메뉴 건너뛰기




Volumn 17, Issue 6, 2012, Pages 1996-2023

Protein-mediated enamel mineralization

Author keywords

Amelogenesis; Amelogenin; Biomineralization; Enamel; Review; Tooth

Indexed keywords

MAMMALIA;

EID: 84860432521     PISSN: 27686701     EISSN: 27686698     Source Type: Journal    
DOI: 10.2741/4034     Document Type: Article
Times cited : (187)

References (205)
  • 2
    • 45549085818 scopus 로고    scopus 로고
    • Mammalian enamel formation
    • Ed Astrid Sigel, H. Sigel&R. K. O. Sigel. John Wiley & Sons, Ltd, Chichester
    • J. Moradian-Oldak and M. L. Paine: Mammalian Enamel Formation. In: Metal Ions In Life Sciences: Ed Astrid Sigel, H. Sigel&R. K. O. Sigel. John Wiley & Sons, Ltd, Chichester (2008).
    • (2008) Metal Ions in Life Sciences
    • Moradian-Oldak, J.1    Paine, M.L.2
  • 3
    • 0033617953 scopus 로고    scopus 로고
    • The structural biology of the developing dental enamel matrix
    • DOI 10.1006/jsbi.1999.4130
    • A. Fincham, J. Moradian-Oldak and J. Simmer: The structural biology of the developing dental enamel matrix. J Struct Biol, 126 (3), 270-99 (1999). (Pubitemid 29402573)
    • (1999) Journal of Structural Biology , vol.126 , Issue.3 , pp. 270-299
    • Fincham, A.G.1    Moradian-Oldak, J.2    Simmer, J.P.3
  • 4
    • 0031968437 scopus 로고    scopus 로고
    • Cellular and chemical events during enamel maturation
    • C. Smith: Cellular and chemical events during enamel maturation. Crit Rev Oral Biol Med, 9, 128-161 (1998). (Pubitemid 28225853)
    • (1998) Critical Reviews in Oral Biology and Medicine , vol.9 , Issue.2 , pp. 128-161
    • Smith, C.E.1
  • 6
    • 0017920977 scopus 로고
    • Four chemically distinct stages in developing enamel from bovine incisor teeth
    • C. Robinson, P. Fuchs, D. Deutsch and J. A. Weatherell: Four chemically distinct stages in developing enamel from bovine incisor teeth. Caries Res, 12 (1), 1-11 (1978). (Pubitemid 8216338)
    • (1978) Caries Research , vol.12 , Issue.1 , pp. 1-11
    • Robinson, C.1    Fuchs, P.2    Deutsch, D.3    Weatherell, J.A.4
  • 7
    • 0018444863 scopus 로고
    • Patterns of enamel maturation
    • P. L. Glick: Patterns of enamel maturation. J Dent Res, 58 (Spec Issue B), 883-95 (1979).
    • (1979) J Dent Res , vol.58 , Issue.SPECL. B , pp. 883-895
    • Glick, P.L.1
  • 8
    • 0030633401 scopus 로고    scopus 로고
    • Microstructure of enamel
    • John Wiley & Sons. New York
    • A. Boyde: Microstructure of Enamel. In: Dental Enamel. Ciba Foundation Symposium 205, John Wiley & Sons., New York (1997).
    • (1997) Dental Enamel. Ciba Foundation Symposium , vol.205
    • Boyde, A.1
  • 9
    • 0033428813 scopus 로고    scopus 로고
    • Biomimetics: Materials fabrication through biology
    • M. Sarikaya: Biomimetics: materials fabrication through biology. Proc Natl Acad Sci USA, 96, 13611-13614 (1999).
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 13611-13614
    • Sarikaya, M.1
  • 10
    • 34147127516 scopus 로고    scopus 로고
    • Enamel inspired nanocomposite fabrication through amelogenin supramolecular assembly
    • DOI 10.1016/j.biomaterials.2007.02.016, PII S0142961207001524
    • Y. Fan, Z. Sun, R. Wang, C. Abbott and J. Moradian-Oldak: Enamel inspired nanocomposite fabrication through amelogenin supramolecular assembly. Biomaterials, 28 (19), 3034-42 (2007). (Pubitemid 46560864)
    • (2007) Biomaterials , vol.28 , Issue.19 , pp. 3034-3042
    • Fan, Y.W.1    Sun, Z.2    Wang, R.3    Abbott, C.4    Moradian-Oldak, J.5
  • 11
    • 12044256704 scopus 로고
    • Molecular tectonics in biomineralization and biomimetic materials chemistry
    • S. Mann: Molecular tectonics in biomineralization and biomimetic materials chemistry. Nature, 365, 499-505 (1993).
    • (1993) Nature , vol.365 , pp. 499-505
    • Mann, S.1
  • 12
    • 57349116196 scopus 로고    scopus 로고
    • Biomimetic systems for hydroxyapatite mineralization inspired by bone and Enamel
    • L. C. Palmer, C. J. Newcomb, S. R. Kaltz, E. D. Spoerke and S. I. Stupp: Biomimetic Systems for Hydroxyapatite Mineralization Inspired By Bone and Enamel. Chemical Reviews, 108 (11), 4754-4783 (2008).
    • (2008) Chemical Reviews , vol.108 , Issue.11 , pp. 4754-4783
    • Palmer, L.C.1    Newcomb, C.J.2    Kaltz, S.R.3    Spoerke, E.D.4    Stupp, S.I.5
  • 13
    • 0035205165 scopus 로고    scopus 로고
    • Mechanical properties of the dentinoenamel junction: AFM studies of nanohardness, elastic modulus, and fracture
    • G. W. Marshall, M. Balooch, R. R. Gallagher, S. A. Gansky and S. J. Marshall: Mechanical properties of the dentinoenamel junction: AFM studies of nanohardness, elastic modulus, and fracture. J Biomed Mater Res, 54 (1), 87-95 (2001).
    • (2001) J Biomed Mater Res , vol.54 , Issue.1 , pp. 87-95
    • Marshall, G.W.1    Balooch, M.2    Gallagher, R.R.3    Gansky, S.A.4    Marshall, S.J.5
  • 14
    • 0035142256 scopus 로고    scopus 로고
    • Mechanical properties of human dental enamel on the nanometre scale
    • DOI 10.1016/S0003-9969(00)00089-3, PII S0003996900000893
    • S. Habelitz, S. J. Marshall, G. W. Marshall, Jr. and M. Balooch: Mechanical properties of human dental enamel on the nanometre scale. Arch Oral Biol, 46 (2), 173-83 (2001). (Pubitemid 32121130)
    • (2001) Archives of Oral Biology , vol.46 , Issue.2 , pp. 173-183
    • Habelitz, S.1    Marshall, S.J.2    Marshall Jr., G.W.3    Balooch, M.4
  • 15
    • 0034990305 scopus 로고    scopus 로고
    • Biological organization of hydroxyapatite crystallites into a fibrous continuum toughens and controls anisotropy in human enamel
    • S. N. White, W. Luo, M. L. Paine, H. Fong, M. Sarikaya and M. L. Snead: Biological organization of hydroxyapitite crystallites into a fibrous continuum toughens and controls anisotropy in human enamel. J Dent Res, 80, 321-326 (2001). (Pubitemid 32501332)
    • (2001) Journal of Dental Research , vol.80 , Issue.1 , pp. 321-326
    • White, S.N.1    Luo, W.2    Paine, M.L.3    Fong, H.4    Sarikaya, M.5    Snead, M.L.6
  • 16
    • 41949117828 scopus 로고    scopus 로고
    • New observations of the hierarchical structure of human enamel, from nanoscale to microscale
    • F. Z. Cui and J. Ge: New observations of the hierarchical structure of human enamel, from nanoscale to microscale. Journal of Tissue Engineering and Regenerative Medicine, 1 (3), 185-191 (2007).
    • (2007) Journal of Tissue Engineering and Regenerative Medicine , vol.1 , Issue.3 , pp. 185-191
    • Cui, F.Z.1    Ge, J.2
  • 17
    • 33646513681 scopus 로고    scopus 로고
    • Growth of ameloblast-lineage cells in a three-dimensional Matrigel environment
    • DOI 10.1111/j.1600-0722.2006.00308.x
    • W. Li, D. Machule, C. Gao and P. K. DenBesten: Growth of ameloblast-lineage cells in a three-dimensional Matrigel environment. Eur J Oral Sci, 114 Suppl 1, 159-63; discussion 164-5, 380-1 (2006). (Pubitemid 43709430)
    • (2006) European Journal of Oral Sciences , vol.114 , Issue.SUPPL. 1 , pp. 159-163
    • Li, W.1    Machule, D.2    Gao, C.3    DenBesten, P.K.4
  • 18
    • 33644788720 scopus 로고    scopus 로고
    • Genes and related proteins involved in amelogenesis imperfecta
    • DOI 10.1177/154405910508401206
    • G. Stephanopoulos, M. E. Garefalaki and K. Lyroudia: Genes and related proteins involved in amelogenesis imperfecta. J Dent Res, 84 (12), 1117-26 (2005). (Pubitemid 43827778)
    • (2005) Journal of Dental Research , vol.84 , Issue.12 , pp. 1117-1126
    • Stephanopoulos, G.1    Garefalaki, M.-E.2    Lyroudia, K.3
  • 19
    • 34547100302 scopus 로고    scopus 로고
    • Developmental biology and genetics of dental malformations
    • J. C. Hu and J. P. Simmer: Developmental biology and genetics of dental malformations. Orthod Craniofac Res, 10 (2), 45-52 (2007).
    • (2007) Orthod Craniofac Res , vol.10 , Issue.2 , pp. 45-52
    • Hu, J.C.1    Simmer, J.P.2
  • 20
    • 34347404486 scopus 로고    scopus 로고
    • The origin and evolution of enamel mineralization genes
    • DOI 10.1159/000102679
    • J. Y. Sire, T. Davit-Beal, S. Delgado and X. Gu: The origin and evolution of enamel mineralization genes. Cells Tissues Organs, 186 (1), 25-48 (2007). (Pubitemid 47026715)
    • (2007) Cells Tissues Organs , vol.186 , Issue.1 , pp. 25-48
    • Sire, J.-Y.1    Davit-Beal, T.2    Delgado, S.3    Gu, X.4
  • 21
    • 33748794760 scopus 로고    scopus 로고
    • Role of macromolecular assembly of enamel matrix proteins in enamel formation
    • H. C. Margolis, E. Beniash and C. E. Fowler: Role of macromolecular assembly of enamel matrix proteins in enamel formation. J Dent Res, 85 (9), 775-93 (2006). (Pubitemid 44409025)
    • (2006) Journal of Dental Research , vol.85 , Issue.9 , pp. 775-793
    • Margolis, H.C.1    Beniash, E.2    Fowler, C.E.3
  • 29
    • 0029317758 scopus 로고
    • Homeobox genes and growth factors in regulation of craniofacial and tooth morphogenesis
    • I. Thesleff: Homeobox genes and growth factors in regulation of craniofacial and tooth morphogenesis. ACTA Odontol Scand, 53, 129-134 (1995).
    • (1995) ACTA Odontol Scand , vol.53 , pp. 129-134
    • Thesleff, I.1
  • 30
    • 0016157794 scopus 로고
    • Morphological classification of rat incisor ameloblasts
    • H. Warshawsky and C. E. Smith: Morphological classification of rat incisor ameloblasts. Anat Rec, 179 (4), 423-46 (1974).
    • (1974) Anat Rec , vol.179 , Issue.4 , pp. 423-446
    • Warshawsky, H.1    Smith, C.E.2
  • 31
    • 0001181644 scopus 로고
    • An electron microscopic study of the amelogenesis in human teeth. I. The fine structure of the ameloblasts
    • E. Ronnholm: An electron microscopic study of the amelogenesis in human teeth. I. The fine structure of the ameloblasts. J Ultrastruct Res, 6, 229-48 (1962).
    • (1962) J Ultrastruct Res , vol.6 , pp. 229-248
    • Ronnholm, E.1
  • 32
    • 0001181646 scopus 로고
    • The amelogenesis of human teeth as revealed by electron microscopy. II. The development of the enamel crystallites
    • E. Ronnholm: The amelogenesis of human teeth as revealed by electron microscopy. II. The development of the enamel crystallites. J Ultrastruct Res, 6, 249-303 (1962).
    • (1962) J Ultrastruct Res , vol.6 , pp. 249-303
    • Ronnholm, E.1
  • 33
    • 63649098101 scopus 로고    scopus 로고
    • Transient amorphous calcium phosphate in forming enamel
    • E. Beniash, R. A. Metzler, R. S. K. Lam and P. Gilbert: Transient amorphous calcium phosphate in forming enamel. J Stru Biol, 166 (2), 133-143 (2009).
    • (2009) J Stru Biol , vol.166 , Issue.2 , pp. 133-143
    • Beniash, E.1    Metzler, R.A.2    Lam, R.S.K.3    Gilbert, P.4
  • 35
    • 77949491927 scopus 로고    scopus 로고
    • A survey of carbonic anhydrase mRNA expression in enamel cells
    • R. S. Lacruz, M. Hilvo, I. Kurtz and M. L. Paine: A survey of carbonic anhydrase mRNA expression in enamel cells. Biochem Biophys Res Commun, 393 (4), 883-7 (2010).
    • (2010) Biochem Biophys Res Commun , vol.393 , Issue.4 , pp. 883-887
    • Lacruz, R.S.1    Hilvo, M.2    Kurtz, I.3    Paine, M.L.4
  • 37
    • 0024615494 scopus 로고
    • Human and mouse amelogenin gene loci are on the sex chromosome
    • E. C. Lau, T. Mohandas, L. J. Shapiro, H. C. Slavkin and M. L. Snead: Human and mouse amelogenin gene loci are on the sex chromosome. Genomics, 4, 162-168 (1989).
    • (1989) Genomics , vol.4 , pp. 162-168
    • Lau, E.C.1    Mohandas, T.2    Shapiro, L.J.3    Slavkin, H.C.4    Snead, M.L.5
  • 39
    • 0025732652 scopus 로고
    • Linkage of amelogenin (Amel) to the distal portion of the mouse X chromosome
    • V. M. Chapman, B. T. Keitz, C. M. Disteche, E. C. Lau and M. L. Snead: Linkage of amelogenin (Amel) to the distal portion of the mouse X chromosome. Genomics, 10, 23-28 (1991).
    • (1991) Genomics , vol.10 , pp. 23-28
    • Chapman, V.M.1    Keitz, B.T.2    Disteche, C.M.3    Lau, E.C.4    Snead, M.L.5
  • 41
    • 0036735323 scopus 로고    scopus 로고
    • Expression of alternatively spliced RNA transcripts of amelogenin gene exons 8 and 9 and its end products in the rat incisor
    • O. Baba, N. Takahashi, T. Terashima, W. Li, P. K. DenBesten and Y. Takano: Expression of alternatively spliced RNA transcripts of amelogenin gene exons 8 and 9 and its end products in the rat incisor. J Histochem Cytochem, 50 (9), 1229-36 (2002). (Pubitemid 34988452)
    • (2002) Journal of Histochemistry and Cytochemistry , vol.50 , Issue.9 , pp. 1229-1236
    • Baba, O.1    Takahashi, N.2    Terashima, T.3    Li, W.4    DenBesten, P.K.5    Takano, Y.6
  • 42
    • 13844254352 scopus 로고    scopus 로고
    • Amelogenin: Lessons from evolution
    • DOI 10.1016/j.archoralbio.2004.09.004
    • J. Y. Sire, S. Delgado, D. Fromentin and M. Girondot: Amelogenin: lessons from evolution. Arch Oral Biol, 50 (2), 205-12 (2005). (Pubitemid 40252941)
    • (2005) Archives of Oral Biology , vol.50 , Issue.2 SPEC. ISS. , pp. 205-212
    • Sire, J.-Y.1    Delgado, S.2    Fromentin, D.3    Girondot, M.4
  • 44
    • 0026733254 scopus 로고
    • Bovine amelogenin message heterogeneity: Alternative splicing and Y-chromosomal gene transcription
    • C. W. Gibson, E. E. Golub, W. R. Abrams, G. Shen, W. Ding and J. Rosenbloom: Bovine amelogenin message heterogeneity: alternative splicing and Y-chromosomal gene transcription. Biochemistry, 31 (35), 8384-8 (1992).
    • (1992) Biochemistry , vol.31 , Issue.35 , pp. 8384-8388
    • Gibson, C.W.1    Golub, E.E.2    Abrams, W.R.3    Shen, G.4    Ding, W.5    Rosenbloom, J.6
  • 46
    • 0028846708 scopus 로고
    • A synthetic, chemically modified ribozyme eliminates amelogenin, the major translation product in developing mouse enamel in vivo
    • S. P. Lyngstadaas, S. Risnes, B. S. Sproat, P. S. Thrane and H. P. Prydz: A synthetic, chemically modified ribozyme eliminates amelogenin, the major translation product in developing mouse enamel in vivo. EMBO J., 14 (21), 5224-5229 (1995).
    • (1995) EMBO J. , vol.14 , Issue.21 , pp. 5224-5229
    • Lyngstadaas, S.P.1    Risnes, S.2    Sproat, B.S.3    Thrane, P.S.4    Prydz, H.P.5
  • 47
    • 0027417821 scopus 로고
    • Antisense inhibition of AMEL translation demonstrates supramolecular controls for enamel HAP crystal growth during embryonic mouse molar development
    • T. G. Diekwisch, S. David, P. Bringas, V. Santos and H. C. Slavkin: Antisense inhibition of amelogenin translation demonstrates supramolecular controls for enamel HAP crystal-growth during embryonic mouse molar development. Development, 117, 471-482 (1993). (Pubitemid 23103158)
    • (1993) Development , vol.117 , Issue.2 , pp. 471-482
    • Diekwisch, T.1    David, S.2    Bringas Jr., P.3    Santos, V.4    Slavkin, H.C.5
  • 49
    • 47249099813 scopus 로고    scopus 로고
    • The amelogenin "enamel proteins" and cells in the periodontium
    • C. W. Gibson: The amelogenin "enamel proteins" and cells in the periodontium. Crit Rev Eukaryot Gene Expr, 18 (4), 345-60 (2008). (Pubitemid 351991364)
    • (2008) Critical Reviews in Eukaryotic Gene Expression , vol.18 , Issue.4 , pp. 345-360
    • Gibson, C.W.1
  • 50
    • 0037280016 scopus 로고    scopus 로고
    • Amelogenin gene splice products: Potential signaling molecules
    • DOI 10.1007/s000180300003
    • A. Veis: Amelogenin gene splice products: potential signaling molecules. Cell Mol Life Sci, 60 (1), 38-55 (2003). (Pubitemid 36223116)
    • (2003) Cellular and Molecular Life Sciences , vol.60 , Issue.1 , pp. 38-55
    • Veis, A.1
  • 51
    • 38049079976 scopus 로고    scopus 로고
    • Leucine-rich amelogenin peptide induces osteogenesis in mouse embryonic stem cells
    • R. Warotayanont, D. Zhu, M. L. Snead and Y. Zhou: Leucine-rich amelogenin peptide induces osteogenesis in mouse embryonic stem cells. Biochem Biophys Res Commun, 367 (1), 1-6 (2008).
    • (2008) Biochem Biophys Res Commun , vol.367 , Issue.1 , pp. 1-6
    • Warotayanont, R.1    Zhu, D.2    Snead, M.L.3    Zhou, Y.4
  • 53
    • 0027451541 scopus 로고
    • Amelogenin post-translational modifications: Carboxy-terminal processing and the phosphorylation of bovine and porcine 'TRAP' and 'LRAP' amelogenins
    • DOI 10.1006/bbrc.1993.2468
    • A. G. Fincham and J. Moradian-Oldak: Amelogenin post-translational modifications: carboxy-terminal processing and the phosphorylation of bovine and porcine "TRAP" and "LRAP" amelogenins. Biochem Biophys Res Commun, 197 (1), 248-55 (1993). (Pubitemid 23358904)
    • (1993) Biochemical and Biophysical Research Communications , vol.197 , Issue.1 , pp. 248-255
    • Fincham, A.G.1    Moradian-Oldak, J.2
  • 54
    • 0033593352 scopus 로고    scopus 로고
    • Tyrosyl motif in amelogenins binds N-acetyl-Dglucosamine
    • R. M. Ravindranath, J. Moradian-Oldak and A. G. Fincham: Tyrosyl motif in amelogenins binds N-acetyl-Dglucosamine. J Biol Chem, 274 (4), 2464-71 (1999).
    • (1999) J Biol Chem , vol.274 , Issue.4 , pp. 2464-2471
    • Ravindranath, R.M.1    Moradian-Oldak, J.2    Fincham, A.G.3
  • 55
    • 0034842815 scopus 로고    scopus 로고
    • Regulated gene expression dictates enamel structure and tooth function
    • DOI 10.1016/S0945-053X(01)00153-6, PII S0945053X01001536
    • M. L. Paine, S. N. White, W. Luo, H. Fong, M. Sarikaya and M. L. Snead: Regulated gene expression dictates enamel structure and tooth function. Matrix Biol., 20, 273-292 (2001). (Pubitemid 32846713)
    • (2001) Matrix Biology , vol.20 , Issue.5-6 , pp. 273-292
    • Paine, M.L.1    White, S.N.2    Luo, W.3    Fong, H.4    Sarikaya, M.5    Snead, M.L.6
  • 56
    • 0014515302 scopus 로고
    • The comparative biochemistry of the organic matrix of developing enamel-II. Ultracentrifugal and electrophoretic characterization of proteins soluble at neutral pH
    • E. P. Katz, J. Seyer, P. T. Levine and M. J. Glimcher: The comparative biochemistry of the organic matrix of developing enamel-II. Ultracentrifugal and electrophoretic characterization of proteins soluble at neutral pH. Arch Oral Biol, 14 (5), 533-9 (1969).
    • (1969) Arch Oral Biol , vol.14 , Issue.5 , pp. 533-539
    • Katz, E.P.1    Seyer, J.2    Levine, P.T.3    Glimcher, M.J.4
  • 57
    • 0014209820 scopus 로고
    • The Sephadex gel filtration characteristics of the neutral soluble proteins of embryonic bovine enamel
    • G. L. Mechanic, E. P. Katz and M. J. Glimcher: The Sephadex gel filtration characteristics of the neutral soluble proteins of embryonic bovine enamel. Biochim Biophys Acta, 133 (1), 97-113 (1967).
    • (1967) Biochim Biophys Acta , vol.133 , Issue.1 , pp. 97-113
    • Mechanic, G.L.1    Katz, E.P.2    Glimcher, M.J.3
  • 58
    • 64349115533 scopus 로고    scopus 로고
    • The tooth enamel protein, porcine amelogenin, is an intrinsically disordered protein with an extended molecular configuration in the monomeric form
    • K. Delak, C. Harcup, R. Lakshminarayanan, Z. Sun, Y. Fan, J. Moradian-Oldak and J. S. Evans: The tooth enamel protein, porcine amelogenin, is an intrinsically disordered protein with an extended molecular configuration in the monomeric form. Biochemistry, 48 (10), 2272-81 (2009).
    • (2009) Biochemistry , vol.48 , Issue.10 , pp. 2272-2281
    • Delak, K.1    Harcup, C.2    Lakshminarayanan, R.3    Sun, Z.4    Fan, Y.5    Moradian-Oldak, J.6    Evans, J.S.7
  • 59
    • 0013805367 scopus 로고
    • The molecular structure of the neutral-soluble proteins of embryonic bovine enamel in the solid state
    • L. C. Bonar, M. J. Glimcher and G. L. Mechanic: The molecular structure of the neutral-soluble proteins of embryonic bovine enamel in the solid state. J Ultrastruct Res, 13 (3), 308-17 (1965).
    • (1965) J Ultrastruct Res , vol.13 , Issue.3 , pp. 308-317
    • Bonar, L.C.1    Glimcher, M.J.2    Mechanic, G.L.3
  • 60
    • 0027403490 scopus 로고
    • Molecular conformation of porcine amelogenin in solution: Three folding units at the N-terminal, central, and C-terminal regions
    • Y. Goto, E. Kogure, T. Takagi, S. Aimoto and T. Aoba: Molecular conformation of porcine amelogenin in solution: three folding units at the N-terminal, central and C-terminal regions. J Biochem, 113 (113), 55-60 (1993). (Pubitemid 23068842)
    • (1993) Journal of Biochemistry , vol.113 , Issue.1 , pp. 55-60
    • Goto, Y.1    Kogure, E.2    Takagi, T.3    Aimoto, S.4    Aoba, T.5
  • 61
    • 0024500210 scopus 로고
    • 138, within a single polypeptide chain: Preliminary molecular mechanics and dynamics studies
    • DOI 10.1002/bip.360280130
    • V. Renugopalakrishnan, N. Pattabiraman, M. Prabhakaran, E. Strawich and M. J. Glimcher: Tooth enamel protein, amelogenin, has a probable beta-spiral internal channel, Gln112-Leu138, within a single polypeptide chain: preliminary molecular mechanics and dynamics studies. Biopolymers, 28 (1), 297-303 (1989). (Pubitemid 19054005)
    • (1989) Biopolymers , vol.28 , Issue.1 , pp. 297-303
    • Renugopalakrishnan, V.1    Pattabiraman, N.2    Prabhakaran, M.3    Strawich, E.4    Glimcher, M.J.5
  • 62
    • 0018442490 scopus 로고
    • Enamel matrix: Structural proteins
    • J. D. Termine, D. A. Torchia and K. M. Conn: Enamel matrix: structural proteins. J Dent Res, 58 (Spec Issue B), 773-81 (1979).
    • (1979) J Dent Res , vol.58 , Issue.SPEC. ISSUE B , pp. 773-781
    • Termine, J.D.1    Torchia, D.A.2    Conn, K.M.3
  • 64
    • 68049128255 scopus 로고    scopus 로고
    • Analysis of secondary structure and self-assembly of amelogenin by variable temperature circular dichroism and isothermal titration calorimetry
    • R. Lakshminarayanan, I. Yoon, B. G. Hegde, D. Fan, C. Du and J. Moradian-Oldak: Analysis of secondary structure and self-assembly of amelogenin by variable temperature circular dichroism and isothermal titration calorimetry. Proteins, 76 (3), 560-9 (2009).
    • (2009) Proteins , vol.76 , Issue.3 , pp. 560-569
    • Lakshminarayanan, R.1    Yoon, I.2    Hegde, B.G.3    Fan, D.4    Du, C.5    Moradian-Oldak, J.6
  • 66
    • 0034677659 scopus 로고    scopus 로고
    • Conformation of the RNA polymerase II C-terminal domain: Circular dichroism of long and short fragments
    • E. A. Bienkiewicz, A. Moon Woody and R. W. Woody: Conformation of the RNA polymerase II C-terminal domain: circular dichroism of long and short fragments. J Mol Biol, 297 (1), 119-33 (2000).
    • (2000) J Mol Biol , vol.297 , Issue.1 , pp. 119-133
    • Bienkiewicz, E.A.1    Woody, A.M.2    Woody, R.W.3
  • 67
    • 36549013310 scopus 로고    scopus 로고
    • The role of secondary structure in the entropically driven amelogenin self-assembly
    • DOI 10.1529/biophysj.107.113936
    • R. Lakshminarayanan, D. Fan, C. Du and J. Moradian-Oldak: The role of secondary structure in the entropically driven amelogenin self-assembly. Biophys J, 93 (10), 3664- 74 (2007). (Pubitemid 350190828)
    • (2007) Biophysical Journal , vol.93 , Issue.10 , pp. 3664-3674
    • Lakshminarayanan, R.1    Fan, D.2    Du, C.3    Moradian-Oldak, J.4
  • 71
    • 80054972812 scopus 로고    scopus 로고
    • In situ AFM study of amelogenin assembly and dis-assembly dynamics on charged surfaces provides insights on matrix protein self-assembly
    • Epub ahead of print
    • C.-L. Chen, K. M. Bromley, J. Moradian-Oldak and J. DeYoreo: In situ AFM Study of Amelogenin Assembly and Dis-assembly Dynamics on Charged Surfaces provides Insights on Matrix Protein Self-Assembly.J Am Chem Soc (2011) (Epub ahead of print).
    • (2011) J Am Chem Soc
    • Chen, C.-L.1    Bromley, K.M.2    Moradian-Oldak, J.3    Deyoreo, J.4
  • 72
    • 14644413519 scopus 로고    scopus 로고
    • Supramolecular assembly of amelogenin nanospheres into birefringent microribbons
    • DOI 10.1126/science.1105675
    • C. Du, G. Falini, S. Fermani, C. Abbott and J. Moradian-Oldak: Supramolecular assembly of amelogenin nanospheres into birefringent microribbons. Science, 307 (5714), 1450-4 (2005). (Pubitemid 40321938)
    • (2005) Science , vol.307 , Issue.5714 , pp. 1450-1454
    • Du, C.1    Falini, G.2    Fermani, S.3    Abbott, C.4    Moradian-Oldak, J.5
  • 73
    • 34548613499 scopus 로고    scopus 로고
    • PH triggered self-assembly of native and recombinant amelogenins under physiological pH and temperature in vitro
    • DOI 10.1016/j.jsb.2007.06.007, PII S1047847707001487
    • F. B. Wiedemann-Bidlack, E. Beniash, Y. Yamakoshi, J. P. Simmer and H. C. Margolis: pH triggered selfassembly of native and recombinant amelogenins under physiological pH and temperature in vitro. J Struct Biol, 160 (1), 57-69 (2007). (Pubitemid 47405235)
    • (2007) Journal of Structural Biology , vol.160 , Issue.1 , pp. 57-69
    • Wiedemann-Bidlack, F.B.1    Beniash, E.2    Yamakoshi, Y.3    Simmer, J.P.4    Margolis, H.C.5
  • 74
    • 79952486476 scopus 로고    scopus 로고
    • Self-aligning amelogenin nanoribbons in oilwater system
    • X. He, S. Wu, O. Martinez-Avila, Y. Cheng and S. Habelitz: Self-aligning amelogenin nanoribbons in oilwater system. J Struct Biol, 174 (1), 203-12 (2011).
    • (2011) J Struct Biol , vol.174 , Issue.1 , pp. 203-212
    • He, X.1    Wu, S.2    Martinez-Avila, O.3    Cheng, Y.4    Habelitz, S.5
  • 75
    • 0032448138 scopus 로고    scopus 로고
    • Does amelogenin nanosphere assembly proceed through intermediary-sized structures?
    • A. G. Fincham, W. Leung, J. Tan and J. Moradian-Oldak: Does amelogenin nanosphere assembly proceed through intermediary-sized structures? Connect Tissue Res, 38 (1-4), 237-40; discussion 241-6 (1998). (Pubitemid 29059948)
    • (1998) Connective Tissue Research , vol.38 , Issue.1-4 , pp. 237-240
    • Fincham, A.G.1    Leung, W.2    Tan, J.3    Moradian-Oldak, J.4
  • 76
    • 80051791489 scopus 로고    scopus 로고
    • Cryogenic transmission electron microscopy study of amelogenin self-assembly at different pH
    • P. A. Fang, H. C. Margolis, J. F. Conway, J. P. Simmer, G. H. Dickinson and E. Beniash: Cryogenic Transmission Electron Microscopy Study of Amelogenin Self-Assembly at Different pH. Cells Tissues Organs 194 (2-4), 166-170 (2011).
    • (2011) Cells Tissues Organs , vol.194 , Issue.2-4 , pp. 166-170
    • Fang, P.A.1    Margolis, H.C.2    Conway, J.F.3    Simmer, J.P.4    Dickinson, G.H.5    Beniash, E.6
  • 77
    • 0013815062 scopus 로고
    • Purification and properties of protein from embryonic bovine enamel
    • G. Nikiforuk and N. S. Simmons: Purification and properties of protein from embryonic bovine enamel. J Dent Res, 44 (6), Suppl:1119-22 (1965).
    • (1965) J Dent Res , vol.44 , Issue.6 SUPPL. , pp. 1119-1122
    • Nikiforuk, G.1    Simmons, N.S.2
  • 79
    • 34347215860 scopus 로고    scopus 로고
    • The emergence of "nanospheres" as basic structural components adopted by amelogenin
    • J. Moradian-Oldak: The emergence of "nanospheres" as basic structural components adopted by amelogenin. J Dent Res, 86 (6), 487-90 (2007).
    • (2007) J Dent Res , vol.86 , Issue.6 , pp. 487-490
    • Moradian-Oldak, J.1
  • 80
    • 0028519190 scopus 로고
    • Detection of monodisperse aggregates of a recombinant amelogenin by dynamic light scattering
    • DOI 10.1002/bip.360341006
    • J. Moradian-Oldak, J. P. Simmer, E. C. Lau, P. E. Sarte, H. C. Slavkin and A. G. Fincham: Detection of monodisperse aggregates of a recombinant amelogenin by dynamic light scattering. Biopolymers, 34 (10), 1339-47 (1994). (Pubitemid 24302943)
    • (1994) Biopolymers , vol.34 , Issue.10 , pp. 1339-1347
    • Moradian-Oldak, J.1    Simmer, J.P.2    Lau, E.C.3    Sarte, P.E.4    Slavkin, H.C.5    Fincham, A.G.6
  • 81
    • 0032457781 scopus 로고    scopus 로고
    • Identification of tuftelin- and amelogenin-interacting proteins using the yeast two-hybrid system
    • C. T. Paine, M. L. Paine and M. L. Snead: Identification of tuftelin- and amelogenin-interacting proteins using the yeast two-hybrid system. Connect Tissue Res, 38 (1-4), 257- 67;discussion 295-303 (1998). (Pubitemid 29059951)
    • (1998) Connective Tissue Research , vol.38 , Issue.1-4 , pp. 257-267
    • Paine, C.T.1    Paine, M.L.2    Snead, M.L.3
  • 82
    • 0033821661 scopus 로고    scopus 로고
    • Self-assembly properties of recombinant engineered amelogenin proteins analyzed by dynamic light scattering and atomic force microscopy
    • J. Moradian-Oldak, M. L. Paine, Y. P. Lei, A. G. Fincham and M. L. Snead: Self-assembly properties of recombinant engineered amelogenin proteins analyzed by dynamic light scattering and atomic force microscopy. J Struct Biol, 131 (1), 27-37 (2000).
    • (2000) J Struct Biol , vol.131 , Issue.1 , pp. 27-37
    • Moradian-Oldak, J.1    Paine, M.L.2    Lei, Y.P.3    Fincham, A.G.4    Snead, M.L.5
  • 83
    • 25144524137 scopus 로고    scopus 로고
    • The onset of amelogenin nanosphere aggregation studied by small-angle X-ray scattering and dynamic light scattering
    • DOI 10.1016/j.jsb.2005.06.007, PII S1047847705001310
    • B. Aichmayer, H. C. Margolis, R. Sigel, Y. Yamakoshi, J. P. Simmer and P. Fratzl: The onset of amelogenin nanosphere aggregation studied by small-angle X-ray scattering and dynamic light scattering. J Struct Biol, 151 (3), 239-49 (2005). (Pubitemid 41338731)
    • (2005) Journal of Structural Biology , vol.151 , Issue.3 , pp. 239-249
    • Aichmayer, B.1    Margolis, H.C.2    Sigel, R.3    Yamakoshi, Y.4    Simmer, J.P.5    Fratzl, P.6
  • 84
    • 59949100536 scopus 로고    scopus 로고
    • Changes in the quaternary structure of amelogenin when adsorbed onto surfaces
    • B. J. Tarasevich, S. Lea, W. Bernt, M. H. Engelhard and W. J. Shaw: Changes in the quaternary structure of amelogenin when adsorbed onto surfaces. Biopolymers, 91 (2), 103-7 (2009).
    • (2009) Biopolymers , vol.91 , Issue.2 , pp. 103-107
    • Tarasevich, B.J.1    Lea, S.2    Bernt, W.3    Engelhard, M.H.4    Shaw, W.J.5
  • 85
    • 12844282379 scopus 로고    scopus 로고
    • The effect of recombinant mouse amelogenins on the formation and organization of hydroxyapatite crystals in vitro
    • DOI 10.1016/j.jsb.2004.11.001, PII S1047847704002138
    • E. Beniash, J. P. Simmer and H. C. Margolis: The effect of recombinant mouse amelogenins on the formation and organization of hydroxyapatite crystals in vitro. J Struct Biol, 149 (2), 182-90 (2005). (Pubitemid 40170100)
    • (2005) Journal of Structural Biology , vol.149 , Issue.2 , pp. 182-190
    • Beniash, E.1    Simmer, J.P.2    Margolis, H.C.3
  • 86
    • 55649104516 scopus 로고    scopus 로고
    • The cooperative selfassembly of 25 and 23kDa amelogenins
    • X. He, W. Li and S. Habelitz: The cooperative selfassembly of 25 and 23kDa amelogenins. J Struct Biol, 164 (3), 314-21 (2008).
    • (2008) J Struct Biol , vol.164 , Issue.3 , pp. 314-321
    • He, X.1    Li, W.2    Habelitz, S.3
  • 88
    • 80053384079 scopus 로고    scopus 로고
    • Amelogenin "nanorods" formation during proteolysis by Mmp-20
    • Aug 5 (Epub ahead of print)
    • X. Yang, Z. Sun, R. Ma, D. Fan and J. Moradian-Oldak: Amelogenin "nanorods" formation during proteolysis by Mmp-20. J Struct Biol. (2011) Aug 5 (Epub ahead of print).
    • (2011) J Struct Biol
    • Yang, X.1    Sun, Z.2    Ma, R.3    Fan, D.4    Moradian-Oldak, J.5
  • 90
    • 33645957322 scopus 로고    scopus 로고
    • Amelogenin supra-molecular assembly in vitro compared with the architecture of the forming enamel matrix
    • J. Moradian-Oldak and M. Goldberg: Amelogenin supra-molecular assembly in vitro compared with the architecture of the forming enamel matrix. Cells Tissues Organs, 181 (3-4), 202-18 (2005).
    • (2005) Cells Tissues Organs , vol.181 , Issue.3-4 , pp. 202-218
    • Moradian-Oldak, J.1    Goldberg, M.2
  • 91
    • 0000086238 scopus 로고
    • The appearance of developing rat incisor enamel using freezefracture technique
    • C. Robinson, P. Fuchs and J. A. Weatherell: The appearance of developing rat incisor enamel using freezefracture technique. J. Crystal Growth, 53, 160-165 (1981).
    • (1981) J. Crystal Growth , vol.53 , pp. 160-165
    • Robinson, C.1    Fuchs, P.2    Weatherell, J.A.3
  • 92
    • 14644394287 scopus 로고    scopus 로고
    • A window on biomineralization
    • DOI 10.1126/science.1109440
    • A. Veis: A window on biomineralization. Science, 307, 1419-1420 (2005). (Pubitemid 40321927)
    • (2005) Science , vol.307 , Issue.5714 , pp. 1419-1420
    • Veis, A.1
  • 93
    • 21844445005 scopus 로고
    • III. The structure of the organic stroma of human enamel during amelogenesis
    • E. Ronnholm: III. The structure of the organic stroma of human enamel during amelogenesis. J Ultrastruct Res, 6, 368-89 (1962).
    • (1962) J Ultrastruct Res , vol.6 , pp. 368-389
    • Ronnholm, E.1
  • 94
    • 0036364509 scopus 로고    scopus 로고
    • Crystal ghosts and biological mineralization: Fancy spectres in an old castle, or neglected structures worthy of belief?
    • DOI 10.1007/s007740200037
    • E. Bonucci: Crystal ghosts and biological mineralization: fancy spectres in an old castle, or neglected structures worthy of belief? J Bone Miner Metab, 20 (5), 249-65 (2002). (Pubitemid 41184322)
    • (2002) Journal of Bone and Mineral Metabolism , vol.20 , Issue.5 , pp. 249-265
    • Bonucci, E.1
  • 95
    • 0000183090 scopus 로고
    • The extracellular nature of enamel in the rat
    • M. L. Watson: The extracellular nature of enamel in the rat. J Biophys Biochem Cytol, 7, 489-92 (1960).
    • (1960) J Biophys Biochem Cytol , vol.7 , pp. 489-492
    • Watson, M.L.1
  • 96
    • 78651157441 scopus 로고
    • The structure and organization of, and the relationship between the organic matrix and the inorganic crystals of embryonic bovine Enamel
    • D. F. Travis and M. J. Glimcher: The Structure And Organization Of, And The Relationship Between The Organic Matrix And The Inorganic Crystals Of Embryonic Bovine Enamel. J Cell Biol, 23, 447-97 (1964).
    • (1964) J Cell Biol , vol.23 , pp. 447-497
    • Travis, D.F.1    Glimcher, M.J.2
  • 97
    • 0016828309 scopus 로고
    • Structural subunit in prisms of immature rat enamel
    • F. C. Smales: Structural subunit in prisms of immature rat enamel. Nature, 258 (5537), 772-4 (1975).
    • (1975) Nature , vol.258 , Issue.5537 , pp. 772-774
    • Smales, F.C.1
  • 98
    • 0026054881 scopus 로고
    • Cyclical changes in pH in bovine developing enamel as sequential bands
    • S. Sasaki, T. Takagi and M. Suzuki: Cyclical changes in pH in bovine developing enamel as sequential bands. Arch Oral Biol, 36, 227-231 (1991).
    • (1991) Arch Oral Biol , vol.36 , pp. 227-231
    • Sasaki, S.1    Takagi, T.2    Suzuki, M.3
  • 99
    • 60649084924 scopus 로고    scopus 로고
    • In vitro study on the interaction between the 32 kDa enamelin and amelogenin
    • D. Fan, C. Du, Z. Sun, R. Lakshminarayanan and J. Moradian-Oldak: In vitro study on the interaction between the 32 kDa enamelin and amelogenin. J Struct Biol, 166 (1), 88-94 (2009).
    • (2009) J Struct Biol , vol.166 , Issue.1 , pp. 88-94
    • Fan, D.1    Du, C.2    Sun, Z.3    Lakshminarayanan, R.4    Moradian-Oldak, J.5
  • 102
    • 0042659481 scopus 로고    scopus 로고
    • Analysis of hydroxyapatite surface coverage by amelogenin nanospheres following the Langmuir model for protein adsorption
    • DOI 10.1007/s00223-002-1099-1
    • N. Bouropoulos and J. Moradian-Oldak: Analysis of hydroxyapatite surface coverage by amelogenin nanospheres following the Langmuir model for protein adsorption. Calcif Tissue Int, 72 (5), 599-603 (2003). (Pubitemid 36958561)
    • (2003) Calcified Tissue International , vol.72 , Issue.5 , pp. 599-603
    • Bouropoulos, N.1    Moradian-Oldak, J.2
  • 103
    • 0024723037 scopus 로고
    • Possible roles of partial sequences at N- and C-termini of amelogenin in protein-enamel mineral interaction
    • T. Aoba, E. C. Moreno, M. Kresak and T. Tanabe: Possible roles of partial sequences at N- and C-termini of amelogenin in protein-enamel mineral interaction. J Dent Res, 68, 1331-1336 (1989).
    • (1989) J Dent Res , vol.68 , pp. 1331-1336
    • Aoba, T.1    Moreno, E.C.2    Kresak, M.3    Tanabe, T.4
  • 104
    • 0032487612 scopus 로고    scopus 로고
    • Interaction of amelogenin with hydroxyapatite crystals: An adherence effect through amelogenin molecular selfassociation
    • J. Moradian-Oldak, J. Tan and A. G. Fincham: Interaction of amelogenin with hydroxyapatite crystals: an adherence effect through amelogenin molecular selfassociation. Biopolymers, 46 (4), 225-38 (1998).
    • (1998) Biopolymers , vol.46 , Issue.4 , pp. 225-238
    • Moradian-Oldak, J.1    Tan, J.2    Fincham, A.G.3
  • 105
    • 4043181150 scopus 로고    scopus 로고
    • Control of octacalcium phosphate and apatite crystal growth by amelogenin matrices
    • M. Iijima and J. Moradian-Oldak: Control of octacalcium phosphate and apatite crystal growth by amelogenin matrices. J. Materials Chemistry, 14 (14), 2189-2199 (2004).
    • (2004) J. Materials Chemistry , vol.14 , Issue.14 , pp. 2189-2199
    • Iijima, M.1    Moradian-Oldak, J.2
  • 106
    • 0034578996 scopus 로고    scopus 로고
    • Effects of amelogenin on the transforming surface microstructures of Bioglass in a calcifying solution
    • H. B. Wen, J. Moradian-Oldak, J. P. Zhong, D. C. Greenspan and A. G. Fincham: Effects of amelogenin on the transforming surface microstructures of Bioglass in a calcifying solution. J Biomed Mater Res, 52 (4), 762-73 (2000).
    • (2000) J Biomed Mater Res , vol.52 , Issue.4 , pp. 762-773
    • Wen, H.B.1    Moradian-Oldak, J.2    Zhong, J.P.3    Greenspan, D.C.4    Fincham, A.G.5
  • 108
    • 0035901789 scopus 로고    scopus 로고
    • Binding of matrix proteins to developing enamel crystals: An atomic force microscopy study
    • DOI 10.1021/la001281r
    • M. L. Wallwork, J. Kirkham, J. Zhang, A. Smith, S. Brookes, R. C. Shore, S. R. Wood, O. Ryu and C. Robinson: Binding of matrix proteins to developing enamel crystals: An atomic force microscope study. Langmuir, 17, 2508-2513. (2001). (Pubitemid 35330130)
    • (2001) Langmuir , vol.17 , Issue.8 , pp. 2508-2513
    • Wallwork, M.L.1    Kirkham, J.2    Zhang, J.3    Smith, D.A.4    Brookes, S.J.5    Shore, R.C.6    Wood, S.R.7    Ryu, O.8    Robinson, C.9
  • 109
    • 77649142033 scopus 로고    scopus 로고
    • How amelogenin orchestrates the organization of hierarchical elongated microstructures of apatite
    • X. Yang, L. Wang, Y. Qin, Z. Sun, Z. J. Henneman, J. Moradian-Oldak and G. H. Nancollas: How amelogenin orchestrates the organization of hierarchical elongated microstructures of apatite. J Phys Chem B, 114 (6), 2293- 300 (2010).
    • (2010) J Phys Chem B , vol.114 , Issue.6 , pp. 2293-2300
    • Yang, X.1    Wang, L.2    Qin, Y.3    Sun, Z.4    Henneman, Z.J.5    Moradian-Oldak, J.6    Nancollas, G.H.7
  • 111
    • 33646503201 scopus 로고    scopus 로고
    • Proteomic analysis of enamel matrix using a two-dimensional protein fractionation system
    • DOI 10.1111/j.1600-0722.2006.00279.x
    • Y. Yamakoshi, J. C. Hu, H. Zhang, T. Iwata, F. Yamakoshi and J. P. Simmer: Proteomic analysis of enamel matrix using a two-dimensional protein fractionation system. Eur J Oral Sci, 114 Suppl 1, 266-71; discussion 285-6, 382 (2006). (Pubitemid 43709447)
    • (2006) European Journal of Oral Sciences , vol.114 , Issue.SUPPL. 1 , pp. 266-271
    • Yamakoshi, Y.1    Hu, J.C.-C.2    Zhang, H.3    Iwata, T.4    Yamakoshi, F.5    Simmer, J.P.6
  • 112
    • 43049092941 scopus 로고    scopus 로고
    • Ameloblastin and amelogenin share a common secretory pathway and are co-secreted during enamel formation
    • S. F. Zalzal, C. E. Smith and A. Nanci: Ameloblastin and amelogenin share a common secretory pathway and are co-secreted during enamel formation. Matrix Biol, 27 (4), 352-9 (2008).
    • (2008) Matrix Biol , vol.27 , Issue.4 , pp. 352-359
    • Zalzal, S.F.1    Smith, C.E.2    Nanci, A.3
  • 115
    • 0034786105 scopus 로고    scopus 로고
    • Calcium binding of enamel proteins and their derivatives with emphasis on the calcium-binding domain of porcine sheathlin
    • DOI 10.1016/S0003-9969(01)00070-X, PII S000399690100070X
    • Y. Yamakoshi, T. Tanabe, S. Oida, C. C. Hu, J. P. Simmer and M. Fukae: Calcium binding of enamel proteins and their derivatives with emphasis on the calcium-binding domain of porcine sheathlin. Arch Oral Biol, 46 (11), 1005- 14 (2001). (Pubitemid 32970397)
    • (2001) Archives of Oral Biology , vol.46 , Issue.11 , pp. 1005-1014
    • Yamakoshi, Y.1    Tanabe, T.2    Oida, S.3    Hub, C.-C.4    Simmer, J.P.5    Fukae, M.6
  • 117
    • 40949121031 scopus 로고    scopus 로고
    • Bioinformatic analysis and molecular modelling of human ameloblastin suggest a two-domain intrinsically unstructured calcium-binding protein
    • J. Vymetal, I. Slaby, A. Spahr, J. Vondrasek and S. P. Lyngstadaas: Bioinformatic analysis and molecular modelling of human ameloblastin suggest a two-domain intrinsically unstructured calcium-binding protein. Eur J Oral Sci, 116 (2), 124-34 (2008).
    • (2008) Eur J Oral Sci , vol.116 , Issue.2 , pp. 124-134
    • Vymetal, J.1    Slaby, I.2    Spahr, A.3    Vondrasek, J.4    Lyngstadaas, S.P.5
  • 119
    • 23444432143 scopus 로고
    • Spatially regulated expression of three receptor tyrosine kinase genes during gastrulation in the zebrafish
    • Q. Xu, N. Holder, R. Patient and S. W. Wilson: Spatially regulated expression of three receptor tyrosine kinase genes during gastrulation in the zebrafish. Development, 120, 287-299 (1994). (Pubitemid 24042397)
    • (1994) Development , vol.120 , Issue.2 , pp. 287-299
    • Xu, O.1    Holder, N.2    Patient, R.3    Wilson, S.W.4
  • 120
    • 0025767907 scopus 로고
    • Immunochemical and immunohistochemical studies, using antisera against porcine 25kDa amelogenin, 89kDa enamelin and the 13- 17kDa nonamelogenins, on immature enamel of the pig and rat
    • T. Uchida, T. Tanabe, M. Fukae, M. Shimizu, M. Yamada, K. Miake and S. Kobayashi: Immunochemical and immunohistochemical studies, using antisera against porcine 25kDa amelogenin, 89kDa enamelin and the 13- 17kDa nonamelogenins, on immature enamel of the pig and rat. Histochemistry, 96, 129-138 (1991).
    • (1991) Histochemistry , vol.96 , pp. 129-138
    • Uchida, T.1    Tanabe, T.2    Fukae, M.3    Shimizu, M.4    Yamada, M.5    Miake, K.6    Kobayashi, S.7
  • 121
    • 0026951427 scopus 로고
    • Localization of glycosylated matrix proteins in secretory porcine enamel and their possible functional roles in enamel mineralization
    • H. Akita, M. Fukae, S. Shimoda and T. Aoba: Localization of glycosylated matrix proteins in secretory porcine enamel and their possible functional roles in enamel mineralization. Arch Oral Biol, 37 (11), 953-62 (1992).
    • (1992) Arch Oral Biol , vol.37 , Issue.11 , pp. 953-962
    • Akita, H.1    Fukae, M.2    Shimoda, S.3    Aoba, T.4
  • 123
    • 67649505431 scopus 로고    scopus 로고
    • A mouse model expressing a truncated form of ameloblastin exhibits dental and junctional epithelium defects
    • R. M. Wazen, P. Moffatt, S. F. Zalzal, Y. Yamada and A. Nanci: A mouse model expressing a truncated form of ameloblastin exhibits dental and junctional epithelium defects. Matrix Biol, 28 (5), 292-303 (2009).
    • (2009) Matrix Biol , vol.28 , Issue.5 , pp. 292-303
    • Wazen, R.M.1    Moffatt, P.2    Zalzal, S.F.3    Yamada, Y.4    Nanci, A.5
  • 124
    • 0030831971 scopus 로고    scopus 로고
    • Synthesis, secretion, degradation, and fate of ameloblastin during the matrix formation stage of the rat incisor as shown by immunocytochemistry and immunochemistry using region-specific antibodies
    • T. Uchida, C. Murakami, N. Dohi, K. Wakida, T. Satoda and O. Takahashi: Synthesis, secretion, degradation, and fate of ameloblastin during the matrix formation stage of the rat incisor as shown by immunocytochemistry and immunochemistry using region-specific antibodies. J Histochem Cytochem, 45 (10), 1329-40 (1997). (Pubitemid 27402794)
    • (1997) Journal of Histochemistry and Cytochemistry , vol.45 , Issue.10 , pp. 1329-1340
    • Uchida, T.1    Murakami, C.2    Dohi, N.3    Wakida, K.4    Satoda, T.5    Takahashi, O.6
  • 126
    • 0030187506 scopus 로고    scopus 로고
    • Enamel biology logodaedaly: Getting to the root of the problem, or "Who's on first
    • M. L. Snead: Enamel biology logodaedaly: Getting to the root of the problem, or "Who's on first...". J Bone Min. Res, 11, 899-904 (1996).
    • (1996) J Bone Min. Res , vol.11 , pp. 899-904
    • Snead, M.L.1
  • 127
    • 0035321491 scopus 로고    scopus 로고
    • A comparison of enamelin and amelogenin expression in developing mouse molars
    • J. C. Hu, X. Sun, C. Zhang and J. P. Simmer: A comparison of enamelin and amelogenin expression in developing mouse molars. Eur J Oral Sci, 109, 125-132 (2001). (Pubitemid 33774020)
    • (2001) European Journal of Oral Sciences , vol.109 , Issue.2 , pp. 125-132
    • Hu, J.C.-C.1    Sun, X.2    Zhang, C.3    Simmer, J.P.4
  • 129
    • 0034303215 scopus 로고    scopus 로고
    • Enamelin maps to human chromosome 4q21 within the autosomal dominant amelogenesis imperfecta locus
    • J. Dong, T. T. Gu, D. Simmons and M. MacDougall: Enamelin maps to human chromosome 4q21 within the autosomal dominant amelogenesis imperfecta locus. Eur J Oral Sci, 108 (5), 353-8 (2000).
    • (2000) Eur J Oral Sci , vol.108 , Issue.5 , pp. 353-358
    • Dong, J.1    Gu, T.T.2    Simmons, D.3    MacDougall, M.4
  • 130
    • 72449159548 scopus 로고    scopus 로고
    • Evolutionary analysis of mammalian enamelin, the largest enamel protein, supports a crucial role for the 32-kDa peptide and reveals selective adaptation in rodents and primates
    • N. Al-Hashimi, J. Y. Sire and S. Delgado: Evolutionary analysis of mammalian enamelin, the largest enamel protein, supports a crucial role for the 32-kDa peptide and reveals selective adaptation in rodents and primates. J Mol Evol, 69 (6), 635-56 (2009).
    • (2009) J Mol Evol , vol.69 , Issue.6 , pp. 635-656
    • Al-Hashimi, N.1    Sire, J.Y.2    Delgado, S.3
  • 132
    • 0032228004 scopus 로고    scopus 로고
    • Sites of asparagine-linked oligosaccharides in porcine 32 kDa enamelin
    • discussion 63-7
    • Y. Yamakoshi, F. H. Pinheiro, T. Tanabe, M. Fukae and M. Shimizu: Sites of asparagine-linked oligosaccharides in porcine 32 kDa enamelin. Connect Tissue Res, 39 (1-3), 39-46; discussion 63-7 (1998).
    • (1998) Connect Tissue Res , vol.39 , Issue.1-3 , pp. 39-46
    • Yamakoshi, Y.1    Pinheiro, F.H.2    Tanabe, T.3    Fukae, M.4    Shimizu, M.5
  • 133
    • 0642275691 scopus 로고    scopus 로고
    • Enamelin and autosomaldominant amelogenesis imperfecta
    • J. C. Hu and Y. Yamakoshi: Enamelin and autosomaldominant amelogenesis imperfecta. Crit Rev Oral Biol Med, 14 (6), 387-98 (2003).
    • (2003) Crit Rev Oral Biol Med , vol.14 , Issue.6 , pp. 387-398
    • Hu, J.C.1    Yamakoshi, Y.2
  • 135
    • 2342631323 scopus 로고    scopus 로고
    • Induction of apatite by the cooperative effect of amelogenin and the 32-kDa enamelin
    • N. Bouropoulos and J. Moradian-Oldak: Induction of apatite by the cooperative effect of amelogenin and the 32- kDa enamelin. J Dent Res, 83 (4), 278-82 (2004). (Pubitemid 41713761)
    • (2004) Journal of Dental Research , vol.83 , Issue.4 , pp. 278-282
    • Bouropoulos, N.1    Moradian-Oldak, J.2
  • 136
    • 80051794842 scopus 로고    scopus 로고
    • The cooperation of enamelin and amelogenin in controlling octacalcium phosphate crystal morphology
    • D. Fan, M. Iijima, K. M. Bromley, X. Yang, S. Mathew and J. Moradian-Oldak: The Cooperation of Enamelin and Amelogenin in Controlling Octacalcium Phosphate Crystal Morphology. Cells Tissues Organs 194 (2-4):194-8 (2011).
    • (2011) Cells Tissues Organs , vol.194 , Issue.2-4 , pp. 194-198
    • Fan, D.1    Iijima, M.2    Bromley, K.M.3    Yang, X.4    Mathew, S.5    Moradian-Oldak, J.6
  • 137
    • 78149318038 scopus 로고    scopus 로고
    • Tooth enamel proteins enamelin and amelogenin cooperate to regulate the growth morphology of octacalcium phosphate crystals
    • M. Iijima, D. Fan, K. M. Bromley, Z. Sun and J. Moradian-Oldak: Tooth enamel proteins enamelin and amelogenin cooperate to regulate the growth morphology of octacalcium phosphate crystals. Cryst Growth Des, 10 (11), 4815-4822 (2010).
    • (2010) Cryst Growth des , vol.10 , Issue.11 , pp. 4815-4822
    • Iijima, M.1    Fan, D.2    Bromley, K.M.3    Sun, Z.4    Moradian-Oldak, J.5
  • 138
    • 2942666256 scopus 로고    scopus 로고
    • Interactions of amelogenins with octacalcium phosphate crystal faces are dose dependent
    • DOI 10.1007/s00223-002-0011-3
    • M. Iijima and J. Moradian-Oldak: Interactions of amelogenins with octacalcium phosphate crystal faces are dose dependent. Calcif Tissue Int, 74 (6), 522-31 (2004). (Pubitemid 38780288)
    • (2004) Calcified Tissue International , vol.74 , Issue.6 , pp. 522-531
    • Iijima, M.1    Moradian-Oldak, J.2
  • 140
    • 33749385201 scopus 로고    scopus 로고
    • Cloning of rat amelotin and localization of the protein to the basal lamina of maturation stage ameloblasts and junctional epithelium
    • DOI 10.1042/BJ20060662
    • P. Moffatt, C. E. Smith, R. St-Arnaud, D. Simmons, J. T. Wright and A. Nanci: Cloning of rat amelotin and localization of the protein to the basal lamina of maturation stage ameloblasts and junctional epithelium. Biochem J, 399 (1), 37-46 (2006). (Pubitemid 44505405)
    • (2006) Biochemical Journal , vol.399 , Issue.1 , pp. 37-46
    • Moffatt, P.1    Smith, C.E.2    St.-Arnaud, R.3    Simmons, D.4    Wright, J.T.5    Nanci, A.6
  • 144
    • 0030473811 scopus 로고    scopus 로고
    • Molecular cloning and mRNA tissue distribution of a novel matrix metalloproteinase isolated from porcine enamel organ
    • DOI 10.1016/S0378-1119(96)00525-2, PII S0378111996005252
    • J. D. Bartlett, J. P. Simmer, J. Xue, H. C. Margolis and E. C. Moreno: Molecular cloning and mRNA tissue distribution of a novel matrix metalloproteinase isolated from porcine enamel organ. Gene, 183, 123-128 (1996). (Pubitemid 27007500)
    • (1996) Gene , vol.183 , Issue.1-2 , pp. 123-128
    • Bartlett, J.D.1    Simmer, J.P.2    Xue, J.3    Margolis, H.C.4    Moreno, E.C.5
  • 145
    • 0032228005 scopus 로고    scopus 로고
    • Degradation of enamel matrix proteins in porcine secretory enamel
    • discussion 141-9
    • M. Fukae and T. Tanabe: Degradation of enamel matrix proteins in porcine secretory enamel. Connect Tissue Res, 39 (1-3), 123-9; discussion 141-9 (1998).
    • (1998) Connect Tissue Res , vol.39 , Issue.1-3 , pp. 123-129
    • Fukae, M.1    Tanabe, T.2
  • 147
    • 16544373418 scopus 로고    scopus 로고
    • Decreased mineral content in MMP-20 null mouse enamel is prominent during the maturation stage
    • J. D. Bartlett, E. Beniash, D. H. Lee and C. E. Smith: Decreased mineral content in MMP-20 null mouse enamel is prominent during the maturation stage. J Dent Res, 83 (12), 909-13 (2004). (Pubitemid 41713826)
    • (2004) Journal of Dental Research , vol.83 , Issue.12 , pp. 909-913
    • Bartlett, J.D.1    Beniash, E.2    Lee, D.H.3    Smith, C.E.4
  • 148
    • 79955962728 scopus 로고    scopus 로고
    • Effect of kallikrein 4 loss on enamel mineralization: Comparison with mice lacking matrix metalloproteinase 20
    • C. E. Smith, A. S. Richardson, Y. Hu, J. D. Bartlett, J. C. Hu and J. P. Simmer: Effect of Kallikrein 4 Loss on Enamel Mineralization: Comparison With Mice Lacking Matrix Metalloproteinase 20. J Biol Chem, 286 (20), 18149-60 (2011).
    • (2011) J Biol Chem , vol.286 , Issue.20 , pp. 18149-18160
    • Smith, C.E.1    Richardson, A.S.2    Hu, Y.3    Bartlett, J.D.4    Hu, J.C.5    Simmer, J.P.6
  • 149
    • 0033278065 scopus 로고    scopus 로고
    • Characterization of recombinant pig enamelysin activity and cleavage of recombinant pig and mouse amelogenins
    • O. H. Ryu, A. G. Fincham, C. C. Hu, C. Zhang, Q. Qian, J. D. Bartlett and J. P. Simmer: Characterization of recombinant pig enamelysin activity and cleavage of recombinant pig and mouse amelogenins. J Dent Res, 78, 743-750 (1999). (Pubitemid 32501273)
    • (1999) Journal of Dental Research , vol.78 , Issue.3 , pp. 743-750
    • Ryu, O.H.1    Fincham, A.G.2    Hu, C.-C.3    Zhang, C.4    Qian, Q.5    Bartlett, J.D.6    Simmer, J.P.7
  • 150
    • 58149379900 scopus 로고    scopus 로고
    • Enamel proteases reduce amelogenin-apatite binding
    • Z. Sun, D. Fan, Y. Fan, C. Du and J. Moradian-Oldak: Enamel proteases reduce amelogenin-apatite binding. J Dent Res, 87 (12), 1133-7 (2008).
    • (2008) J Dent Res , vol.87 , Issue.12 , pp. 1133-1137
    • Sun, Z.1    Fan, D.2    Fan, Y.3    Du, C.4    Moradian-Oldak, J.5
  • 152
    • 58049214871 scopus 로고    scopus 로고
    • Enzymatic processing of amelogenin during continuous crystallization of apatite
    • V. Uskokovic, M. K. Kim, W. Li and S. Habelitz: Enzymatic processing of amelogenin during continuous crystallization of apatite. J Mate Res, 23 (12), 3184-3195 (2008).
    • (2008) J Mate Res , vol.23 , Issue.12 , pp. 3184-3195
    • Uskokovic, V.1    Kim, M.K.2    Li, W.3    Habelitz, S.4
  • 154
    • 0038655332 scopus 로고    scopus 로고
    • Porcine kallikrein-4 activation, glycosylation, activity, and expression in prokaryotic and eukaryotic hosts
    • O. Ryu, J. C. Hu, Y. Yamakoshi, J. L. Villemain, X. Cao, C. Zhang, J. D. Bartlett and J. P. Simmer: Porcine kallikrein-4 activation, glycosylation, activity, and expression in prokaryotic and eukaryotic hosts. Eur J Oral Sci, 110 (5), 358-65 (2002).
    • (2002) Eur J Oral Sci , vol.110 , Issue.5 , pp. 358-365
    • Ryu, O.1    Hu, J.C.2    Yamakoshi, Y.3    Villemain, J.L.4    Cao, X.5    Zhang, C.6    Bartlett, J.D.7    Simmer, J.P.8
  • 155
    • 33646520806 scopus 로고    scopus 로고
    • How do enamelysin and kallikrein 4 process the 32-kDa enamelin?
    • DOI 10.1111/j.1600-0722.2006.00281.x
    • Y. Yamakoshi, J. C. Hu, M. Fukae, F. Yamakoshi and J. P. Simmer: How do enamelysin and kallikrein 4 process the 32-kDa enamelin? Eur J Oral Sci, 114 Suppl 1, 45-51; discussion 93-5, 379-80 (2006). (Pubitemid 43709414)
    • (2006) European Journal of Oral Sciences , vol.114 , Issue.SUPPL. 1 , pp. 45-51
    • Yamakoshi, Y.1    Hu, J.C.-C.2    Fukae, M.3    Yamakoshi, F.4    Simmer, J.P.5
  • 157
    • 67650529834 scopus 로고    scopus 로고
    • Hypomaturation enamel defects in Klk4 knockout/LacZ knockin mice
    • J. P. Simmer, Y. Hu, R. Lertlam, Y. Yamakoshi and J. C. Hu: Hypomaturation enamel defects in Klk4 knockout/LacZ knockin mice. J Biol Chem, 284 (28), 19110-21 (2009).
    • (2009) J Biol Chem , vol.284 , Issue.28 , pp. 19110-19121
    • Simmer, J.P.1    Hu, Y.2    Lertlam, R.3    Yamakoshi, Y.4    Hu, J.C.5
  • 158
    • 57449102191 scopus 로고    scopus 로고
    • Lysosomal protease expression in mature enamel
    • C. E. Tye, R. L. Lorenz and J. D. Bartlett: Lysosomal protease expression in mature enamel. Cells Tissues Organs, 189 (1-4), 111-4 (2009).
    • (2009) Cells Tissues Organs , vol.189 , Issue.1-4 , pp. 111-114
    • Tye, C.E.1    Lorenz, R.L.2    Bartlett, J.D.3
  • 159
    • 0346390810 scopus 로고
    • PH gradients in the developing teeth of young mice from autoradiography of (14C)DMO
    • G. E. Lyman and W. J. Waddell: pH gradients in the developing teeth of young mice from autoradiography of (14C)DMO. Am J Physiol, 232 (4), F364-7 (1977).
    • (1977) Am J Physiol , vol.232 , Issue.4
    • Lyman, G.E.1    Waddell, W.J.2
  • 160
    • 34250225724 scopus 로고
    • 45Ca incorporation with maturation ameloblast morphology in the rat incisor
    • Y. Takano, M. A. Crenshaw and E. J. Reith: Correlation of 45Ca incorporation with maturation ameloblast morphology in the rat incisor. Calcif Tissue Int, 34, 211-213 (1982). (Pubitemid 12128650)
    • (1982) Calcified Tissue International , vol.34 , Issue.2 , pp. 211-213
    • Takano, Y.1    Crenshaw, M.A.2    Reith, E.J.3
  • 161
    • 0030275714 scopus 로고    scopus 로고
    • Developmental changes in the pH of enamel fluid and its effects on matrix-resident proteinases
    • C. E. Smith, M. Issid, H. C. Margolis and E. C. Moreno: Developmental changes in the pH of enamel fluid and its effects on matrix-resident
    • (1996) Adv Dent Res , vol.10 , Issue.2 , pp. 159-169
    • Smith, C.E.1    Issid, M.2    Margolis, H.C.3    Moreno, E.C.4
  • 162
    • 0028961292 scopus 로고
    • Overview of morphological changes in enamel organ cells associated with major events in amelogenesis
    • C. E. Smith and A. Nanci: Overview of morphological changes in enamel organ cells associated with major events in amelogenesis. Int J Dev Biol, 39, 153-161 (1995).
    • (1995) Int J Dev Biol , vol.39 , pp. 153-161
    • Smith, C.E.1    Nanci, A.2
  • 163
    • 0023556160 scopus 로고
    • Cyclic induction and rapid movement of sequential waves of new smooth-ended ameloblast modulation bands in rat incisors as visualized by polychrome fluorescent labeling and GBHA-staining of maturing enamel
    • C. E. Smith, M. D. McKee and A. Nanci: Cyclic induction and rapid movement of sequential waves of new smooth-ended ameloblast modulation bands in rat incisors as visualized by polychrome fluorescent labeling and GBHA-staining of maturing enamel. Adv Dent Res, 1 (2), 162-75 (1987).
    • (1987) Adv Dent Res , vol.1 , Issue.2 , pp. 162-175
    • Smith, C.E.1    McKee, M.D.2    Nanci, A.3
  • 164
    • 0023634203 scopus 로고
    • The enamel fluid in the early secretory stage of porcine amelogenesis: Chemical composition and saturation with respect to enamel mineral
    • T. Aoba and E. C. Moreno: The enamel fluid in the early secretory stage of porcine amelogenesis: chemical composition and saturation with respect to enamel mineral. Calcif Tissue Int, 41 (2), 86-94 (1987).
    • (1987) Calcif Tissue Int , vol.41 , Issue.2 , pp. 86-94
    • Aoba, T.1    Moreno, E.C.2
  • 165
    • 0029977004 scopus 로고    scopus 로고
    • Immunohistochemical localization of carbonic anhydrase isozyme II in rat incisor epithelial cells at various stages of amelogenesis
    • DOI 10.1007/s004410050639
    • S. Toyosawa, Y. Ogawa, T. Inagaki and N. Ijuhin: Immunohistochemical localization of carbonic anhydrase isozyme II in rat incisor epithelial cells at various stages of amelogenesis. Cell Tissue Res, 285 (2), 217-25 (1996). (Pubitemid 26248394)
    • (1996) Cell and Tissue Research , vol.285 , Issue.2 , pp. 217-225
    • Toyosawa, S.1    Ogawa, Y.2    Inagaki, T.3    Ijuhin, N.4
  • 166
    • 33646518089 scopus 로고    scopus 로고
    • Evidence by signal peptide trap technology for the expression of carbonic anhydrase 6 in rat incisor enamel organs
    • DOI 10.1111/j.1600-0722.2006.00273.x
    • C. E. Smith, A. Nanci and P. Moffatt: Evidence by signal peptide trap technology for the expression of carbonic anhydrase 6 in rat incisor enamel organs. Eur J Oral Sci, 114 Suppl 1, 147-53; discussion 164-5, 380-1 (2006). (Pubitemid 43709428)
    • (2006) European Journal of Oral Sciences , vol.114 , Issue.SUPPL. 1 , pp. 147-153
    • Smith, C.E.1    Nanci, A.2    Moffatt, P.3
  • 168
    • 0020407377 scopus 로고
    • Mechanisms by which the enamel organ controls calcium entry into developing enamel
    • Spec No
    • M. A. Crenshaw and Y. Takano: Mechanisms by which the enamel organ controls calcium entry into developing enamel. J Dent Res, Spec No, 1574-9 (1982).
    • (1982) J Dent Res , pp. 1574-1579
    • Crenshaw, M.A.1    Takano, Y.2
  • 169
    • 0023557205 scopus 로고
    • Na-K-ATPase in the enamel organ: Localization and possible roles in enamel formation
    • P. R. Garant, T. Sasaki and P. E. Colflesh: Na-K-ATPase in the enamel organ: localization and possible roles in enamel formation. Adv Dent Res, 1 (2), 267-75 (1987).
    • (1987) Adv Dent Res , vol.1 , Issue.2 , pp. 267-275
    • Garant, P.R.1    Sasaki, T.2    Colflesh, P.E.3
  • 170
    • 0030119870 scopus 로고    scopus 로고
    • Prevalence of dental erosion and the implications for oral health
    • J. H. Nunn: Prevalence of dental erosion and the implications for oral health. Eur J Oral Sci, 104 (2), 156-61 (1996).
    • (1996) Eur J Oral Sci , vol.104 , Issue.2 , pp. 156-161
    • Nunn, J.H.1
  • 171
    • 0036009850 scopus 로고    scopus 로고
    • A nomenclature for X-linked amelogenesis imperfecta
    • DOI 10.1016/S0003-9969(02)00005-5, PII S0003996902000055
    • P. S. Hart, T. C. Hart, J. P. Simmer and J. T. Wright: A nomenclature for X-linked amelogenesis imperfecta. Arch Oral Biol., 47, 255-260 (2002). (Pubitemid 34288876)
    • (2002) Archives of Oral Biology , vol.47 , Issue.4 , pp. 255-260
    • Hart, P.S.1    Hart, T.C.2    Simmer, J.P.3    Wright, J.T.4
  • 174
    • 0031568256 scopus 로고    scopus 로고
    • Mapping of the locus for autosomal dominant amelogenesis imperfecta (AIH2) to a 4-Mb YAC contig on chromosome 4q11-q21
    • DOI 10.1006/geno.1996.4485
    • C. Karrman, B. Backman, M. Dixon, G. Holmgren and K. Forsman: Mapping of the locus for autosomal dominant amelogenesis imperfecta (AIH2) to a 4-Mb YAC contig on chromosome 4q11-q21. Genomics, 39, 164-170 (1997). (Pubitemid 27069214)
    • (1997) Genomics , vol.39 , Issue.2 , pp. 164-170
    • Karrman, C.1    Backman, B.2    Dixon, M.3    Holmgren, G.4    Forsman, K.5
  • 176
    • 84860444868 scopus 로고    scopus 로고
    • Consequences of amelogenin mutations: Implications in Amelogenesis Imperfecta
    • Ed M. Goldberg, Bentham Books Ltd, Dubai
    • J. T. Wright: Consequences of amelogenin mutations: Implications in Amelogenesis Imperfecta. In: Amelogenins; Multifaceted proteins for dental and bone formation and repair. Ed M. Goldberg. Bentham Books Ltd, Dubai (2010).
    • (2010) Amelogenins; Multifaceted Proteins for Dental and Bone Formation and Repair
    • Wright, J.T.1
  • 177
    • 78650412788 scopus 로고    scopus 로고
    • Perturbed amelogenin secondary structure leads to uncontrolled aggregation in amelogenesis imperfecta mutant proteins
    • R. Lakshminarayanan, K. M. Bromley, Y. P. Lei, M. L. Snead and J. Moradian-Oldak: Perturbed amelogenin secondary structure leads to uncontrolled aggregation in amelogenesis imperfecta mutant proteins. J Biol Chem, 285 (52), 40593-603 (2010).
    • (2010) J Biol Chem , vol.285 , Issue.52 , pp. 40593-40603
    • Lakshminarayanan, R.1    Bromley, K.M.2    Lei, Y.P.3    Snead, M.L.4    Moradian-Oldak, J.5
  • 178
    • 80051800959 scopus 로고    scopus 로고
    • Folding, assembly, and aggregation of recombinant murine amelogenins with T21I and P41T point mutations
    • K. M. Bromley, R. Lakshminarayanan, Y. P. Lei, M. L. Snead and J. Moradian-Oldak: Folding, Assembly, and Aggregation of Recombinant Murine Amelogenins with T21I and P41T Point Mutations. Cells Tissues Organs, 194 (2-4), 284-90 (2011).
    • (2011) Cells Tissues Organs , vol.194 , Issue.2-4 , pp. 284-290
    • Bromley, K.M.1    Lakshminarayanan, R.2    Lei, Y.P.3    Snead, M.L.4    Moradian-Oldak, J.5
  • 179
    • 0035133863 scopus 로고    scopus 로고
    • Reduced hydrolysis of amelogenin may result in X-linked amelogenesis imperfecta
    • DOI 10.1016/S0945-053X(00)00121-9, PII S0945053X00001219
    • W. Li, C. W. Gibson, D. W. Abrams, D. W. Andrews and P. K. DenBesten: Reduced hydrolysis of amelogenin may result in X-linked amelogenesis imperfecta. Matrix Biology, 19, 755-760 (2001). (Pubitemid 32162030)
    • (2001) Matrix Biology , vol.19 , Issue.8 , pp. 755-760
    • Li, W.1    Gibson, C.W.2    Abrams, W.R.3    Andrews, D.W.4    DenBesten, P.K.5
  • 180
    • 0031106113 scopus 로고    scopus 로고
    • An amelogenin gene defect associated with human X-linked amelogenesis imperfecta
    • DOI 10.1016/S0003-9969(96)00099-4, PII S0003996996000994
    • P. M. Collier, J. J. Sauk, J. Rosenbloom, Z. A. Yuan and C. W. Gibson: An amelogenin gene defect associated with human x-linked amelogenesis imperfecta. Archs Oral Biol., 42 (3), 235-242 (1997). (Pubitemid 27218201)
    • (1997) Archives of Oral Biology , vol.42 , Issue.3 , pp. 235-242
    • Collier, P.M.1    Sauk, J.J.2    Rosenbloom, J.3    Yuan, Z.A.4    Gibson, C.W.5
  • 182
    • 0034857932 scopus 로고    scopus 로고
    • Amelogenins: Assembly, processing and control of crystal morphology
    • DOI 10.1016/S0945-053X(01)00154-8, PII S0945053X01001548
    • J. Moradian-Oldak: Amelogenins: assembly, processing and control of crystal morphology. Matrix Biol, 20 (5-6), 293-305 (2001). (Pubitemid 32846714)
    • (2001) Matrix Biology , vol.20 , Issue.5-6 , pp. 293-305
    • Moradian-Oldak, J.1
  • 184
    • 0035422249 scopus 로고    scopus 로고
    • Mutation of the gene encoding the enamel-specific protein, enamelin, causes autosomal-dominant amelogenesis imperfecta
    • M. H. Rajpar, K. Harley, C. Laing, R. M. Davies and M. J. Dixon: Mutation of the gene encoding the enamelspecific protein, enamelin, causes autosomal-dominant amelogenesis imperfecta. Hum Mol Genet, 10, 1673-1677 (2001). (Pubitemid 32776297)
    • (2001) Human Molecular Genetics , vol.10 , Issue.16 , pp. 1673-1677
    • Rajpar, M.H.1    Harley, K.2    Laing, C.3    Davies, R.M.4    Dixon, M.J.5
  • 185
    • 0036827621 scopus 로고    scopus 로고
    • Autosomal-dominant hypoplastic form of amelogenesis imperfecta caused by an enamelin gene mutation at the exon-intron boundary
    • M. Kida, T. Ariga, T. Shirakawa, H. Oguchi and Y. Sakiyama: Autosomal-dominant hypoplastic form of amelogenesis imperfecta caused by an enamelin gene mutation at the exon-intron boundary. J Dent Res, 81 (11), 738-42 (2002).
    • (2002) J Dent Res , vol.81 , Issue.11 , pp. 738-742
    • Kida, M.1    Ariga, T.2    Shirakawa, T.3    Oguchi, H.4    Sakiyama, Y.5
  • 186
    • 0036566265 scopus 로고    scopus 로고
    • A nonsense mutation in the enamelin gene causes local hypoplastic autosomal dominant amelogenesis imperfecta (AIH2)
    • C. K. Mardh, B. Backman, G. Holmgren, J. C. Hu, J. P. Simmer and K. Forsman-Semb: A nonsense mutation in the enamelin gene causes local hypoplastic autosomal dominant amelogenesis imperfecta (AIH2). Hum Mol Genet, 11, 1069-1074 (2002). (Pubitemid 34521088)
    • (2002) Human Molecular Genetics , vol.11 , Issue.9 , pp. 1069-1074
    • Mardh, C.K.1    Backman, B.2    Holmgren, G.3    Hu, J.C.-C.4    Simmer, J.P.5    Forsman-Semb, K.6
  • 188
    • 0141497179 scopus 로고    scopus 로고
    • Exclusion of candidate genes in two families with autosomal dominant hypocalcified amelogenesis imperfecta
    • DOI 10.1034/j.1600-0722.2003.00046.x
    • P. S. Hart, J. T. Wright, M. Savage, G. Kang, J. T. Bensen, M. C. Gorry and T. C. Hart: Exclusion of candidate genes in two families with autosomal dominant hypocalcified amelogenesis imperfecta. Eur J Oral Sci, 111 (4), 326-31 (2003). (Pubitemid 37465501)
    • (2003) European Journal of Oral Sciences , vol.111 , Issue.4 , pp. 326-331
    • Hart, P.S.1    Wright, J.T.2    Savage, M.3    Kang, G.4    Bensen, J.T.5    Gorry, M.C.6    Hart, T.C.7
  • 189
    • 33947158110 scopus 로고    scopus 로고
    • Identification of a novel mutation in the enamalin gene in a family with autosomal-dominant amelogenesis imperfecta
    • DOI 10.1016/j.archoralbio.2006.09.014, PII S0003996906002597
    • S. J. Gutierrez, M. Chaves, D. M. Torres and I. Briceno: Identification of a novel mutation in the enamalin gene in a family with autosomal-dominant amelogenesis imperfecta. Arch Oral Biol, 52 (5), 503-6 (2007). (Pubitemid 46399641)
    • (2007) Archives of Oral Biology , vol.52 , Issue.5 , pp. 503-506
    • Gutierrez, S.J.1    Chaves, M.2    Torres, D.M.3    Briceno, I.4
  • 191
    • 33845277788 scopus 로고    scopus 로고
    • The molecular etiologies and associated phenotypes of amelogenesis imperfecta
    • DOI 10.1002/ajmg.a.31358
    • J. T. Wright: The molecular etiologies and associated phenotypes of amelogenesis imperfecta. Am J Med Genet A, 140 (23), 2547-55 (2006). (Pubitemid 44865082)
    • (2006) American Journal of Medical Genetics, Part A , vol.140 , Issue.23 , pp. 2547-2555
    • Wright, J.T.1
  • 194
    • 67649888572 scopus 로고    scopus 로고
    • Exclusion of candidate genes in seven Turkish families with autosomal recessive amelogenesis imperfecta
    • S. Becerik, D. Cogulu, G. Emingil, T. Han, P. S. Hart and T. C. Hart: Exclusion of candidate genes in seven Turkish families with autosomal recessive amelogenesis imperfecta. Am J Med Genet A, 149A (7), 1392-8 (2009).
    • (2009) Am J Med Genet A , vol.149 A , Issue.7 , pp. 1392-1398
    • Becerik, S.1    Cogulu, D.2    Emingil, G.3    Han, T.4    Hart, P.S.5    Hart, T.C.6
  • 196
    • 77649168069 scopus 로고    scopus 로고
    • The regeneration of tooth enamel
    • J. Moradian-Oldak: The regeneration of tooth enamel. Dimens Dent Hyg, 7 (8), 12-15 (2009).
    • (2009) Dimens Dent Hyg , vol.7 , Issue.8 , pp. 12-15
    • Moradian-Oldak, J.1
  • 197
    • 33847151614 scopus 로고    scopus 로고
    • Self-organization of hydroxyapatite nanorods through oriented attachment
    • DOI 10.1016/j.biomaterials.2007.01.033, PII S0142961207000920
    • J. D. Chen, Y. J. Wang, K. Wei, S. H. Zhang and X. T. Shi: Self-organization of hydroxyapatite nanorods through oriented attachment. Biomaterials, 28 (14), 2275-80 (2007). (Pubitemid 46282936)
    • (2007) Biomaterials , vol.28 , Issue.14 , pp. 2275-2280
    • Chen, J.D.1    Wang, Y.J.2    Wei, K.3    Zhang, S.H.4    Shi, X.T.5
  • 198
    • 68249140288 scopus 로고    scopus 로고
    • Kinetic model for hydroxyapatite precipitation on human enamel surface by electrolytic deposition
    • C. Lei, Y. Liao and Z. Feng: Kinetic model for hydroxyapatite precipitation on human enamel surface by electrolytic deposition. Biomed Mater, 4 (3), 035010 (2009).
    • (2009) Biomed Mater , vol.4 , Issue.3 , pp. 035010
    • Lei, C.1    Liao, Y.2    Feng, Z.3
  • 199
    • 66349106840 scopus 로고    scopus 로고
    • Direct growth of human enamel-like calcium phosphate microstructures on human tooth
    • X. Wang, C. Xia, Z. Zhang, X. Deng, S. Wei, G. Zheng and H. Chen: Direct growth of human enamel-like calcium phosphate microstructures on human tooth. J Nanosci Nanotechnol, 9 (2), 1361-4 (2009).
    • (2009) J Nanosci Nanotechnol , vol.9 , Issue.2 , pp. 1361-1364
    • Wang, X.1    Xia, C.2    Zhang, Z.3    Deng, X.4    Wei, S.5    Zheng, G.6    Chen, H.7
  • 200
    • 70349664209 scopus 로고    scopus 로고
    • Chemical regeneration of human tooth enamel under nearphysiological conditions
    • Y. Yin, S. Yun, J. Fang and H. Chen: Chemical regeneration of human tooth enamel under nearphysiological conditions. Chem Commun (Camb) (39), 5892-4 (2009).
    • (2009) Chem Commun (Camb) , vol.39 , pp. 5892-5894
    • Yin, Y.1    Yun, S.2    Fang, J.3    Chen, H.4
  • 201
    • 67349250834 scopus 로고    scopus 로고
    • Preparation of nanometer-scale rod array of hydroxyapatite crystal
    • S. Hayakawa, Y. Li, K. Tsuru, A. Osaka, E. Fujii and K. Kawabata: Preparation of nanometer-scale rod array of hydroxyapatite crystal. Acta Biomater, 5 (6), 2152-60 (2009).
    • (2009) Acta Biomater , vol.5 , Issue.6 , pp. 2152-2160
    • Hayakawa, S.1    Li, Y.2    Tsuru, K.3    Osaka, A.4    Fujii, E.5    Kawabata, K.6
  • 203
    • 0035154839 scopus 로고    scopus 로고
    • Effects of bovine amelogenins on the crystal morphology of octacalcium phosphate in a model system of tooth enamel formation
    • DOI 10.1016/S0022-0248(00)00984-2
    • M. Iijima, Y. Moriwaki, T. Takagi and J. Moradian-Oldak: Effects of bovine amelogenins on the crystal morphology of octacalcium phosphate in a model system of tooth enamel formation. J of Crystal Growth, 222 (3), 615- 626 (2001). (Pubitemid 32093347)
    • (2001) Journal of Crystal Growth , vol.222 , Issue.3 , pp. 615-626
    • Iijima, M.1    Moriwaki, Y.2    Takagi, T.3    Moradian-Oldak, J.4
  • 204
    • 56749182087 scopus 로고    scopus 로고
    • Controlled remineralization of enamel in the presence of amelogenin and fluoride
    • Y. Fan, Z. Sun and J. Moradian-Oldak: Controlled remineralization of enamel in the presence of amelogenin and fluoride. Biomaterials, 30 (4), 478-83 (2009).
    • (2009) Biomaterials , vol.30 , Issue.4 , pp. 478-483
    • Fan, Y.1    Sun, Z.2    Moradian-Oldak, J.3
  • 205
    • 79953859109 scopus 로고    scopus 로고
    • Amelogenin-assisted ex vivo remineralization of human enamel: Effects of supersaturation degree and fluoride concentration
    • Y. Fan, J. R. Nelson, J. R. Alvarez, J. Hagan, A. Berrier and X. Xu: Amelogenin-assisted ex vivo remineralization of human enamel: Effects of supersaturation degree and fluoride concentration. Acta Biomater, 7 (5), 2293-302 (2011).
    • (2011) Acta Biomater , vol.7 , Issue.5 , pp. 2293-2302
    • Fan, Y.1    Nelson, J.R.2    Alvarez, J.R.3    Hagan, J.4    Berrier, A.5    Xu, X.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.