+ transport. Biochem. J. 227 (1985) 317-326
    • (1985) Biochem. J. , vol.227 , pp. 317-326
    • Tuan, R.S.1
  • 383
    • 0025186044 scopus 로고
    • Ca(2+)-activated ATPase of the mouse chorioallantoic placenta: Developmental expression, characterization and cytohistochemical localization
    • Tuan R.S., and Bigioni N. Ca(2+)-activated ATPase of the mouse chorioallantoic placenta: Developmental expression, characterization and cytohistochemical localization. Development 110 (1990) 505-513
    • (1990) Development , vol.110 , pp. 505-513
    • Tuan, R.S.1    Bigioni, N.2
  • 384
    • 0023920575 scopus 로고
    • Mouse placental 57-kDa calcium-binding protein: I. Cloning of cDNA and characterization of developmental expression
    • Tuan R.S., and Kirwin J.J. Mouse placental 57-kDa calcium-binding protein: I. Cloning of cDNA and characterization of developmental expression. Differentiation 37 (1988) 98-103
    • (1988) Differentiation , vol.37 , pp. 98-103
    • Tuan, R.S.1    Kirwin, J.J.2
  • 385
    • 0023106764 scopus 로고
    • Calcium-activated ATPase of the human placenta: Identification, characterization, and functional involvement in calcium transport
    • Tuan R.S., and Kushner T. Calcium-activated ATPase of the human placenta: Identification, characterization, and functional involvement in calcium transport. Placenta 8 (1987) 53-64
    • (1987) Placenta , vol.8 , pp. 53-64
    • Tuan, R.S.1    Kushner, T.2
  • 387
    • 4344701254 scopus 로고    scopus 로고
    • Calcium homeostasis during pregnancy and lactation in Brazilian women with low calcium intakes: A longitudinal study
    • Vargas Zapata C.L., Donangelo C.M., Woodhouse L.R., Abrams S.A., Spencer E.M., and King J.C. Calcium homeostasis during pregnancy and lactation in Brazilian women with low calcium intakes: A longitudinal study. Am. J. Clin. Nutr. 80 (2004) 417-422
    • (2004) Am. J. Clin. Nutr. , vol.80 , pp. 417-422
    • Vargas Zapata, C.L.1    Donangelo, C.M.2    Woodhouse, L.R.3    Abrams, S.A.4    Spencer, E.M.5    King, J.C.6
  • 388
    • 0037337639 scopus 로고    scopus 로고
    • Mg2+-dependent gating and strong inward rectification of the cation channel TRPV6
    • Voets T., Janssens A., Prenen J., Droogmans G., and Nilius B. Mg2+-dependent gating and strong inward rectification of the cation channel TRPV6. J. Gen. Physiol. 121 (2003) 245-260
    • (2003) J. Gen. Physiol. , vol.121 , pp. 245-260
    • Voets, T.1    Janssens, A.2    Prenen, J.3    Droogmans, G.4    Nilius, B.5
  • 389
    • 0026074356 scopus 로고
    • The calmodulin-binding domain mediates the self-association of the plasma membrane Ca2+ pump
    • Vorherr T., Kessler T., Hofmann F., and Carafoli E. The calmodulin-binding domain mediates the self-association of the plasma membrane Ca2+ pump. J. Biol. Chem. 266 (1991) 22-27
    • (1991) J. Biol. Chem. , vol.266 , pp. 22-27
    • Vorherr, T.1    Kessler, T.2    Hofmann, F.3    Carafoli, E.4
  • 390
    • 0030941067 scopus 로고    scopus 로고
    • Macrophage migration inhibitory factor in the human ovary: Presence in the follicular fluids and production by granulosa cells
    • Wada S., Fujimoto S., Mizue Y., and Nishihira J. Macrophage migration inhibitory factor in the human ovary: Presence in the follicular fluids and production by granulosa cells. Biochem. Mol. Biol. Int. 41 (1997) 805-814
    • (1997) Biochem. Mol. Biol. Int. , vol.41 , pp. 805-814
    • Wada, S.1    Fujimoto, S.2    Mizue, Y.3    Nishihira, J.4
  • 391
    • 0031748657 scopus 로고    scopus 로고
    • T-type and L-type calcium channel blockers exert opposite effects on renin secretion and renin gene expression in conscious rats
    • Wagner C., Kramer B.K., Hinder M., Kieninger M., and Kurtz A. T-type and L-type calcium channel blockers exert opposite effects on renin secretion and renin gene expression in conscious rats. Br. J. Pharmacol. 124 (1998) 579-585
    • (1998) Br. J. Pharmacol. , vol.124 , pp. 579-585
    • Wagner, C.1    Kramer, B.K.2    Hinder, M.3    Kieninger, M.4    Kurtz, A.5
  • 392
    • 0027525382 scopus 로고
    • Single-channel analysis of a cloned human heart L-type Ca2+ channel alpha 1 subunit and the effects of a cardiac beta subunit
    • Wakamori M., Mikala G., Schwartz A., and Yatani A. Single-channel analysis of a cloned human heart L-type Ca2+ channel alpha 1 subunit and the effects of a cardiac beta subunit. Biochem. Biophys. Res. Commun. 196 (1993) 1170-1176
    • (1993) Biochem. Biophys. Res. Commun. , vol.196 , pp. 1170-1176
    • Wakamori, M.1    Mikala, G.2    Schwartz, A.3    Yatani, A.4
  • 394
    • 0023276320 scopus 로고
    • Cellular junctions on the free surface of human placental syncytium
    • Wang T., and Schneider J. Cellular junctions on the free surface of human placental syncytium. Arch. Gynecol. 240 (1987) 211-216
    • (1987) Arch. Gynecol. , vol.240 , pp. 211-216
    • Wang, T.1    Schneider, J.2
  • 395
    • 0023132416 scopus 로고
    • Analysis and in situ detection of cholecalcin messenger RNA (9000 Mr CaBP) in the uterus of the pregnant rat
    • Warembourg M., Perret C., and Thomasset M. Analysis and in situ detection of cholecalcin messenger RNA (9000 Mr CaBP) in the uterus of the pregnant rat. Cell Tissue Res. 247 (1987) 51-57
    • (1987) Cell Tissue Res. , vol.247 , pp. 51-57
    • Warembourg, M.1    Perret, C.2    Thomasset, M.3
  • 396
    • 0024540461 scopus 로고
    • On the molecular mechanism of intestinal calcium transport
    • Wasserman R.H., and Fullmer C.S. On the molecular mechanism of intestinal calcium transport. Adv. Exp. Med. Biol. 249 (1989) 45-65
    • (1989) Adv. Exp. Med. Biol. , vol.249 , pp. 45-65
    • Wasserman, R.H.1    Fullmer, C.S.2
  • 397
    • 0013937404 scopus 로고
    • Vitamin D and transfer of plasma calcium to intestinal lumen in chicks and rats
    • Wasserman R.H., Taylor A.N., and Kallfelz F.A. Vitamin D and transfer of plasma calcium to intestinal lumen in chicks and rats. Am. J. Physiol. 211 (1966) 419-423
    • (1966) Am. J. Physiol. , vol.211 , pp. 419-423
    • Wasserman, R.H.1    Taylor, A.N.2    Kallfelz, F.A.3
  • 398
    • 0026734754 scopus 로고
    • Regulated temporal and spatial expression of the calcium-binding proteins calcyclin and OPN (osteopontin) in mouse tissues during pregnancy
    • Waterhouse P., Parhar R.S., Guo X., Lala P.K., and Denhardt D.T. Regulated temporal and spatial expression of the calcium-binding proteins calcyclin and OPN (osteopontin) in mouse tissues during pregnancy. Mol. Reprod. Dev. 32 (1992) 315-323
    • (1992) Mol. Reprod. Dev. , vol.32 , pp. 315-323
    • Waterhouse, P.1    Parhar, R.S.2    Guo, X.3    Lala, P.K.4    Denhardt, D.T.5
  • 399
    • 0023741187 scopus 로고
    • Influence of season and latitude on the cutaneous synthesis of vitamin D3: Exposure to winter sunlight in Boston and Edmonton will not promote vitamin D3 synthesis in human skin
    • Webb A.R., Kline L., and Holick M.F. Influence of season and latitude on the cutaneous synthesis of vitamin D3: Exposure to winter sunlight in Boston and Edmonton will not promote vitamin D3 synthesis in human skin. J. Clin. Endocrinol. Metab. 67 (1988) 373-378
    • (1988) J. Clin. Endocrinol. Metab. , vol.67 , pp. 373-378
    • Webb, A.R.1    Kline, L.2    Holick, M.F.3
  • 400
    • 0035930968 scopus 로고    scopus 로고
    • Gene structure and regulation of the murine epithelial calcium channels ECaC1 and 2
    • Weber K., Erben R.G., Rump A., and Adamski J. Gene structure and regulation of the murine epithelial calcium channels ECaC1 and 2. Biochem. Biophys. Res. Commun. 289 (2001) 1287-1294
    • (2001) Biochem. Biophys. Res. Commun. , vol.289 , pp. 1287-1294
    • Weber, K.1    Erben, R.G.2    Rump, A.3    Adamski, J.4
  • 401
    • 15244356572 scopus 로고    scopus 로고
    • Vitamin D deficiency and whole-body and femur bone mass relative to weight in healthy newborns
    • Weiler H., Fitzpatrick-Wong S., Veitch R., Kovacs H., Schellenberg J., McCloy U., and Yuen C.K. Vitamin D deficiency and whole-body and femur bone mass relative to weight in healthy newborns. Cmaj 172 (2005) 757-761
    • (2005) Cmaj , vol.172 , pp. 757-761
    • Weiler, H.1    Fitzpatrick-Wong, S.2    Veitch, R.3    Kovacs, H.4    Schellenberg, J.5    McCloy, U.6    Yuen, C.K.7
  • 402
    • 0000834861 scopus 로고
    • Biology of implantation
    • Knobil E., and Neill J.D. (Eds), Lippincott Williams & Wilkins, New York
    • Weitlauf H.M. Biology of implantation. In: Knobil E., and Neill J.D. (Eds). "The Physiology of Reproduction" (1988), Lippincott Williams & Wilkins, New York 231-262
    • (1988) "The Physiology of Reproduction" , pp. 231-262
    • Weitlauf, H.M.1
  • 405
    • 0345643514 scopus 로고    scopus 로고
    • Regulation of matrix metalloproteinase expression in tumor invasion
    • Westermarck J., and Kahari V.M. Regulation of matrix metalloproteinase expression in tumor invasion. FASEB J. 13 (1999) 781-792
    • (1999) FASEB J. , vol.13 , pp. 781-792
    • Westermarck, J.1    Kahari, V.M.2
  • 406
  • 412
    • 3042807960 scopus 로고    scopus 로고
    • 1,25-Dihydroxyvitamin D3 increases the expression of the CaT1 epithelial calcium channel in the Caco-2 human intestinal cell line
    • Wood R.J., Tchack L., and Taparia S. 1,25-Dihydroxyvitamin D3 increases the expression of the CaT1 epithelial calcium channel in the Caco-2 human intestinal cell line. BMC Physiol. 1 (2001) 11
    • (2001) BMC Physiol. , vol.1 , pp. 11
    • Wood, R.J.1    Tchack, L.2    Taparia, S.3
  • 413
    • 0023770171 scopus 로고
    • Molecular cloning of mammalian 28,000 Mr vitamin D-dependent calcium binding protein (calbindin-D28K): Expression of calbindin-D28K RNAs in rodent brain and kidney
    • Wood T.L., Kobayashi Y., Frantz G., Varghese S., Christakos S., and Tobin A.J. Molecular cloning of mammalian 28,000 Mr vitamin D-dependent calcium binding protein (calbindin-D28K): Expression of calbindin-D28K RNAs in rodent brain and kidney. Dna 7 (1988) 585-593
    • (1988) Dna , vol.7 , pp. 585-593
    • Wood, T.L.1    Kobayashi, Y.2    Frantz, G.3    Varghese, S.4    Christakos, S.5    Tobin, A.J.6
  • 414
    • 0030814032 scopus 로고    scopus 로고
    • P11, a unique member of the S100 family of calcium-binding proteins, interacts with and inhibits the activity of the 85-kDa cytosolic phospholipase A2
    • Wu T., Angus C.W., Yao X.L., Logun C., and Shelhamer J.H. P11, a unique member of the S100 family of calcium-binding proteins, interacts with and inhibits the activity of the 85-kDa cytosolic phospholipase A2. J. Biol. Chem. 272 (1997) 17145-17153
    • (1997) J. Biol. Chem. , vol.272 , pp. 17145-17153
    • Wu, T.1    Angus, C.W.2    Yao, X.L.3    Logun, C.4    Shelhamer, J.H.5
  • 415
    • 0031916976 scopus 로고    scopus 로고
    • The physiology of parathyroid hormone-related protein: An emerging role as a developmental factor
    • Wysolmerski J.J., and Stewart A.F. The physiology of parathyroid hormone-related protein: An emerging role as a developmental factor. Annu. Rev. Physiol. 60 (1998) 431-460
    • (1998) Annu. Rev. Physiol. , vol.60 , pp. 431-460
    • Wysolmerski, J.J.1    Stewart, A.F.2
  • 416
    • 0033568290 scopus 로고    scopus 로고
    • Expression of translationally controlled tumour protein is regulated by calcium at both the transcriptional and post-transcriptional level
    • Xu A., Bellamy A.R., and Taylor J.A. Expression of translationally controlled tumour protein is regulated by calcium at both the transcriptional and post-transcriptional level. Biochem. J. 342 Pt. 3 (1999) 683-689
    • (1999) Biochem. J. , vol.342 , Issue.PART 3 , pp. 683-689
    • Xu, A.1    Bellamy, A.R.2    Taylor, J.A.3
  • 417
    • 0036184515 scopus 로고    scopus 로고
    • Calcium channels-4basic aspects of their structure, function and gene encoding; anesthetic action on the channels-a review
    • Yamakage M., and Namiki A. Calcium channels-4basic aspects of their structure, function and gene encoding; anesthetic action on the channels-a review. Can. J. Anaesth. 49 (2002) 151-164
    • (2002) Can. J. Anaesth. , vol.49 , pp. 151-164
    • Yamakage, M.1    Namiki, A.2
  • 418
    • 0027205380 scopus 로고
    • The major binding protein of the interferon antagonist sarcolectin in human placenta is a macrophage migration inhibitory factor
    • Zeng F.Y., Weiser W.Y., Kratzin H., Stahl B., Karas M., and Gabius H.J. The major binding protein of the interferon antagonist sarcolectin in human placenta is a macrophage migration inhibitory factor. Arch. Biochem. Biophys. 303 (1993) 74-80
    • (1993) Arch. Biochem. Biophys. , vol.303 , pp. 74-80
    • Zeng, F.Y.1    Weiser, W.Y.2    Kratzin, H.3    Stahl, B.4    Karas, M.5    Gabius, H.J.6
  • 419
    • 0035918158 scopus 로고    scopus 로고
    • Muscarinic acetylcholine receptor regulation of TRP6 Ca2+ channel isoforms. Molecular structures and functional characterization
    • Zhang L., and Saffen D. Muscarinic acetylcholine receptor regulation of TRP6 Ca2+ channel isoforms. Molecular structures and functional characterization. J. Biol. Chem. 276 (2001) 13331-13339
    • (2001) J. Biol. Chem. , vol.276 , pp. 13331-13339
    • Zhang, L.1    Saffen, D.2
  • 420
    • 0030922747 scopus 로고    scopus 로고
    • Human cytotrophoblasts adopt a vascular phenotype as they differentiate. A strategy for successful endovascular invasion?
    • Zhou Y., Fisher S.J., Janatpour M., Genbacev O., Dejana E., Wheelock M., and Damsky C.H. Human cytotrophoblasts adopt a vascular phenotype as they differentiate. A strategy for successful endovascular invasion?. J. Clin. Invest. 99 (1997) 2139-2151
    • (1997) J. Clin. Invest. , vol.99 , pp. 2139-2151
    • Zhou, Y.1    Fisher, S.J.2    Janatpour, M.3    Genbacev, O.4    Dejana, E.5    Wheelock, M.6    Damsky, C.H.7
  • 421
    • 0029994314 scopus 로고    scopus 로고
    • trp, a novel mammalian gene family essential for agonist-activated capacitative Ca2+ entry
    • Zhu X., Jiang M., Peyton M., Boulay G., Hurst R., Stefani E., and Birnbaumer L. trp, a novel mammalian gene family essential for agonist-activated capacitative Ca2+ entry. Cell 85 (1996) 661-671
    • (1996) Cell , vol.85 , pp. 661-671
    • Zhu, X.1    Jiang, M.2    Peyton, M.3    Boulay, G.4    Hurst, R.5    Stefani, E.6    Birnbaumer, L.7
  • 422
    • 0031594711 scopus 로고    scopus 로고
    • Receptor-activated Ca2+ influx via human Trp3 stably expressed in human embryonic kidney (HEK)293 cells. Evidence for a non-capacitative Ca2+ entry
    • Zhu X., Jiang M., and Birnbaumer L. Receptor-activated Ca2+ influx via human Trp3 stably expressed in human embryonic kidney (HEK)293 cells. Evidence for a non-capacitative Ca2+ entry. J. Biol. Chem. 273 (1998) 133-142
    • (1998) J. Biol. Chem. , vol.273 , pp. 133-142
    • Zhu, X.1    Jiang, M.2    Birnbaumer, L.3
  • 423
    • 0022976875 scopus 로고
    • Identification of a molecular target for the calcium-modulated protein S100. Fructose-1,6-bisphosphate aldolase
    • Zimmer D.B., and Van Eldik L.J. Identification of a molecular target for the calcium-modulated protein S100. Fructose-1,6-bisphosphate aldolase. J. Biol. Chem. 261 (1986) 11424-11428
    • (1986) J. Biol. Chem. , vol.261 , pp. 11424-11428
    • Zimmer, D.B.1    Van Eldik, L.J.2
  • 424
    • 0028928357 scopus 로고
    • The S100 protein family: History, function, and expression
    • Zimmer D.B., Cornwall E.H., Landar A., and Song W. The S100 protein family: History, function, and expression. Brain Res. Bull. 37 (1995) 417-429
    • (1995) Brain Res. Bull. , vol.37 , pp. 417-429
    • Zimmer, D.B.1    Cornwall, E.H.2    Landar, A.3    Song, W.4
  • 425
    • 0027336649 scopus 로고
    • Mitogen-regulated Ca2+ current of T lymphocytes is activated by depletion of intracellular Ca2+ stores
    • Zweifach A., and Lewis R.S. Mitogen-regulated Ca2+ current of T lymphocytes is activated by depletion of intracellular Ca2+ stores. Proc. Natl. Acad. Sci. USA 90 (1993) 6295-6299
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 6295-6299
    • Zweifach, A.1    Lewis, R.S.2
  • 426
    • 0036960028 scopus 로고    scopus 로고
    • The isoform- and location-dependence of the functioning of the plasma membrane calcium pump
    • Zylinska L., Kawecka I., Lachowicz L., and Szemraj J. The isoform- and location-dependence of the functioning of the plasma membrane calcium pump. Cell. Mol. Biol. Lett. 7 (2002) 1037-1045
    • (2002) Cell. Mol. Biol. Lett. , vol.7 , pp. 1037-1045
    • Zylinska, L.1    Kawecka, I.2    Lachowicz, L.3    Szemraj, J.4


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