메뉴 건너뛰기




Volumn , Issue , 2003, Pages 651-678

Hypophosphatasia

Author keywords

[No Author keywords available]

Indexed keywords


EID: 2342645617     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-012286551-0/50029-4     Document Type: Chapter
Times cited : (11)

References (223)
  • 1
    • 0001587178 scopus 로고
    • Mutations affecting bone-forming cells
    • Telford, Baltimore, B.K. Hall (Ed.)
    • Cole D.E., Cohen M.M. Mutations affecting bone-forming cells. The Osteoblast and Osteocyte 1990, 431-487. Telford, Baltimore. B.K. Hall (Ed.).
    • (1990) The Osteoblast and Osteocyte , pp. 431-487
    • Cole, D.E.1    Cohen, M.M.2
  • 2
    • 0027930471 scopus 로고
    • Hypophosphatasia and the role of alkaline phosphatase in skeletal mineralization
    • Whyte M.P. Hypophosphatasia and the role of alkaline phosphatase in skeletal mineralization. Endocr. Rev. 1994, 15:439-461.
    • (1994) Endocr. Rev. , vol.15 , pp. 439-461
    • Whyte, M.P.1
  • 4
    • 0001594259 scopus 로고    scopus 로고
    • Hypophosphatasia
    • McGraw-Hill, Totowa, NJ, C.R. Scriver, A.L. Beaudet, W.S. Sly, D. Valle, B. Childs, K.W. Kinzler, B. Vogelstein (Eds.), 8th ed.
    • Whyte M.P. Hypophosphatasia. The Metabolic and Molecular Bases of Inherited Disease 2001, 5313-5329. McGraw-Hill, Totowa, NJ. 8th ed. C.R. Scriver, A.L. Beaudet, W.S. Sly, D. Valle, B. Childs, K.W. Kinzler, B. Vogelstein (Eds.).
    • (2001) The Metabolic and Molecular Bases of Inherited Disease , pp. 5313-5329
    • Whyte, M.P.1
  • 5
    • 0019989821 scopus 로고
    • Alkaline phosphatase isoenzymes
    • Moss D.W. Alkaline phosphatase isoenzymes. Clin. Chem. 1982, 28:2007-2016.
    • (1982) Clin. Chem. , vol.28 , pp. 2007-2016
    • Moss, D.W.1
  • 8
    • 0025181742 scopus 로고
    • Structure of alkaline phosphatases
    • Kim E.E., Wyckoff H.W. Structure of alkaline phosphatases. Clin. Chim. Acta 1989, 186:175-187.
    • (1989) Clin. Chim. Acta , vol.186 , pp. 175-187
    • Kim, E.E.1    Wyckoff, H.W.2
  • 9
    • 0022446237 scopus 로고
    • Nucleotide sequence of the alkaline phosphatase gene of Escherichia coli
    • Chang C.N., Kuang W.J., Chen E.Y. Nucleotide sequence of the alkaline phosphatase gene of Escherichia coli. Gene 1986, 44:121-125.
    • (1986) Gene , vol.44 , pp. 121-125
    • Chang, C.N.1    Kuang, W.J.2    Chen, E.Y.3
  • 10
    • 0023354335 scopus 로고
    • Alkaline phosphatase which lacks its own signal sequence becomes enzymatically active when fused to N-terminal sequences of Escherichia coli haemolysin (HlyA)
    • Erb K., Vogel M., Wagner W., Goebel W. Alkaline phosphatase which lacks its own signal sequence becomes enzymatically active when fused to N-terminal sequences of Escherichia coli haemolysin (HlyA). Mol Gen. Genet. 1987, 208:88-93.
    • (1987) Mol Gen. Genet. , vol.208 , pp. 88-93
    • Erb, K.1    Vogel, M.2    Wagner, W.3    Goebel, W.4
  • 11
    • 0023708995 scopus 로고
    • Alteration of the amino terminus of the mature sequence of a periplasmic protein can severely affect protein export in Escherichia coli
    • Li P., Beckwith J., Inouye H. Alteration of the amino terminus of the mature sequence of a periplasmic protein can severely affect protein export in Escherichia coli. Proc. Natl. Acad. Sci. USA 1988, 85:7685-7689.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 7685-7689
    • Li, P.1    Beckwith, J.2    Inouye, H.3
  • 13
    • 0023600057 scopus 로고
    • Nucleotide sequence of the iap gene, responsible for alkaline phosphatase isozyme conversion in Escherichia coli, and identification of the gene product
    • Ishino Y., Shinagawa H., Makino K., Amemura M., Nakata A. Nucleotide sequence of the iap gene, responsible for alkaline phosphatase isozyme conversion in Escherichia coli, and identification of the gene product. J.Bacteriol. 1987, 169:5429-5433.
    • (1987) J.Bacteriol. , vol.169 , pp. 5429-5433
    • Ishino, Y.1    Shinagawa, H.2    Makino, K.3    Amemura, M.4    Nakata, A.5
  • 14
    • 0030965606 scopus 로고    scopus 로고
    • Roles of disulfide bonds in bacterial alkaline phosphatase
    • Sone M., Kishigami S., Yoshihisa T., Ito K. Roles of disulfide bonds in bacterial alkaline phosphatase. J.Biol. Chem. 1997, 272:6174-6178.
    • (1997) J.Biol. Chem. , vol.272 , pp. 6174-6178
    • Sone, M.1    Kishigami, S.2    Yoshihisa, T.3    Ito, K.4
  • 16
    • 0027468143 scopus 로고
    • Magnesium in the active site of Escher- ichia coli alkaline phosphatase is important for both structural stabilization and catalysis
    • Janeway C.M., Xu X., Murphy J.E., Chaidaroglou A., Kantrowitz E.R. Magnesium in the active site of Escher- ichia coli alkaline phosphatase is important for both structural stabilization and catalysis. Biochemistry 1993, 32:1601-1609.
    • (1993) Biochemistry , vol.32 , pp. 1601-1609
    • Janeway, C.M.1    Xu, X.2    Murphy, J.E.3    Chaidaroglou, A.4    Kantrowitz, E.R.5
  • 17
    • 0034705337 scopus 로고    scopus 로고
    • A revised mechanism for the alkaline phosphatase reaction involving three metal ions
    • Stec B., Holtz K.M., Kantrowitz E.R. A revised mechanism for the alkaline phosphatase reaction involving three metal ions. J.Mol. Biol. 2000, 299:1303-1311.
    • (2000) J.Mol. Biol. , vol.299 , pp. 1303-1311
    • Stec, B.1    Holtz, K.M.2    Kantrowitz, E.R.3
  • 18
    • 0025777694 scopus 로고
    • Reaction mechanism of alkaline phosphatase based on crystal structures. Two-metal ion catalysis
    • Kim E.E., Wyckoff H.W. Reaction mechanism of alkaline phosphatase based on crystal structures. Two-metal ion catalysis. J.Mol Biol 1991, 218:449-464.
    • (1991) J.Mol Biol , vol.218 , pp. 449-464
    • Kim, E.E.1    Wyckoff, H.W.2
  • 19
    • 0025977645 scopus 로고
    • Bacillus subtilis alkaline phos- phatases III and IV. Cloning, sequencing, and comparisons of deduced amino acid sequence with Escherichia coli alkaline phosp
    • Hulett F.M., Kim E.E., Bookstein C., Kapp N.V., Edwards C.W., Wyckoff H.W. Bacillus subtilis alkaline phos- phatases III and IV. Cloning, sequencing, and comparisons of deduced amino acid sequence with Escherichia coli alkaline phosp. J.Biol. Chem. 1991, 266:1077-1084.
    • (1991) J.Biol. Chem. , vol.266 , pp. 1077-1084
    • Hulett, F.M.1    Kim, E.E.2    Bookstein, C.3    Kapp, N.V.4    Edwards, C.W.5    Wyckoff, H.W.6
  • 20
    • 0023515035 scopus 로고
    • Structural characteristics of the PHO8 gene encoding repressible alkaline phosphatase in Saccharomyces cerevisiae
    • Kaneko Y., Hayashi N., Toh-e A., Banno I., Oshima Y. Structural characteristics of the PHO8 gene encoding repressible alkaline phosphatase in Saccharomyces cerevisiae. Gene 1987, 58:137-148.
    • (1987) Gene , vol.58 , pp. 137-148
    • Kaneko, Y.1    Hayashi, N.2    Toh-e, A.3    Banno, I.4    Oshima, Y.5
  • 21
    • 0027944629 scopus 로고
    • Stage-specific expression of alkaline phosphatase during neural development in the mouse
    • Narisawa S., Hasegawa H., Watanabe K., Millan J.L. Stage-specific expression of alkaline phosphatase during neural development in the mouse. Dev. Dyn. 1994, 201:227-235.
    • (1994) Dev. Dyn. , vol.201 , pp. 227-235
    • Narisawa, S.1    Hasegawa, H.2    Watanabe, K.3    Millan, J.L.4
  • 22
    • 0025285987 scopus 로고
    • Isol- ation and characterization of the mouse liver/bone/kidney-type alkaline phosphatase gene
    • Terao M., Studer M., Gianni M., Garattini E. Isol- ation and characterization of the mouse liver/bone/kidney-type alkaline phosphatase gene. Biochem. J. 1990, 268:641-648.
    • (1990) Biochem. J. , vol.268 , pp. 641-648
    • Terao, M.1    Studer, M.2    Gianni, M.3    Garattini, E.4
  • 23
    • 0022991723 scopus 로고
    • Comparative biochemical study of alkaline phosphatase isozymes in fish, amphibians, reptiles, birds and mammals
    • Yora T., Sakagishi Y. Comparative biochemical study of alkaline phosphatase isozymes in fish, amphibians, reptiles, birds and mammals. Comp. Biochem. Physiol. B 1986, 85:649-658.
    • (1986) Comp. Biochem. Physiol. B , vol.85 , pp. 649-658
    • Yora, T.1    Sakagishi, Y.2
  • 24
    • 0022641144 scopus 로고
    • Ontogenic and phylogenic studies of intestinal, hepatic, and placental alkaline phosphatases. Evidence that intestinal alkaline phosphatase is a late evolutio
    • Komoda T., Koyama L., Nagata A., Sakagishi Y., DeSchryver- Kecskemeti K., Alpers D.H. Ontogenic and phylogenic studies of intestinal, hepatic, and placental alkaline phosphatases. Evidence that intestinal alkaline phosphatase is a late evolutio. Gastroenterology 1986, 91:277-286.
    • (1986) Gastroenterology , vol.91 , pp. 277-286
    • Komoda, T.1    Koyama, L.2    Nagata, A.3    Sakagishi, Y.4    DeSchryver-Kecskemeti, K.5    Alpers, D.H.6
  • 25
    • 0025223838 scopus 로고
    • Genomic structure and comparison of mouse tissue-specific alkaline phosphatase genes
    • Manes T., Glade K., Ziomek C.A., Millan J.L. Genomic structure and comparison of mouse tissue-specific alkaline phosphatase genes. Genomics 1990, 8:541-554.
    • (1990) Genomics , vol.8 , pp. 541-554
    • Manes, T.1    Glade, K.2    Ziomek, C.A.3    Millan, J.L.4
  • 26
    • 0024846465 scopus 로고
    • Localization of two alkaline phosphatase genes to the proximal region of mouse chromosome 1
    • Schurr E., Henthorn P.S., Harris H., Skamene E., Gros P. Localization of two alkaline phosphatase genes to the proximal region of mouse chromosome 1. Cytogenet. Cell. Genet. 1989, 52:65-67.
    • (1989) Cytogenet. Cell. Genet. , vol.52 , pp. 65-67
    • Schurr, E.1    Henthorn, P.S.2    Harris, H.3    Skamene, E.4    Gros, P.5
  • 27
    • 0021664741 scopus 로고
    • Present status and future trends of human alkaline phosphatases
    • Stigbrand T. Present status and future trends of human alkaline phosphatases. Prog. Clin. Biol. Res. 1984, 166:3-14.
    • (1984) Prog. Clin. Biol. Res. , vol.166 , pp. 3-14
    • Stigbrand, T.1
  • 28
    • 0022970889 scopus 로고
    • Molecular cloning and sequence analysis ofhuman placental alkaline phosphatase
    • Millan J.L. Molecular cloning and sequence analysis ofhuman placental alkaline phosphatase. J.Biol. Chem. 1986, 261:3112-3115.
    • (1986) J.Biol. Chem. , vol.261 , pp. 3112-3115
    • Millan, J.L.1
  • 30
    • 0021007961 scopus 로고
    • Applications of monoclonal antibodies in enzyme genetics
    • Harris H. Applications of monoclonal antibodies in enzyme genetics. Annu. Rev. Genet. 1983, 17:279-314.
    • (1983) Annu. Rev. Genet. , vol.17 , pp. 279-314
    • Harris, H.1
  • 31
    • 0023578909 scopus 로고
    • Two gene duplication events in the evolution of the human heat-stable alkaline phosphatases
    • Knoll B.J., Rothblum K.N., Longley M. Two gene duplication events in the evolution of the human heat-stable alkaline phosphatases. Gene 1987, 60:267-276.
    • (1987) Gene , vol.60 , pp. 267-276
    • Knoll, B.J.1    Rothblum, K.N.2    Longley, M.3
  • 32
    • 0023939569 scopus 로고
    • Seminoma-derived Nagaoisozyme is encoded by a germ-cell alkaline phosphatase gene
    • Millan J.L., Manes T. Seminoma-derived Nagaoisozyme is encoded by a germ-cell alkaline phosphatase gene. Proc. Natl. Acad. Sci. USA 1988, 85:3024-3028.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 3024-3028
    • Millan, J.L.1    Manes, T.2
  • 36
    • 0023104842 scopus 로고
    • Partial characterization of human ileal alkaline phosphatase: Differences between human ileal and duodenal enzymes
    • Miura M., Matsuzaki H., Sakagishi Y., Komoda T. Partial characterization of human ileal alkaline phosphatase: Differences between human ileal and duodenal enzymes. Clin. Chim. Ada 1987, 163:279-287.
    • (1987) Clin. Chim. Ada , vol.163 , pp. 279-287
    • Miura, M.1    Matsuzaki, H.2    Sakagishi, Y.3    Komoda, T.4
  • 42
    • 0025367098 scopus 로고
    • Characterization of a 5'-flanking region of the human liverJboneJkidney alkaline phosphatase gene: Two kinds of mRNA from a single gene
    • Matsuura S., Kishi F., Kajii T. Characterization of a 5'-flanking region of the human liverJboneJkidney alkaline phosphatase gene: Two kinds of mRNA from a single gene. Biochem. Biophys. Res. Commun. 1990, 168:993-1000.
    • (1990) Biochem. Biophys. Res. Commun. , vol.168 , pp. 993-1000
    • Matsuura, S.1    Kishi, F.2    Kajii, T.3
  • 43
    • 0031036060 scopus 로고    scopus 로고
    • Human tissue non-specific alkaline phosphatases: Sugar-moiety-induced enzymic and antigenic modulations and genetic aspects
    • Nosjean O., Koyama I., Goseki M., Roux B., Komoda T. Human tissue non-specific alkaline phosphatases: Sugar-moiety-induced enzymic and antigenic modulations and genetic aspects. Biochem. J. 1997, 321:297-303. (Pt. 2).
    • (1997) Biochem. J. , vol.321 , Issue.2 PT , pp. 297-303
    • Nosjean, O.1    Koyama, I.2    Goseki, M.3    Roux, B.4    Komoda, T.5
  • 45
    • 0035202335 scopus 로고    scopus 로고
    • Putting its fingers on stressful situations: The heavy metal-regulatory transcription factor MTF-1
    • Lichtlen P., Schaffner W. Putting its fingers on stressful situations: The heavy metal-regulatory transcription factor MTF-1. Bioessays 2001, 23:1010-1017.
    • (2001) Bioessays , vol.23 , pp. 1010-1017
    • Lichtlen, P.1    Schaffner, W.2
  • 46
    • 0026517635 scopus 로고
    • Site-specific mutations in the COOH-terminus of placental alkaline phosphatase: A single amino acid change converts a phosphatidylinositol-glycan-anchored pro
    • Lowe M.E. Site-specific mutations in the COOH-terminus of placental alkaline phosphatase: A single amino acid change converts a phosphatidylinositol-glycan-anchored pro. J.Cell Biol. 1992, 116:799-807.
    • (1992) J.Cell Biol. , vol.116 , pp. 799-807
    • Lowe, M.E.1
  • 47
    • 0023654822 scopus 로고
    • Biochemistry of the glycosyl-phosphatidylinositol membrane protein anchors
    • Low M.G. Biochemistry of the glycosyl-phosphatidylinositol membrane protein anchors. Biochem. J. 1987, 244:1-13.
    • (1987) Biochem. J. , vol.244 , pp. 1-13
    • Low, M.G.1
  • 48
    • 0030885251 scopus 로고    scopus 로고
    • Mammalian GPI proteins: Sorting, membrane residence and functions
    • Nosjean O., Briolay A., Roux B. Mammalian GPI proteins: Sorting, membrane residence and functions. Biochim. Biophys. Acta 1997, 1331:153-186.
    • (1997) Biochim. Biophys. Acta , vol.1331 , pp. 153-186
    • Nosjean, O.1    Briolay, A.2    Roux, B.3
  • 49
    • 0023976289 scopus 로고
    • Aspartic acid-484 of nascent placental alkaline phosphatase condenses with a phospha- tidylinositol glycan to become the carboxyl terminus of the mature enzym
    • Micanovic R., Bailey C.A., Brink L., Gerber L., Pan Y.C., Hulmes J.D., Udenfriend S. Aspartic acid-484 of nascent placental alkaline phosphatase condenses with a phospha- tidylinositol glycan to become the carboxyl terminus of the mature enzym. Proc. Natl. Acad. Sci. USA 1988, 85:1398-1402.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 1398-1402
    • Micanovic, R.1    Bailey, C.A.2    Brink, L.3    Gerber, L.4    Pan, Y.C.5    Hulmes, J.D.6    Udenfriend, S.7
  • 50
    • 0024490113 scopus 로고
    • Processing at the carboxyl terminus of nascent placental alkaline phosphatase in a cell-free system: Evidence for specific cleavage of a signal peptide
    • Bailey C.A., Gerber L., Howard A.D., Udenfriend S. Processing at the carboxyl terminus of nascent placental alkaline phosphatase in a cell-free system: Evidence for specific cleavage of a signal peptide. Proc. Natl. Acad. Sci. USA 1989, 86:22-26.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 22-26
    • Bailey, C.A.1    Gerber, L.2    Howard, A.D.3    Udenfriend, S.4
  • 51
    • 0027048872 scopus 로고
    • Placental alkaline phosphatase: A model for studying COOH-terminal processing of phosphatidylinositol-glycan-anchored membrane proteins
    • Amthauer R., Kodukula K., Udenfriend S. Placental alkaline phosphatase: A model for studying COOH-terminal processing of phosphatidylinositol-glycan-anchored membrane proteins. Clin. Chem. 1992, 38:2510-2516.
    • (1992) Clin. Chem. , vol.38 , pp. 2510-2516
    • Amthauer, R.1    Kodukula, K.2    Udenfriend, S.3
  • 52
    • 0031971180 scopus 로고    scopus 로고
    • Defective intracellular transport of tissue-nonspecific alkaline phosphatase with an Alal62>Thr mutation associated with lethal hypophosphatasia
    • Shibata H., Fukushi M., Igarashi A., Misumi Y., Ikehara Y., Ohashi Y., Oda K. Defective intracellular transport of tissue-nonspecific alkaline phosphatase with an Alal62>Thr mutation associated with lethal hypophosphatasia. J.Biochem. (Tokyo) 1998, 123:968-977.
    • (1998) J.Biochem. (Tokyo) , vol.123 , pp. 968-977
    • Shibata, H.1    Fukushi, M.2    Igarashi, A.3    Misumi, Y.4    Ikehara, Y.5    Ohashi, Y.6    Oda, K.7
  • 53
    • 0028950984 scopus 로고
    • Cleavage without anchor addition accompanies the processing of a nascent protein to its glycosylphosphatidylinositol nchored form
    • Maxwell S.E., Ramalingam S., Gerber L.D., Udenfriend S. Cleavage without anchor addition accompanies the processing of a nascent protein to its glycosylphosphatidylinositol nchored form. Proc. Natl. Acad. Sci. USA 1995, 92:1550-1554.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 1550-1554
    • Maxwell, S.E.1    Ramalingam, S.2    Gerber, L.D.3    Udenfriend, S.4
  • 54
    • 0033988812 scopus 로고    scopus 로고
    • Effects of retinoic acid on N-glycosylation and mRNA stability of the liverJboneJkidney alkaline phosphatase in neuronal cells
    • Mueller W.H., Kleefeld D., Khattab B., Meissner J.D., Scheibe R.J. Effects of retinoic acid on N-glycosylation and mRNA stability of the liverJboneJkidney alkaline phosphatase in neuronal cells. J.Cell. Physiol 2000, 182:50-61.
    • (2000) J.Cell. Physiol , vol.182 , pp. 50-61
    • Mueller, W.H.1    Kleefeld, D.2    Khattab, B.3    Meissner, J.D.4    Scheibe, R.J.5
  • 55
    • 0035576329 scopus 로고    scopus 로고
    • Conserved core structure and active site residues in alkaline phosphatase superfamly enzymes
    • Galperin M.Y., Jedrzejas M.J. Conserved core structure and active site residues in alkaline phosphatase superfamly enzymes. Proteins 2001, 45:318-324.
    • (2001) Proteins , vol.45 , pp. 318-324
    • Galperin, M.Y.1    Jedrzejas, M.J.2
  • 56
    • 0032461412 scopus 로고    scopus 로고
    • A superamily of metalloenzymes unifies phosphopentomutase and cofactor-independent phosphoglycerate mutase with alkaline phosphatases and sulfatases
    • Galperin M.Y., Bairoch A., Koonin E.V. A superamily of metalloenzymes unifies phosphopentomutase and cofactor-independent phosphoglycerate mutase with alkaline phosphatases and sulfatases. Protein Sci. 1998, 7:1829-1835.
    • (1998) Protein Sci. , vol.7 , pp. 1829-1835
    • Galperin, M.Y.1    Bairoch, A.2    Koonin, E.V.3
  • 57
    • 0033117461 scopus 로고    scopus 로고
    • Catalytic promiscuity and the evolution of new enzymatic activities
    • O'Brien P.J., Herschlag D. Catalytic promiscuity and the evolution of new enzymatic activities. Chem. Biol. 1999, 6:R91-R105.
    • (1999) Chem. Biol. , vol.6
    • O'Brien, P.J.1    Herschlag, D.2
  • 58
    • 0035937857 scopus 로고    scopus 로고
    • Crystal structure of alkaline phosphatase from human placenta at 1.8 A resolution. Implication for a substrate specificity
    • Le Du M.H., Stigbrand T., Taussig M.J., Menez A., Stura E.A. Crystal structure of alkaline phosphatase from human placenta at 1.8 A resolution. Implication for a substrate specificity. J.Biol. Chem. 2001, 276:9158-9165.
    • (2001) J.Biol. Chem. , vol.276 , pp. 9158-9165
    • Le Du, M.H.1    Stigbrand, T.2    Taussig, M.J.3    Menez, A.4    Stura, E.A.5
  • 59
    • 0035903096 scopus 로고    scopus 로고
    • Structural evidence for a functional roleof human tissue nonspecific alkaline phosphatase in bone mineralization
    • Mornet E., Stura E., Lia-Baldini A.S., Stigbrand T., Menez A., Le Du M.H. Structural evidence for a functional roleof human tissue nonspecific alkaline phosphatase in bone mineralization. J.Biol. Chem. 2001, 276:31171-31178.
    • (2001) J.Biol. Chem. , vol.276 , pp. 31171-31178
    • Mornet, E.1    Stura, E.2    Lia-Baldini, A.S.3    Stigbrand, T.4    Menez, A.5    Le Du, M.H.6
  • 60
    • 0030928122 scopus 로고    scopus 로고
    • Mammalian alkaline phosphatases are allosteric enzymes
    • Hoylaerts M.F., Manes T., Millan J.L. Mammalian alkaline phosphatases are allosteric enzymes. J.Biol. Chem. 1997, 272:22781-22787.
    • (1997) J.Biol. Chem. , vol.272 , pp. 22781-22787
    • Hoylaerts, M.F.1    Manes, T.2    Millan, J.L.3
  • 61
    • 0027373184 scopus 로고
    • Modifications in a flexible surface loop modulate the isozyme-specific properties of mammalian alkaline phosphatases
    • Bossi M., Hoylaerts M.F., Millan J.L. Modifications in a flexible surface loop modulate the isozyme-specific properties of mammalian alkaline phosphatases. J.Biol. Chem. 1993, 268:25409-25416.
    • (1993) J.Biol. Chem. , vol.268 , pp. 25409-25416
    • Bossi, M.1    Hoylaerts, M.F.2    Millan, J.L.3
  • 63
    • 0022621303 scopus 로고
    • Modification of the active site of alkaline phosphatase by sitedirected mutagenesis
    • Ghosh S.S., Bock S.C., Rokita S.E., Kaiser E.T. Modification of the active site of alkaline phosphatase by sitedirected mutagenesis. Science 1986, 231:145-148.
    • (1986) Science , vol.231 , pp. 145-148
    • Ghosh, S.S.1    Bock, S.C.2    Rokita, S.E.3    Kaiser, E.T.4
  • 64
    • 0035873714 scopus 로고    scopus 로고
    • Functional interrelationships in the alkaline phosphatase superfamily: Phosphodiesterase activity of Escherichia coli alkaline phosphatase
    • O'Brien P.J., Herschlag D. Functional interrelationships in the alkaline phosphatase superfamily: Phosphodiesterase activity of Escherichia coli alkaline phosphatase. Biochemistry 2001, 40:5691-5699.
    • (2001) Biochemistry , vol.40 , pp. 5691-5699
    • O'Brien, P.J.1    Herschlag, D.2
  • 65
    • 0019331867 scopus 로고
    • Phosphorylated intermediate of alkaline phosphatase
    • Cocivera M., McManaman J., Wilson I.B. Phosphorylated intermediate of alkaline phosphatase. Biochemistry 1980, 19:2901-2907.
    • (1980) Biochemistry , vol.19 , pp. 2901-2907
    • Cocivera, M.1    McManaman, J.2    Wilson, I.B.3
  • 66
    • 0022552227 scopus 로고
    • Leaving group dependence in the phosphorylation of Escherichia coli alkaline phosphatase by monophosphate esters
    • Hall A.D., Williams A. Leaving group dependence in the phosphorylation of Escherichia coli alkaline phosphatase by monophosphate esters. Biochemistry 1986, 25:4784-4790.
    • (1986) Biochemistry , vol.25 , pp. 4784-4790
    • Hall, A.D.1    Williams, A.2
  • 67
    • 0022971360 scopus 로고
    • Normalactivity of nucleoside triphosphate pyrophosphatase in alkaline phosphatase-deficient fibroblasts from patients with infantile hypophosphatasia
    • Caswell A.M., Whyte M.P., Russell R.G. Normalactivity of nucleoside triphosphate pyrophosphatase in alkaline phosphatase-deficient fibroblasts from patients with infantile hypophosphatasia. J.Clin. Endocrinol Metab 1986, 63:1237-1241.
    • (1986) J.Clin. Endocrinol Metab , vol.63 , pp. 1237-1241
    • Caswell, A.M.1    Whyte, M.P.2    Russell, R.G.3
  • 68
    • 0025856050 scopus 로고
    • Hypophophatasiaand the extracellular metabolism of inorganic pyrophosphate: Clinical and laboratory aspects
    • Caswell A.M., Whyte M.P., Russell R.G. Hypophophatasiaand the extracellular metabolism of inorganic pyrophosphate: Clinical and laboratory aspects. Crit. Rev. Clin. Lab. Sci. 1991, 28:175-232.
    • (1991) Crit. Rev. Clin. Lab. Sci. , vol.28 , pp. 175-232
    • Caswell, A.M.1    Whyte, M.P.2    Russell, R.G.3
  • 69
    • 0026079126 scopus 로고
    • The alkaline phosphatase from bone: Transphosphorylating activityand kinetic mechanism
    • Muller K., Schellenberger V., Borneleit P., Treide A. The alkaline phosphatase from bone: Transphosphorylating activityand kinetic mechanism. Biochim. Biophys. Acta 1991, 1076:308-313.
    • (1991) Biochim. Biophys. Acta , vol.1076 , pp. 308-313
    • Muller, K.1    Schellenberger, V.2    Borneleit, P.3    Treide, A.4
  • 70
    • 0026683627 scopus 로고
    • Phosphotransferase activity associated with rat osseous plate alkaline phosphatase: A possible role in biomineralization
    • Pizauro J.M., Ciancaglini P., Leone F.A. Phosphotransferase activity associated with rat osseous plate alkaline phosphatase: A possible role in biomineralization. Int. J. Biochem. 1992, 24:1391-1396.
    • (1992) Int. J. Biochem. , vol.24 , pp. 1391-1396
    • Pizauro, J.M.1    Ciancaglini, P.2    Leone, F.A.3
  • 71
    • 0023259042 scopus 로고
    • Phosphotransferase activity of human alkaline phosphatases and the role of enzyme Zn2+
    • Stinson R.A., McPhee J.L., Collier H.B. Phosphotransferase activity of human alkaline phosphatases and the role of enzyme Zn2+. Biochim. Biophys. Acta 1987, 913:272-278.
    • (1987) Biochim. Biophys. Acta , vol.913 , pp. 272-278
    • Stinson, R.A.1    McPhee, J.L.2    Collier, H.B.3
  • 72
    • 0023336806 scopus 로고
    • Tyrosine-specific dephosphorylation-phosphorylation with alkaline phosphatases and epidermal growth factor receptor kinase as evidenced by 31P NMR spectroscop
    • Takahashi K., Shimidzu M., Shindo H., Kawamoto T., Nishi M., Matsumoto U., Taniguchi S. Tyrosine-specific dephosphorylation-phosphorylation with alkaline phosphatases and epidermal growth factor receptor kinase as evidenced by 31P NMR spectroscop. J.Biochem. (Tokyo) 1987, 101:1107-1114.
    • (1987) J.Biochem. (Tokyo) , vol.101 , pp. 1107-1114
    • Takahashi, K.1    Shimidzu, M.2    Shindo, H.3    Kawamoto, T.4    Nishi, M.5    Matsumoto, U.6    Taniguchi, S.7
  • 73
    • 0025032279 scopus 로고
    • Differences in phosphatidate hydrolytic activity of human alkaline phosphatase isozymes
    • Sumikawa K., Okochi T., Adachi K. Differences in phosphatidate hydrolytic activity of human alkaline phosphatase isozymes. Biochim. Biophys. Acta 1990, 1046:27-31.
    • (1990) Biochim. Biophys. Acta , vol.1046 , pp. 27-31
    • Sumikawa, K.1    Okochi, T.2    Adachi, K.3
  • 75
    • 20444502785 scopus 로고
    • Metabolic abnormalities in hypophosphatasia
    • Fraser D., Yendt E.R., Christie F.H.E. Metabolic abnormalities in hypophosphatasia. Lancet 1955, 1:286.
    • (1955) Lancet , vol.1 , pp. 286
    • Fraser, D.1    Yendt, E.R.2    Christie, F.H.E.3
  • 76
    • 0016956817 scopus 로고
    • Metabolism of inorganic pyrophosphate(PPi)
    • Russell R.G. Metabolism of inorganic pyrophosphate(PPi). Arthritis Rheum 1976, 19(Suppl. 3):465-478.
    • (1976) Arthritis Rheum , vol.19 , Issue.SUPPL. 3 , pp. 465-478
    • Russell, R.G.1
  • 77
    • 0021811803 scopus 로고
    • Markedly increased circulating pyridoxal-5'-phosphate levels in hypophosphatasia. Alkaline phosphatase acts in vitamin B6 metabolism
    • Whyte M.P., Mahuren J.D., Vrabel L.A., Coburn S.P. Markedly increased circulating pyridoxal-5'-phosphate levels in hypophosphatasia. Alkaline phosphatase acts in vitamin B6 metabolism. J.Clin. Invest. 1985, 76:752-756.
    • (1985) J.Clin. Invest. , vol.76 , pp. 752-756
    • Whyte, M.P.1    Mahuren, J.D.2    Vrabel, L.A.3    Coburn, S.P.4
  • 78
    • 0023897043 scopus 로고
    • Perinatal hypophosphatasia: Tissue levels of vitamin B6 are unremarkable despite markedly increased circulating concentrations of pyridoxal-S'-phosphate. Evid
    • Whyte M.P., Mahuren J.D., Fedde K.N., Cole F.S., McCabe E.R., Coburn S.P. Perinatal hypophosphatasia: Tissue levels of vitamin B6 are unremarkable despite markedly increased circulating concentrations of pyridoxal-S'-phosphate. Evid. J.Clin. Invest. 1988, 81:1234-1239.
    • (1988) J.Clin. Invest. , vol.81 , pp. 1234-1239
    • Whyte, M.P.1    Mahuren, J.D.2    Fedde, K.N.3    Cole, F.S.4    McCabe, E.R.5    Coburn, S.P.6
  • 79
    • 0031764923 scopus 로고    scopus 로고
    • Alkaline phosphatase (EC 3.1.3.1) in serum is inhibited by physiological concentrations of inorganic phosphate
    • Coburn S.P., Mahuren J.D., Jain M., Zubovic Y., Wortsman J. Alkaline phosphatase (EC 3.1.3.1) in serum is inhibited by physiological concentrations of inorganic phosphate. J.Clin. Endocrinol. Metab. 1998, 83:3951-3957.
    • (1998) J.Clin. Endocrinol. Metab. , vol.83 , pp. 3951-3957
    • Coburn, S.P.1    Mahuren, J.D.2    Jain, M.3    Zubovic, Y.4    Wortsman, J.5
  • 80
    • 0032546421 scopus 로고    scopus 로고
    • Allosteric modulation of pyrophosphatase activity of rat osseous plate alkaline phosphatase by magnesium ions
    • Leone F.A., Rezende L.A., Ciancaglini P., Pizauro J.M. Allosteric modulation of pyrophosphatase activity of rat osseous plate alkaline phosphatase by magnesium ions. Int. J. Biochem. Cell Biol. 1998, 30:89-97.
    • (1998) Int. J. Biochem. Cell Biol. , vol.30 , pp. 89-97
    • Leone, F.A.1    Rezende, L.A.2    Ciancaglini, P.3    Pizauro, J.M.4
  • 81
    • 0028273779 scopus 로고
    • Specific activity of skeletal alkaline phosphatase in human osteo-blast-line cells regulated by phosphate, phosphate esters, and phosphate analogs and release
    • Farley J.R., Hall S.L., Tanner M.A., Wergedal J.E. Specific activity of skeletal alkaline phosphatase in human osteo-blast-line cells regulated by phosphate, phosphate esters, and phosphate analogs and release. J.Bone Miner. Res. 1994, 9:497-508.
    • (1994) J.Bone Miner. Res. , vol.9 , pp. 497-508
    • Farley, J.R.1    Hall, S.L.2    Tanner, M.A.3    Wergedal, J.E.4
  • 82
    • 0023156045 scopus 로고
    • Tetrameric alkaline phosphatase from human liver is converted to dimers by phospha-tidylinositol phospholipase C
    • Hawrylak K., Stinson R.A. Tetrameric alkaline phosphatase from human liver is converted to dimers by phospha-tidylinositol phospholipase C. FEBS Lett. 1987, 212:289-291.
    • (1987) FEBS Lett. , vol.212 , pp. 289-291
    • Hawrylak, K.1    Stinson, R.A.2
  • 84
    • 0023872334 scopus 로고
    • A phospholipase D specific for the phosphatidylinositol anchor of cell-surface proteins is abundant in plasma
    • Low M.G., Prasad A.R. A phospholipase D specific for the phosphatidylinositol anchor of cell-surface proteins is abundant in plasma. Proc. Natl. Acad. Sci. USA 1988, 85:980-984.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 980-984
    • Low, M.G.1    Prasad, A.R.2
  • 85
    • 0023430368 scopus 로고
    • High lateral mobility of endogenous and transfected alkaline phosphatase: A phosphatidylinositol-anchored membrane protein
    • Noda M., Yoon K., Rodan G.A., Koppel D.E. High lateral mobility of endogenous and transfected alkaline phosphatase: A phosphatidylinositol-anchored membrane protein. J.Cell Biol. 1987, 105:1671-1677.
    • (1987) J.Cell Biol. , vol.105 , pp. 1671-1677
    • Noda, M.1    Yoon, K.2    Rodan, G.A.3    Koppel, D.E.4
  • 86
    • 0030781023 scopus 로고    scopus 로고
    • Glycosyl-phosphatidylinositol anchored membrane enzymes
    • Hooper N.M. Glycosyl-phosphatidylinositol anchored membrane enzymes. Clin. Chim. Acta 1997, 266:3-12.
    • (1997) Clin. Chim. Acta , vol.266 , pp. 3-12
    • Hooper, N.M.1
  • 87
    • 0023872240 scopus 로고
    • Biosynthesis of placental alkaline phosphatase and its post-translational modification by glycophospholipid for membrane-anchoring
    • Takami N., Ogata S., Oda K., Misumi Y., Ikehara Y. Biosynthesis of placental alkaline phosphatase and its post-translational modification by glycophospholipid for membrane-anchoring. J.Biol. Chem. 1988, 263:3016-3021.
    • (1988) J.Biol. Chem. , vol.263 , pp. 3016-3021
    • Takami, N.1    Ogata, S.2    Oda, K.3    Misumi, Y.4    Ikehara, Y.5
  • 88
    • 0027739887 scopus 로고
    • Expression and nature of the alkaline phosphatase gene in cultured osteosar-coma cells
    • Stinson R.A., Thacker J.D., Lin C.C. Expression and nature of the alkaline phosphatase gene in cultured osteosar-coma cells. Clin. Chim. Acta 1993, 221:105-114.
    • (1993) Clin. Chim. Acta , vol.221 , pp. 105-114
    • Stinson, R.A.1    Thacker, J.D.2    Lin, C.C.3
  • 89
    • 0032740242 scopus 로고    scopus 로고
    • Differential expression and activity of tissue-nonspecific alkaline phosphatase (TNAP) in rat odontogenic cells in vivo
    • Hotton D., Mauro N., Lezot F., Forest N., Berdal A. Differential expression and activity of tissue-nonspecific alkaline phosphatase (TNAP) in rat odontogenic cells in vivo. J.Histochem. Cytochem. 1999, 47:1541-1552.
    • (1999) J.Histochem. Cytochem. , vol.47 , pp. 1541-1552
    • Hotton, D.1    Mauro, N.2    Lezot, F.3    Forest, N.4    Berdal, A.5
  • 90
    • 0023724387 scopus 로고
    • Alkaline phosphatase is an ectoenzyme that acts on micromolar concentrations of natural substrates at physiologic pH in human osteosar-coma (SAOS-2) cells
    • Fedde K.N., Lane C.C., Whyte M.P. Alkaline phosphatase is an ectoenzyme that acts on micromolar concentrations of natural substrates at physiologic pH in human osteosar-coma (SAOS-2) cells. Arch. Biochem. Biophys. 1988, 264:400-409.
    • (1988) Arch. Biochem. Biophys. , vol.264 , pp. 400-409
    • Fedde, K.N.1    Lane, C.C.2    Whyte, M.P.3
  • 92
    • 0027468760 scopus 로고
    • Detergent insolubility of alkaline phosphatase during biosynthetic transport and endocytosis. Role of cholesterol
    • Cerneus D.P., Ueffing E., Posthuma G., Strous G.J., van der E.A. Detergent insolubility of alkaline phosphatase during biosynthetic transport and endocytosis. Role of cholesterol. J.Biol. Chem. 1993, 268:3150-3155.
    • (1993) J.Biol. Chem. , vol.268 , pp. 3150-3155
    • Cerneus, D.P.1    Ueffing, E.2    Posthuma, G.3    Strous, G.J.4    van der, E.A.5
  • 93
    • 0026528391 scopus 로고
    • Epithelial cell lines that induce bone formation in vivo produce alkaline phosphatase-enriched matrix vesicles in culture
    • Boyan B.D., Swain L.D., Schwartz Z., Ramirez V., Carnes D.L. Epithelial cell lines that induce bone formation in vivo produce alkaline phosphatase-enriched matrix vesicles in culture. Clin. Orthop. 1992, 277:266-276.
    • (1992) Clin. Orthop. , vol.277 , pp. 266-276
    • Boyan, B.D.1    Swain, L.D.2    Schwartz, Z.3    Ramirez, V.4    Carnes, D.L.5
  • 94
    • 0028099997 scopus 로고
    • Interpretation and clinical significance of alkaline phosphatase isoenzyme patterns
    • Van Hoof V.O., De Broe M.E. Interpretation and clinical significance of alkaline phosphatase isoenzyme patterns. Crit. Rev. Clin. Lab. Sci. 1994, 31:197-293.
    • (1994) Crit. Rev. Clin. Lab. Sci. , vol.31 , pp. 197-293
    • Van Hoof, V.O.1    De Broe, M.E.2
  • 95
    • 0023009015 scopus 로고
    • Roles of alkaline phosphatase and labile internal mineral in matrix vesicle-mediated calcification. Effect of selective release of membrane-bound alkaline pho
    • Register T.C., McLean F.M., Low M.G., Wuthier R.E. Roles of alkaline phosphatase and labile internal mineral in matrix vesicle-mediated calcification. Effect of selective release of membrane-bound alkaline pho. J.Biol. Chem. 1986, 261:9354-9360.
    • (1986) J.Biol. Chem. , vol.261 , pp. 9354-9360
    • Register, T.C.1    McLean, F.M.2    Low, M.G.3    Wuthier, R.E.4
  • 96
    • 0023645335 scopus 로고
    • Disposition of preformed mineral in matrix vesicles. Internal localization and association with alkaline phosphatase
    • McLean F.M., Keller P.J., Genge B.R., Walters S.A., Wuthier R.E. Disposition of preformed mineral in matrix vesicles. Internal localization and association with alkaline phosphatase. J.Biol. Chem. 1987, 262:10481-10488.
    • (1987) J.Biol. Chem. , vol.262 , pp. 10481-10488
    • McLean, F.M.1    Keller, P.J.2    Genge, B.R.3    Walters, S.A.4    Wuthier, R.E.5
  • 97
    • 0032712430 scopus 로고    scopus 로고
    • Isoforms of bone alkaline phosphatase: Characterization and origin in human trabecular and cortical bone
    • Magnusson P., Larsson L., Magnusson M., Davie M.W., Sharp C.A. Isoforms of bone alkaline phosphatase: Characterization and origin in human trabecular and cortical bone. J.Bone Miner. Res. 1999, 14:1926-1933.
    • (1999) J.Bone Miner. Res. , vol.14 , pp. 1926-1933
    • Magnusson, P.1    Larsson, L.2    Magnusson, M.3    Davie, M.W.4    Sharp, C.A.5
  • 98
    • 0034113511 scopus 로고    scopus 로고
    • Hypophosphatasia: The mutations in the tissue-nonspecific alkaline phosphatase gene
    • Mornet E. Hypophosphatasia: The mutations in the tissue-nonspecific alkaline phosphatase gene. Hum. Mutat. 2000, 15:309-315.
    • (2000) Hum. Mutat. , vol.15 , pp. 309-315
    • Mornet, E.1
  • 99
    • 0027451573 scopus 로고
    • Changes in cell adhesion and cell proliferation are associated with expression of tissue non-specific alkaline phosphatase
    • Hui M., Hu M., Tenenbaum H.C. Changes in cell adhesion and cell proliferation are associated with expression of tissue non-specific alkaline phosphatase. Cell Tissue Res. 1993, 274:429-437.
    • (1993) Cell Tissue Res. , vol.274 , pp. 429-437
    • Hui, M.1    Hu, M.2    Tenenbaum, H.C.3
  • 100
    • 0023199692 scopus 로고
    • Infantile hypophosphatasia fibroblasts proliferate normally in culture: Evidence against a role for alkaline phosphatase (tissue nonspecific isoenzyme) in the
    • Whyte M.P., Vrabel L.A. Infantile hypophosphatasia fibroblasts proliferate normally in culture: Evidence against a role for alkaline phosphatase (tissue nonspecific isoenzyme) in the. Calcif. Tissue Int. 1987, 40:1-7.
    • (1987) Calcif. Tissue Int. , vol.40 , pp. 1-7
    • Whyte, M.P.1    Vrabel, L.A.2
  • 101
    • 0023479077 scopus 로고
    • Separation and identification of alkaline phosphatase isoenzymes and isoforms in serum of healthy persons by isoelectric focusing
    • Griffiths J., Black J. Separation and identification of alkaline phosphatase isoenzymes and isoforms in serum of healthy persons by isoelectric focusing. Clin. Chem. 1987, 33:2171-2177.
    • (1987) Clin. Chem. , vol.33 , pp. 2171-2177
    • Griffiths, J.1    Black, J.2
  • 102
    • 0015523082 scopus 로고
    • L-Homoarginine. An organ-specific, uncompetitive inhibitor of human liver and bone alkaline phosphohydrolases
    • Lin C.W., Fishman W.H. L-Homoarginine. An organ-specific, uncompetitive inhibitor of human liver and bone alkaline phosphohydrolases. J.Biol. Chem. 1972, 247:3082-3087.
    • (1972) J.Biol. Chem. , vol.247 , pp. 3082-3087
    • Lin, C.W.1    Fishman, W.H.2
  • 103
    • 0018098683 scopus 로고
    • Differentialinhibition of the products of the human alkaline phosphatase loci
    • Mulivor R.A., Plotkin L.I., Harris H. Differentialinhibition of the products of the human alkaline phosphatase loci. Ann. Hum. Genet. 1978, 42:1-13.
    • (1978) Ann. Hum. Genet. , vol.42 , pp. 1-13
    • Mulivor, R.A.1    Plotkin, L.I.2    Harris, H.3
  • 104
    • 0019992729 scopus 로고
    • Evidence that alkaline phosphatase from human neutrophils is the same gene product as the liverJkidneyJbone isoenzyme
    • Gainer A.L., Stinson R.A. Evidence that alkaline phosphatase from human neutrophils is the same gene product as the liverJkidneyJbone isoenzyme. Clin. Chim. Acta 1982, 123:11-17.
    • (1982) Clin. Chim. Acta , vol.123 , pp. 11-17
    • Gainer, A.L.1    Stinson, R.A.2
  • 106
    • 0022273632 scopus 로고
    • Isolation and characterization of alkaline phosphatase-containing granules (phosphasomes) from human polymorphonuclear leucocytes
    • Smith G.P., Sharp G., Peters T.J. Isolation and characterization of alkaline phosphatase-containing granules (phosphasomes) from human polymorphonuclear leucocytes. J.Cell Sci. 1985, 76:167-178.
    • (1985) J.Cell Sci. , vol.76 , pp. 167-178
    • Smith, G.P.1    Sharp, G.2    Peters, T.J.3
  • 107
    • 0021662509 scopus 로고
    • Aspects of the relationship between liver, kidney and bone alkaline phosphatases
    • Moss D.W. Aspects of the relationship between liver, kidney and bone alkaline phosphatases. Prog. Clin. Biol. Res. 1984, 166:79-86.
    • (1984) Prog. Clin. Biol. Res. , vol.166 , pp. 79-86
    • Moss, D.W.1
  • 108
    • 0022471023 scopus 로고
    • Quantitative method for determining serum alkaline phosphatase isoenzyme activity I. Guanidine hydrochloride: New reagent for selectively inhibiting major ser
    • Shephard M.D., Peake M.J. Quantitative method for determining serum alkaline phosphatase isoenzyme activity I. Guanidine hydrochloride: New reagent for selectively inhibiting major ser. J.Clin. Pathol. 1986, 39:1025-1030.
    • (1986) J.Clin. Pathol. , vol.39 , pp. 1025-1030
    • Shephard, M.D.1    Peake, M.J.2
  • 109
    • 0022909195 scopus 로고
    • Multiple forms of acid and alkaline phosphatases: Genetics, expression and tissue-specific modification
    • Moss D.W. Multiple forms of acid and alkaline phosphatases: Genetics, expression and tissue-specific modification. Clin. Chim. Acta 1986, 161:123-135.
    • (1986) Clin. Chim. Acta , vol.161 , pp. 123-135
    • Moss, D.W.1
  • 111
    • 0020622240 scopus 로고
    • Total bone and liver alkaline phosphatases in plasma: Biological variations and reference limits
    • Schiele F., Henny J., Hitz J., Petitclerc C., Gueguen R., Siest G. Total bone and liver alkaline phosphatases in plasma: Biological variations and reference limits. Clin. Chem. 1983, 29:634-641.
    • (1983) Clin. Chem. , vol.29 , pp. 634-641
    • Schiele, F.1    Henny, J.2    Hitz, J.3    Petitclerc, C.4    Gueguen, R.5    Siest, G.6
  • 112
    • 0019790967 scopus 로고
    • Improved method for quantitative determination in serum of alkaline phosphatase of skeletal origin
    • Farley J.R., Chesnut C.H., Baylink D.J. Improved method for quantitative determination in serum of alkaline phosphatase of skeletal origin. Clin. Chem. 1981, 27:2002-2007.
    • (1981) Clin. Chem. , vol.27 , pp. 2002-2007
    • Farley, J.R.1    Chesnut, C.H.2    Baylink, D.J.3
  • 113
    • 0022572056 scopus 로고
    • Skeletal alkaline phosphatase activity as a bone formation index in vitro
    • Farley J.R., Baylink D.J. Skeletal alkaline phosphatase activity as a bone formation index in vitro. Metabolism 1986, 35:563-571.
    • (1986) Metabolism , vol.35 , pp. 563-571
    • Farley, J.R.1    Baylink, D.J.2
  • 114
    • 0026687210 scopus 로고
    • An alternate origin for the placental isoenzymeof alkaline phosphatase
    • Griffiths J. An alternate origin for the placental isoenzymeof alkaline phosphatase. Arch. Pathol. Lab. Med. 1992, 116:1019-1024.
    • (1992) Arch. Pathol. Lab. Med. , vol.116 , pp. 1019-1024
    • Griffiths, J.1
  • 115
    • 0028914274 scopus 로고
    • Alkaline phosphatase: Placental and tissue-nonspecific isoenzymes hydrolyze phosphoethanolamine, inorganic pyrophosphate, and pyridoxal 5'-phosphate. Substrat
    • Whyte M.P., Landt M., Ryan L.M., Mulivor R.A., Henthorn P.S., Fedde K.N., Mahuren J.D., Coburn S.P. Alkaline phosphatase: Placental and tissue-nonspecific isoenzymes hydrolyze phosphoethanolamine, inorganic pyrophosphate, and pyridoxal 5'-phosphate. Substrat. J.Clin. Invest. 1995, 95:1440-1445.
    • (1995) J.Clin. Invest. , vol.95 , pp. 1440-1445
    • Whyte, M.P.1    Landt, M.2    Ryan, L.M.3    Mulivor, R.A.4    Henthorn, P.S.5    Fedde, K.N.6    Mahuren, J.D.7    Coburn, S.P.8
  • 116
    • 0034867464 scopus 로고    scopus 로고
    • Hypophosphatasia: Molecular diagnosis of Rathbun's original case
    • Mumm S., Jones J., Finnegan P., Whyte M.P. Hypophosphatasia: Molecular diagnosis of Rathbun's original case. J.Bone Miner. Res. 2001, 16:1724-1727.
    • (2001) J.Bone Miner. Res. , vol.16 , pp. 1724-1727
    • Mumm, S.1    Jones, J.2    Finnegan, P.3    Whyte, M.P.4
  • 117
    • 0001206301 scopus 로고
    • Hypophosphatasia
    • Fraser D. Hypophosphatasia. Am. J. Med. 1957, 22:730-746.
    • (1957) Am. J. Med. , vol.22 , pp. 730-746
    • Fraser, D.1
  • 119
    • 0017807590 scopus 로고
    • Prenatal diagnosis of hypophosphatasia; Genetic, biochemical, and clinical studies
    • Mulivor R.A., Mennuti M., Zackai E.H., Harris H. Prenatal diagnosis of hypophosphatasia; Genetic, biochemical, and clinical studies. Am. J. Hum. Genet. 1978, 30:271-282.
    • (1978) Am. J. Hum. Genet. , vol.30 , pp. 271-282
    • Mulivor, R.A.1    Mennuti, M.2    Zackai, E.H.3    Harris, H.4
  • 120
    • 0020071636 scopus 로고
    • Hypophosphatasia congenita letalis
    • Wolff C., Zabransky S. Hypophosphatasia congenita letalis. Eur. J. Pediatr. 1982, 138:197-199.
    • (1982) Eur. J. Pediatr. , vol.138 , pp. 197-199
    • Wolff, C.1    Zabransky, S.2
  • 121
    • 0024242898 scopus 로고
    • Pulmonary hypoplasia in neonatal hypophosphatasia
    • Silver M.M., Vilos G.A., Milne K.J. Pulmonary hypoplasia in neonatal hypophosphatasia. Pediatr. Pathol. 1988, 8:483-493.
    • (1988) Pediatr. Pathol. , vol.8 , pp. 483-493
    • Silver, M.M.1    Vilos, G.A.2    Milne, K.J.3
  • 122
    • 0026053143 scopus 로고
    • Perinatal lethal hypophosphatasia; Clinical, radiologic and morphologic findings
    • Shohat M., Rimoin D.L., Gruber H.E., Lachman R.S. Perinatal lethal hypophosphatasia; Clinical, radiologic and morphologic findings. Pediatr. Radiol. 1991, 21:421-427.
    • (1991) Pediatr. Radiol. , vol.21 , pp. 421-427
    • Shohat, M.1    Rimoin, D.L.2    Gruber, H.E.3    Lachman, R.S.4
  • 123
    • 0014243518 scopus 로고
    • Hypophosphatasia: Clinical and metabolic studies
    • Teree T.M., Klein L.R. Hypophosphatasia: Clinical and metabolic studies. J.Pediatr. 1968, 72:41-50.
    • (1968) J.Pediatr. , vol.72 , pp. 41-50
    • Teree, T.M.1    Klein, L.R.2
  • 126
    • 0020450679 scopus 로고
    • Circulating vitamin D metabolite levels in hypophosphatasia
    • Whyte M.P., Seino Y. Circulating vitamin D metabolite levels in hypophosphatasia. J.Clin. Endocrinol. Metab. 1982, 55:178-180.
    • (1982) J.Clin. Endocrinol. Metab. , vol.55 , pp. 178-180
    • Whyte, M.P.1    Seino, Y.2
  • 127
    • 0017598947 scopus 로고
    • Neonatal hypophosphatasia with elevated serum parathyroid hormone
    • Maesaka H., Niitsu N., Suwa S., Fujita T. Neonatal hypophosphatasia with elevated serum parathyroid hormone. Eur. J. Pediatr. 1977, 125:71-80.
    • (1977) Eur. J. Pediatr. , vol.125 , pp. 71-80
    • Maesaka, H.1    Niitsu, N.2    Suwa, S.3    Fujita, T.4
  • 129
    • 0025098098 scopus 로고
    • Hyperphosphatemia in infantile hypophosphatasia: Implications for carrier diagnosis and screening
    • Chodirker B.N., Evans J.A., Seargeant L.E., Cheang M.S., Greenberg C.R. Hyperphosphatemia in infantile hypophosphatasia: Implications for carrier diagnosis and screening. Am. J. Hum. Genet. 1990, 46:280-285.
    • (1990) Am. J. Hum. Genet. , vol.46 , pp. 280-285
    • Chodirker, B.N.1    Evans, J.A.2    Seargeant, L.E.3    Cheang, M.S.4    Greenberg, C.R.5
  • 131
    • 0024524763 scopus 로고
    • Skin dimples in hypophosphatasia
    • Wendling D., Blanc D., Hory B. Skin dimples in hypophosphatasia. Dermatologica 1989, 178:179-180.
    • (1989) Dermatologica , vol.178 , pp. 179-180
    • Wendling, D.1    Blanc, D.2    Hory, B.3
  • 132
    • 0022637532 scopus 로고
    • Infantile hypophosphatasia: Normalization of circulating bone alkaline phosphatase activity followed by skeletal reminer-alization. Evidence for an intact str
    • Whyte M.P., Magill H.L., Fallon M.D., Herrod H.G. Infantile hypophosphatasia: Normalization of circulating bone alkaline phosphatase activity followed by skeletal reminer-alization. Evidence for an intact str. J.Pediatr. 1986, 108:82-88.
    • (1986) J.Pediatr. , vol.108 , pp. 82-88
    • Whyte, M.P.1    Magill, H.L.2    Fallon, M.D.3    Herrod, H.G.4
  • 133
    • 0018358397 scopus 로고
    • Skull scintigraphy in infantile hypophosphatasia
    • Sty J.R., Boedecker R.A., Babbitt D.P. Skull scintigraphy in infantile hypophosphatasia. J.Nucl. Med. 1979, 20:305-306.
    • (1979) J.Nucl. Med. , vol.20 , pp. 305-306
    • Sty, J.R.1    Boedecker, R.A.2    Babbitt, D.P.3
  • 135
    • 0032839769 scopus 로고    scopus 로고
    • Bone metabolism and bone mineral density in childhood hypophosphatasia
    • Girschick H.J., Schneider P., Kruse K., Huppertz H.I. Bone metabolism and bone mineral density in childhood hypophosphatasia. Bone 1999, 25:361-367.
    • (1999) Bone , vol.25 , pp. 361-367
    • Girschick, H.J.1    Schneider, P.2    Kruse, K.3    Huppertz, H.I.4
  • 136
    • 0022968773 scopus 로고
    • Management of femoral fractures and pseudofractures in adult hypophosphatasia
    • Coe J.D., Murphy W.A., Whyte M.P. Management of femoral fractures and pseudofractures in adult hypophosphatasia. J.Bone Joint Surg. Am. 1986, 68:981-990.
    • (1986) J.Bone Joint Surg. Am. , vol.68 , pp. 981-990
    • Coe, J.D.1    Murphy, W.A.2    Whyte, M.P.3
  • 137
    • 0019940289 scopus 로고
    • Adulthypophosphatasia with chondrocalcinosis and arthropathy. Variable penetrance of hypophosphatasemia in a large Oklahoma kindred
    • Whyte M.P., Murphy W.A., Fallon M.D. Adulthypophosphatasia with chondrocalcinosis and arthropathy. Variable penetrance of hypophosphatasemia in a large Oklahoma kindred. Am. J. Med 1982, 72:631-641.
    • (1982) Am. J. Med , vol.72 , pp. 631-641
    • Whyte, M.P.1    Murphy, W.A.2    Fallon, M.D.3
  • 139
    • 0015802288 scopus 로고
    • Childhood hypophosphatasia and the premature loss of teeth. A clinical and laboratory study of seven cases. Oral Surg
    • Beumer J., Trowbridge H.O., Silverman S., Eisenberg E. Childhood hypophosphatasia and the premature loss of teeth. A clinical and laboratory study of seven cases. Oral Surg. Oral Med. Oral Pathol 1973, 35:631-640.
    • (1973) Oral Med. Oral Pathol , vol.35 , pp. 631-640
    • Beumer, J.1    Trowbridge, H.O.2    Silverman, S.3    Eisenberg, E.4
  • 141
    • 0025144554 scopus 로고
    • Pseudohypophosphatasia:Aberrant localization and substrate specificity of alkaline phosphatase in cultured skin fibroblasts
    • Fedde K.N., Cole D.E., Whyte M.P. Pseudohypophosphatasia:Aberrant localization and substrate specificity of alkaline phosphatase in cultured skin fibroblasts. Am. J. Hum. Genet. 1990, 41:776-783.
    • (1990) Am. J. Hum. Genet. , vol.41 , pp. 776-783
    • Fedde, K.N.1    Cole, D.E.2    Whyte, M.P.3
  • 142
    • 0020041466 scopus 로고
    • Turnover rate of skeletal alkaline phosphatase in humans
    • Posen S., Grunstein H.S. Turnover rate of skeletal alkaline phosphatase in humans. Clin. Chem. 1982, 28:153-154.
    • (1982) Clin. Chem. , vol.28 , pp. 153-154
    • Posen, S.1    Grunstein, H.S.2
  • 143
    • 0021719343 scopus 로고
    • Enzyme replacement therapy for infantile hypophosphatasia attempted by intravenous infusions of alkaline phosphatase-rich Paget plasma: Results in three addit
    • Whyte M.P., McAlister W.H., Patton L.S., Magill H.L., Fallon M.D., Lorentz W.B., Herrod H.G. Enzyme replacement therapy for infantile hypophosphatasia attempted by intravenous infusions of alkaline phosphatase-rich Paget plasma: Results in three addit. J.Pediatr. 1984, 105:926-933.
    • (1984) J.Pediatr. , vol.105 , pp. 926-933
    • Whyte, M.P.1    McAlister, W.H.2    Patton, L.S.3    Magill, H.L.4    Fallon, M.D.5    Lorentz, W.B.6    Herrod, H.G.7
  • 145
    • 0020546002 scopus 로고
    • Alkaline phosphatase deficiency in cultured skin fibroblasts from patients with hypophosphatasia: Comparison of the infantile, childhood, and adult forms
    • Whyte M.P., Vrabel L.A., Schwartz T.D. Alkaline phosphatase deficiency in cultured skin fibroblasts from patients with hypophosphatasia: Comparison of the infantile, childhood, and adult forms. J.Clin. Endocrinol Metab. 1983, 57:831-837.
    • (1983) J.Clin. Endocrinol Metab. , vol.57 , pp. 831-837
    • Whyte, M.P.1    Vrabel, L.A.2    Schwartz, T.D.3
  • 147
    • 0028911502 scopus 로고
    • Effect of gestational age on levels of serum alkaline phosphatase isoenzymes in healthy pregnant women
    • Okesina A.B., Donaldson D., Lascelles P.T., Morris P. Effect of gestational age on levels of serum alkaline phosphatase isoenzymes in healthy pregnant women. Int. J. Gynaecol Obstet. 1995, 48:25-29.
    • (1995) Int. J. Gynaecol Obstet. , vol.48 , pp. 25-29
    • Okesina, A.B.1    Donaldson, D.2    Lascelles, P.T.3    Morris, P.4
  • 148
    • 0034009975 scopus 로고    scopus 로고
    • A detailed assessment of alterations in bon turnover, calcium homeostasis, and bone density in normal pregnancy
    • Black A.J., Topping J., Durham B., Farquharson R.G., Fraser W.D. A detailed assessment of alterations in bon turnover, calcium homeostasis, and bone density in normal pregnancy. J.Bone Miner. Res. 2000, 15:557-563.
    • (2000) J.Bone Miner. Res. , vol.15 , pp. 557-563
    • Black, A.J.1    Topping, J.2    Durham, B.3    Farquharson, R.G.4    Fraser, W.D.5
  • 149
    • 0024566781 scopus 로고
    • Hypomagnesemia and low alkaline phosphatase activity in patients' serum after cardiac surgery
    • Lum G., Marquardt C., Khuri S.F. Hypomagnesemia and low alkaline phosphatase activity in patients' serum after cardiac surgery. Clin. Chem. 1989, 35:664-667.
    • (1989) Clin. Chem. , vol.35 , pp. 664-667
    • Lum, G.1    Marquardt, C.2    Khuri, S.F.3
  • 150
    • 0028952722 scopus 로고
    • Significance of low serum alkaline phosphatase activity in a predominantly adult male population
    • Lum G. Significance of low serum alkaline phosphatase activity in a predominantly adult male population. Clin. Chem. 1995, 41:515-518.
    • (1995) Clin. Chem. , vol.41 , pp. 515-518
    • Lum, G.1
  • 152
    • 0021079828 scopus 로고
    • Clinical, laboratory, and genetic investigations of hypophosphatasia: Support for autosomal dominant inheritance with homozygous lethality
    • Eastman J.R., Bixler D. Clinical, laboratory, and genetic investigations of hypophosphatasia: Support for autosomal dominant inheritance with homozygous lethality. J.Craniofac. Genet. Dev. Biol. 1983, 3:213-234.
    • (1983) J.Craniofac. Genet. Dev. Biol. , vol.3 , pp. 213-234
    • Eastman, J.R.1    Bixler, D.2
  • 153
    • 0017884940 scopus 로고
    • Theurinary excretion of phosphoethanolamine in diseases other than hypophosphatasia
    • Licata A.A., Radfar N., Bartter F.C., Bou E. Theurinary excretion of phosphoethanolamine in diseases other than hypophosphatasia. Am. J. Med. 1978, 64:133-138.
    • (1978) Am. J. Med. , vol.64 , pp. 133-138
    • Licata, A.A.1    Radfar, N.2    Bartter, F.C.3    Bou, E.4
  • 154
    • 0025008072 scopus 로고
    • Increased urinary phosphoethanolamine in a man with asymptomatic osteopenia
    • Licata A.A. Increased urinary phosphoethanolamine in a man with asymptomatic osteopenia. Am. J. Med. 1990, 89:688-689.
    • (1990) Am. J. Med. , vol.89 , pp. 688-689
    • Licata, A.A.1
  • 155
    • 0015057271 scopus 로고
    • Inorganic pyrophosphate in plasma in normal persons and in patients with hypophosphatasia, osteogenesis imperfecta, and other disorders of bone
    • Russell R.G., Bisaz S., Donath A., Morgan D.B., Fleisch H. Inorganic pyrophosphate in plasma in normal persons and in patients with hypophosphatasia, osteogenesis imperfecta, and other disorders of bone. J.Clin. Invest. 1971, 50:961-969.
    • (1971) J.Clin. Invest. , vol.50 , pp. 961-969
    • Russell, R.G.1    Bisaz, S.2    Donath, A.3    Morgan, D.B.4    Fleisch, H.5
  • 156
    • 0026079493 scopus 로고
    • Raised urinary excretion of inorganic pyrophosphate in asymptomatic members of a hypophosphatasia kindred
    • Macfarlane J.D., Poorthuis B.J., Mulivor R.A., Caswell A.M. Raised urinary excretion of inorganic pyrophosphate in asymptomatic members of a hypophosphatasia kindred. Clin. Chun. Acta 1991, 202:141-148.
    • (1991) Clin. Chun. Acta , vol.202 , pp. 141-148
    • Macfarlane, J.D.1    Poorthuis, B.J.2    Mulivor, R.A.3    Caswell, A.M.4
  • 157
    • 0018640893 scopus 로고
    • Quantification of human plasma inorganic pyrophosphate. II. Biologic variables
    • Ryan L.M., Kozin F., McCarty D.J. Quantification of human plasma inorganic pyrophosphate. II. Biologic variables. Arthritis Rheum. 1979, 22:892-895.
    • (1979) Arthritis Rheum. , vol.22 , pp. 892-895
    • Ryan, L.M.1    Kozin, F.2    McCarty, D.J.3
  • 158
    • 0018636286 scopus 로고
    • Quantification of human plasma inorganic pyrophosphate. I. Normal values in osteoarthritis and calcium pyrophosphate dihydrate crystal deposition disease
    • Ryan L.M., Kozin F., McCarty D.J. Quantification of human plasma inorganic pyrophosphate. I. Normal values in osteoarthritis and calcium pyrophosphate dihydrate crystal deposition disease. Arthritis Rheum. 1979, 22:886-891.
    • (1979) Arthritis Rheum. , vol.22 , pp. 886-891
    • Ryan, L.M.1    Kozin, F.2    McCarty, D.J.3
  • 159
    • 0017759124 scopus 로고
    • Analysis of inorganic pyrophosphate at the picomole level
    • Cheung C.P., Suhadolnik R.J. Analysis of inorganic pyrophosphate at the picomole level. Anal. Biochem. 1977, 83:61-63.
    • (1977) Anal. Biochem. , vol.83 , pp. 61-63
    • Cheung, C.P.1    Suhadolnik, R.J.2
  • 160
    • 0025641050 scopus 로고
    • Increased plasma pyridoxal-5'-phosphate levels before and after pyridoxine loading in carriers of perinatalJinfantile hypophosphatasia
    • Chodirker B.N., Coburn S.P., Seargeant L.E., Whyte M.P., Greenberg C.R. Increased plasma pyridoxal-5'-phosphate levels before and after pyridoxine loading in carriers of perinatalJinfantile hypophosphatasia. J.Inherit. Metab. Dis. 1990, 13:891-896.
    • (1990) J.Inherit. Metab. Dis. , vol.13 , pp. 891-896
    • Chodirker, B.N.1    Coburn, S.P.2    Seargeant, L.E.3    Whyte, M.P.4    Greenberg, C.R.5
  • 161
    • 0031972544 scopus 로고    scopus 로고
    • Relationship between serum alkaline phosphatase and pyridoxal-5'-phosphate levels in hypophosphatasia
    • Iqbal S.J., Brain A., Reynolds T.M., Penny M., Holland S. Relationship between serum alkaline phosphatase and pyridoxal-5'-phosphate levels in hypophosphatasia. Clin. Set (Colch.) 1998, 94:203-206.
    • (1998) Clin. Set (Colch.) , vol.94 , pp. 203-206
    • Iqbal, S.J.1    Brain, A.2    Reynolds, T.M.3    Penny, M.4    Holland, S.5
  • 162
    • 0032988592 scopus 로고    scopus 로고
    • Red-cell thiamine pyrophosphate levels in hypophosphatasia
    • Iqbal S.J., Talwar D., Davies T. Red-cell thiamine pyrophosphate levels in hypophosphatasia. J.Inherit. Metab. Dis. 1999, 22:95-96.
    • (1999) J.Inherit. Metab. Dis. , vol.22 , pp. 95-96
    • Iqbal, S.J.1    Talwar, D.2    Davies, T.3
  • 163
    • 0022381584 scopus 로고
    • Histologic and ultrastructural studies on the mineralization process in hypophosphatasia
    • Ornoy A., Adomian G.E., Rimoin D.L. Histologic and ultrastructural studies on the mineralization process in hypophosphatasia. Am. J. Med. Genet. 1985, 22:743-758.
    • (1985) Am. J. Med. Genet. , vol.22 , pp. 743-758
    • Ornoy, A.1    Adomian, G.E.2    Rimoin, D.L.3
  • 164
    • 0030696783 scopus 로고    scopus 로고
    • Matrix vesicles in osteomalacic hypophosphatasia bone contain apatite-like mineral crystals
    • Anderson H.C., Hsu H.H., Morris D.C., Fedde K.N., Whyte M.P. Matrix vesicles in osteomalacic hypophosphatasia bone contain apatite-like mineral crystals. Am. J. Pathol 1997, 151:1555-1561.
    • (1997) Am. J. Pathol , vol.151 , pp. 1555-1561
    • Anderson, H.C.1    Hsu, H.H.2    Morris, D.C.3    Fedde, K.N.4    Whyte, M.P.5
  • 165
    • 0026507227 scopus 로고
    • Evidence for specific interaction between matrix vesicle proteins and the connective tissue matrix
    • Wu L.N., Genge B.R., Wuthier R.E. Evidence for specific interaction between matrix vesicle proteins and the connective tissue matrix. Bone Miner. 1992, 17:247-252.
    • (1992) Bone Miner. , vol.17 , pp. 247-252
    • Wu, L.N.1    Genge, B.R.2    Wuthier, R.E.3
  • 166
    • 0027364067 scopus 로고
    • Evidence against a role for alkaline phosphatase in the dephosphorylation of plasma membrane proteins: Hypophosphatasia fibroblast study
    • Fedde K.N., Michel M.P., Whyte M.P. Evidence against a role for alkaline phosphatase in the dephosphorylation of plasma membrane proteins: Hypophosphatasia fibroblast study. J.Cell Biochem. 1993, 53:43-50.
    • (1993) J.Cell Biochem. , vol.53 , pp. 43-50
    • Fedde, K.N.1    Michel, M.P.2    Whyte, M.P.3
  • 167
    • 0011322884 scopus 로고
    • A missense mutation in the human liverJboneJkidney alkaline phosphatase gene causing a lethal form of hypophosphatasia
    • Weiss M.J., Cole D.E., Ray K., Whyte M.P., Lafferty M.A., Mulivor R.A., Harris H. A missense mutation in the human liverJboneJkidney alkaline phosphatase gene causing a lethal form of hypophosphatasia. Proc. Natl Acad. Sci. USA 1988, 85:7666-7669.
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 7666-7669
    • Weiss, M.J.1    Cole, D.E.2    Ray, K.3    Whyte, M.P.4    Lafferty, M.A.5    Mulivor, R.A.6    Harris, H.7
  • 168
    • 0027337789 scopus 로고
    • The Ala-161→Thr substitution in Escherichia coli alkaline phosphatase does not result in loss of enzymatic activity although the homologous mutation in huma
    • Chaidaroglou A., Kantrowitz E.R. The Ala-161→Thr substitution in Escherichia coli alkaline phosphatase does not result in loss of enzymatic activity although the homologous mutation in huma. Biochem. Biophys. Res. Commun. 1993, 193:1104-1109.
    • (1993) Biochem. Biophys. Res. Commun. , vol.193 , pp. 1104-1109
    • Chaidaroglou, A.1    Kantrowitz, E.R.2
  • 169
    • 0026713191 scopus 로고
    • Different missense mutations at the tissue-nonspecific alkaline phosphatase gene locus in autosomal reces-sively inherited forms of mild and severe hypophosph
    • Henthorn P.S., Raducha M., Fedde K.N., Lafferty M.A., Whyte M.P. Different missense mutations at the tissue-nonspecific alkaline phosphatase gene locus in autosomal reces-sively inherited forms of mild and severe hypophosph. Proc. Natl. Acad. Sci. USA 1992, 89:9924-9928.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 9924-9928
    • Henthorn, P.S.1    Raducha, M.2    Fedde, K.N.3    Lafferty, M.A.4    Whyte, M.P.5
  • 170
  • 171
    • 0028024690 scopus 로고
    • Novel missense and frameshift mutations in the tissue-nonspecific alkaline phosphatase gene in a Japanese patient with hypophosphatasia
    • Orimo H., Hayashi Z., Watanabe A., Hirayama T., Hirayama T., Shimada T. Novel missense and frameshift mutations in the tissue-nonspecific alkaline phosphatase gene in a Japanese patient with hypophosphatasia. Hum. Mol. Genet. 1994, 3:1683-1684.
    • (1994) Hum. Mol. Genet. , vol.3 , pp. 1683-1684
    • Orimo, H.1    Hayashi, Z.2    Watanabe, A.3    Hirayama, T.4    Hirayama, T.5    Shimada, T.6
  • 172
    • 0028861934 scopus 로고
    • Infantile hypophosphatasia: Successful prenatal assessment by testing for tissue-non-specific alkaline phosphatase isoenzyme gene mutations
    • Henthorn P.S., Whyte M.P. Infantile hypophosphatasia: Successful prenatal assessment by testing for tissue-non-specific alkaline phosphatase isoenzyme gene mutations. Prenat. Diagn. 1995, 15:1001-1006.
    • (1995) Prenat. Diagn. , vol.15 , pp. 1001-1006
    • Henthorn, P.S.1    Whyte, M.P.2
  • 179
    • 0036353341 scopus 로고    scopus 로고
    • Denaturing gradient gel electro-phoresis analysis of the tissue nonspecific alkaline phosphatase isoenzyme gene in hypophosphatasia
    • Mumm S., Jones J., Finnegan P., Henthorn P.S., Podgornik M.N., Whyte M.P. Denaturing gradient gel electro-phoresis analysis of the tissue nonspecific alkaline phosphatase isoenzyme gene in hypophosphatasia. Mol Genet. Metab. 2002, 75:143-153.
    • (2002) Mol Genet. Metab. , vol.75 , pp. 143-153
    • Mumm, S.1    Jones, J.2    Finnegan, P.3    Henthorn, P.S.4    Podgornik, M.N.5    Whyte, M.P.6
  • 180
    • 0027062860 scopus 로고
    • Missense mutations of the tissue-nonspecific alkaline phosphatase gene in hypophosphatasia
    • Henthorn P.S., Whyte M.P. Missense mutations of the tissue-nonspecific alkaline phosphatase gene in hypophosphatasia. Clin. Chem. 1992, 38:2501-2505.
    • (1992) Clin. Chem. , vol.38 , pp. 2501-2505
    • Henthorn, P.S.1    Whyte, M.P.2
  • 182
    • 0031613674 scopus 로고    scopus 로고
    • A novel missense mutation of the tissue-nonspecific alkaline phosphatase gene detected in a patient with hypophosphatasia
    • Sugimoto N., Iwamoto S., Hoshino Y., Kajii E. A novel missense mutation of the tissue-nonspecific alkaline phosphatase gene detected in a patient with hypophosphatasia. J.Hum. Genet. 1998, 43:160-164.
    • (1998) J.Hum. Genet. , vol.43 , pp. 160-164
    • Sugimoto, N.1    Iwamoto, S.2    Hoshino, Y.3    Kajii, E.4
  • 183
    • 0034335426 scopus 로고    scopus 로고
    • Asp361Val mutant of alkaline phosphatase found in patients with dominantly inherited hypophosphatasia inhibits the activity of the wild-type enzyme
    • Muller H.L., Yamazaki M., Michigami T., Kageyama T., Schonau E., Schneider P., Ozono K. Asp361Val mutant of alkaline phosphatase found in patients with dominantly inherited hypophosphatasia inhibits the activity of the wild-type enzyme. J.Clin. Endocrinol. Metab. 2000, 85:743-747.
    • (2000) J.Clin. Endocrinol. Metab. , vol.85 , pp. 743-747
    • Muller, H.L.1    Yamazaki, M.2    Michigami, T.3    Kageyama, T.4    Schonau, E.5    Schneider, P.6    Ozono, K.7
  • 184
    • 0025265856 scopus 로고
    • Infantile hypophosphatasia: Autosomal recessive transmission to two related sibships
    • Moore C.A., Ward J.C., Rivas M.L., Magill H.L., Whyte M.P. Infantile hypophosphatasia: Autosomal recessive transmission to two related sibships. Am. J. Med. Genet. 1990, 36:15-22.
    • (1990) Am. J. Med. Genet. , vol.36 , pp. 15-22
    • Moore, C.A.1    Ward, J.C.2    Rivas, M.L.3    Magill, H.L.4    Whyte, M.P.5
  • 185
    • 0029115393 scopus 로고
    • Mice lacking tissue non-specific alkaline phosphatase die from seizures due to defective metabolism of vitamin B-6
    • Waymire K.G., Mahuren J.D., Jaje J.M., Guilarte T.R., Coburn S.P., MacGregor G.R. Mice lacking tissue non-specific alkaline phosphatase die from seizures due to defective metabolism of vitamin B-6. Nature Genet. 1995, 11:45-51.
    • (1995) Nature Genet. , vol.11 , pp. 45-51
    • Waymire, K.G.1    Mahuren, J.D.2    Jaje, J.M.3    Guilarte, T.R.4    Coburn, S.P.5    MacGregor, G.R.6
  • 186
    • 1842409589 scopus 로고    scopus 로고
    • In-activation of two mouse alkaline phosphatase genes and establishment of a model of infantile hypophosphatasia
    • Narisawa S., Frohlander N., Millan J.L. In-activation of two mouse alkaline phosphatase genes and establishment of a model of infantile hypophosphatasia. Dev. Dyn. 1997, 208:432-446.
    • (1997) Dev. Dyn. , vol.208 , pp. 432-446
    • Narisawa, S.1    Frohlander, N.2    Millan, J.L.3
  • 187
    • 0035160863 scopus 로고    scopus 로고
    • Abnormal vitamin B6 metabolism in alkaline phosphatase knock-out mice causes multiple abnormalities, but not the impaired bone mineral ization
    • Narisawa S., Wennberg C., Millan J.L. Abnormal vitamin B6 metabolism in alkaline phosphatase knock-out mice causes multiple abnormalities, but not the impaired bone mineral ization. J.Pathol 2001, 193:125-133.
    • (2001) J.Pathol , vol.193 , pp. 125-133
    • Narisawa, S.1    Wennberg, C.2    Millan, J.L.3
  • 192
    • 0009761007 scopus 로고
    • Failure of hyper-phosphatasemia by intravenous infusion of purified placental alkaline phosphatase (ALP) to correct severe hypophosphatasia: Evidence against
    • Whyte M.P., Habib D., Coburn S.P., Tecklenburg F., Ryan L.M., Fedde K.N., Stinson R.A. Failure of hyper-phosphatasemia by intravenous infusion of purified placental alkaline phosphatase (ALP) to correct severe hypophosphatasia: Evidence against. J.Bone Miner. Res. 1992, 7(Suppl. 1):252.
    • (1992) J.Bone Miner. Res. , vol.7 , Issue.SUPPL. 1 , pp. 252
    • Whyte, M.P.1    Habib, D.2    Coburn, S.P.3    Tecklenburg, F.4    Ryan, L.M.5    Fedde, K.N.6    Stinson, R.A.7
  • 193
    • 0033892896 scopus 로고    scopus 로고
    • Infantile hypophosphatasia: Disappointing results of treatment
    • Deeb A.A., Bruce S.N., Morris A.A., Cheetham T.D. Infantile hypophosphatasia: Disappointing results of treatment. Acta Paediatr. 2000, 89:730-733.
    • (2000) Acta Paediatr. , vol.89 , pp. 730-733
    • Deeb, A.A.1    Bruce, S.N.2    Morris, A.A.3    Cheetham, T.D.4
  • 194
    • 0031964993 scopus 로고    scopus 로고
    • Increase in leukocyte alkaline phosphatase in a patient with hypophosphatasia during pregnancy
    • Iqbal S.J. Increase in leukocyte alkaline phosphatase in a patient with hypophosphatasia during pregnancy. J.Inherit. Metab. Dis. 1998, 21:83-84.
    • (1998) J.Inherit. Metab. Dis. , vol.21 , pp. 83-84
    • Iqbal, S.J.1
  • 196
    • 0030827641 scopus 로고    scopus 로고
    • Infantile hypophosphatasia: Treatment options to control hypercalcemia, hypercalciuria, and chronic bone demineralization
    • Barcia J.P., Strife C.F., Langman C.B. Infantile hypophosphatasia: Treatment options to control hypercalcemia, hypercalciuria, and chronic bone demineralization. J.Pediatr. 1997, 130:825-828.
    • (1997) J.Pediatr. , vol.130 , pp. 825-828
    • Barcia, J.P.1    Strife, C.F.2    Langman, C.B.3
  • 197
    • 0032836399 scopus 로고    scopus 로고
    • Treatment of childhood hypophosphatasia with nonsteroidal antiinflammatory drugs
    • Girschick H.J., Seyberth H.W., Huppertz H.I. Treatment of childhood hypophosphatasia with nonsteroidal antiinflammatory drugs. Bone 1999, 25:603-607.
    • (1999) Bone , vol.25 , pp. 603-607
    • Girschick, H.J.1    Seyberth, H.W.2    Huppertz, H.I.3
  • 199
    • 0032852456 scopus 로고    scopus 로고
    • Mechanical failure of a gamma nail in a patient with an impending pathologic subtrochanteric fracture
    • Randle J.A., Meisami-Fard B., McKee M.D. Mechanical failure of a gamma nail in a patient with an impending pathologic subtrochanteric fracture. Can. J. Surg. 1999, 42:384-386.
    • (1999) Can. J. Surg. , vol.42 , pp. 384-386
    • Randle, J.A.1    Meisami-Fard, B.2    McKee, M.D.3
  • 200
    • 0020393275 scopus 로고
    • Adult hypophosphatasia: Generalized deficiency of alkaline phosphatase activity demonstrated with cultured skin fibroblasts
    • Whyte M.P., Vrabel L.A., Schwartz T.D. Adult hypophosphatasia: Generalized deficiency of alkaline phosphatase activity demonstrated with cultured skin fibroblasts. Trans. Assoc. Am. Physicians 1982, 95:253-263.
    • (1982) Trans. Assoc. Am. Physicians , vol.95 , pp. 253-263
    • Whyte, M.P.1    Vrabel, L.A.2    Schwartz, T.D.3
  • 202
    • 0019421502 scopus 로고
    • Heterogeneity of adult hypophosphatasia. Report of severe and mild cases
    • Weinstein R.S., Whyte M.P. Heterogeneity of adult hypophosphatasia. Report of severe and mild cases. Arch. Intern. Med. 1981, 141:727-731.
    • (1981) Arch. Intern. Med. , vol.141 , pp. 727-731
    • Weinstein, R.S.1    Whyte, M.P.2
  • 203
    • 0023118111 scopus 로고
    • The physical characteristics and enzymatic modification of fetal intestinal alkaline phosphatase in amniotic fluid
    • Moss D.W., Whitaker K.B. The physical characteristics and enzymatic modification of fetal intestinal alkaline phosphatase in amniotic fluid. Clin. Biochem. 1987, 20:9-12.
    • (1987) Clin. Biochem. , vol.20 , pp. 9-12
    • Moss, D.W.1    Whitaker, K.B.2
  • 204
    • 0023271873 scopus 로고
    • Isoenzymes of alkaline phosphatase in amniotic fluid: Implications in prenatal screening for cystic fibrosis
    • Stinson R.A., McPhee J.L. Isoenzymes of alkaline phosphatase in amniotic fluid: Implications in prenatal screening for cystic fibrosis. Clin. Biochem. 1987, 20:241-244.
    • (1987) Clin. Biochem. , vol.20 , pp. 241-244
    • Stinson, R.A.1    McPhee, J.L.2
  • 205
    • 0022345468 scopus 로고
    • First trimester diagnosis of hypophosphatasia with a monoclonal antibody to the liverJboneJ kidney isoenzyme of alkaline phosphatase
    • Warren R.C., McKenzie C.F., Rodeck C.H., Moscoso G., Brock D.J., Barron L. First trimester diagnosis of hypophosphatasia with a monoclonal antibody to the liverJboneJ kidney isoenzyme of alkaline phosphatase. Lancet 1985, 2:856-858.
    • (1985) Lancet , vol.2 , pp. 856-858
    • Warren, R.C.1    McKenzie, C.F.2    Rodeck, C.H.3    Moscoso, G.4    Brock, D.J.5    Barron, L.6
  • 208
    • 0032818867 scopus 로고    scopus 로고
    • Correlation of alkaline phosphatase (ALP) determination and analysis of the tissue nonspecific ALP gene in prenatal diagnosis of severe hypophosphatasia
    • Mornet E., Muller F., Ngo S., Taillandier A., Simon-Bouy B., Maire L., Oury J.F. Correlation of alkaline phosphatase (ALP) determination and analysis of the tissue nonspecific ALP gene in prenatal diagnosis of severe hypophosphatasia. Prenat. Diagn. 1999, 19:755-757.
    • (1999) Prenat. Diagn. , vol.19 , pp. 755-757
    • Mornet, E.1    Muller, F.2    Ngo, S.3    Taillandier, A.4    Simon-Bouy, B.5    Maire, L.6    Oury, J.F.7
  • 209
    • 0032717995 scopus 로고    scopus 로고
    • Perinatal hypophosphatasia: Diagnosis and detection of heterozygote carriers within the family
    • Gehring B., Mornet E., Plath H., Hansmann M., Bartmann P., Brenner R.E. Perinatal hypophosphatasia: Diagnosis and detection of heterozygote carriers within the family. Clin. Genet. 1999, 56:313-317.
    • (1999) Clin. Genet. , vol.56 , pp. 313-317
    • Gehring, B.1    Mornet, E.2    Plath, H.3    Hansmann, M.4    Bartmann, P.5    Brenner, R.E.6
  • 211
    • 0033615462 scopus 로고    scopus 로고
    • Mild hypophosphatasia mimicking severe osteogenesis imperfecta in utero: Bent but not broken
    • Pauli R.M., Modaff P., Sipes S.L., Whyte M.P. Mild hypophosphatasia mimicking severe osteogenesis imperfecta in utero: Bent but not broken. Am. J. Med. Genet. 1999, 86:434-438.
    • (1999) Am. J. Med. Genet. , vol.86 , pp. 434-438
    • Pauli, R.M.1    Modaff, P.2    Sipes, S.L.3    Whyte, M.P.4
  • 216
    • 0025021039 scopus 로고
    • The human alkaline phosphatases: What we know and what we don't know
    • Harris H. The human alkaline phosphatases: What we know and what we don't know. Clin. Chim. Acta 1990, 186:133-150.
    • (1990) Clin. Chim. Acta , vol.186 , pp. 133-150
    • Harris, H.1
  • 217
    • 0023857873 scopus 로고
    • A monoclonal antibody capture assay for intestinal alkaline phosphatase and the measurement of this isoenzyme in pregnancy
    • Bailyes E.M., Seymour P.M., Fulton I., Price C.P., Luzio J.P. A monoclonal antibody capture assay for intestinal alkaline phosphatase and the measurement of this isoenzyme in pregnancy. Clin. Chim. Acta 1988, 172:261-21 A.
    • (1988) Clin. Chim. Acta , vol.172
    • Bailyes, E.M.1    Seymour, P.M.2    Fulton, I.3    Price, C.P.4    Luzio, J.P.5
  • 218
    • 0025184825 scopus 로고
    • Alkaline phosphatase (tissue-nonspecific isoenzyme) is a phosphoethanolamine and pyridoxal-S'-phosphate ectophosphatase: Normal and hypophosphatasia fibroblas
    • Fedde K.N., Whyte M.P. Alkaline phosphatase (tissue-nonspecific isoenzyme) is a phosphoethanolamine and pyridoxal-S'-phosphate ectophosphatase: Normal and hypophosphatasia fibroblas. Am. J. Hum. Genet. 1990, 47:767-775.
    • (1990) Am. J. Hum. Genet. , vol.47 , pp. 767-775
    • Fedde, K.N.1    Whyte, M.P.2
  • 219
    • 0033407479 scopus 로고    scopus 로고
    • Activity increase after extraction of alkaline phosphatase from human osteoblastic membranes by nonionic detergents: Influence of age and sex
    • Bourrat C., Radisson J., Chavassieux P., Azzar G., Roux B., Meunier P.J. Activity increase after extraction of alkaline phosphatase from human osteoblastic membranes by nonionic detergents: Influence of age and sex. Calcif. Tissue Int. 2000, 66:22-28.
    • (2000) Calcif. Tissue Int. , vol.66 , pp. 22-28
    • Bourrat, C.1    Radisson, J.2    Chavassieux, P.3    Azzar, G.4    Roux, B.5    Meunier, P.J.6
  • 220
    • 0026100168 scopus 로고
    • Phenotype suppression: A postulated molecular mechanism for mediating the relationship of proliferation and differentiation by FosJJun interactions at AP-1 si
    • Lian J.B., Stein G.S., Bortell R., Owen T.A. Phenotype suppression: A postulated molecular mechanism for mediating the relationship of proliferation and differentiation by FosJJun interactions at AP-1 si. J.Cell Biochem. 1991, 45:9-14.
    • (1991) J.Cell Biochem. , vol.45 , pp. 9-14
    • Lian, J.B.1    Stein, G.S.2    Bortell, R.3    Owen, T.A.4
  • 221
    • 0035223876 scopus 로고    scopus 로고
    • Stretch-mediated activation of selective MAPK subtypes and potentiation of AP-1 binding in human osteoblastic cells
    • Peverali F.A., Basdra E.K., Papavassiliou A.G. Stretch-mediated activation of selective MAPK subtypes and potentiation of AP-1 binding in human osteoblastic cells. Mol. Med. 2001, 7:68-78.
    • (2001) Mol. Med. , vol.7 , pp. 68-78
    • Peverali, F.A.1    Basdra, E.K.2    Papavassiliou, A.G.3
  • 222
    • 0028971143 scopus 로고
    • Matlnd and Matlnspector: New fast and versatile tools for detection of consensus matches in nucleotide sequence data
    • Quandt K., Freeh K., Karas H., Wingender E., Werner T. Matlnd and Matlnspector: New fast and versatile tools for detection of consensus matches in nucleotide sequence data. Nucleic Acids Res. 1995, 23:4878-4884.
    • (1995) Nucleic Acids Res. , vol.23 , pp. 4878-4884
    • Quandt, K.1    Freeh, K.2    Karas, H.3    Wingender, E.4    Werner, T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.