메뉴 건너뛰기




Volumn , Issue 205, 1997, Pages 118-134

Amelogenin proteins of developing dental enamel

Author keywords

[No Author keywords available]

Indexed keywords

AMELOGENIN; ENAMEL PROTEIN;

EID: 0030633402     PISSN: 03005208     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (84)

References (41)
  • 1
    • 0001829223 scopus 로고
    • Mechanism of amelogenetic mineralization in minipig secretory enamel
    • Fearnhead RW (ed) Florence, Yokahama
    • Aoba T, Moreno EC 1989 Mechanism of amelogenetic mineralization in minipig secretory enamel. In: Fearnhead RW (ed) Tooth enamel, vol V. Florence, Yokahama, p 163-167
    • (1989) Tooth Enamel , vol.5 , pp. 163-167
    • Aoba, T.1    Moreno, E.C.2
  • 2
    • 0025494186 scopus 로고
    • Molecular conformation of porcine amelogenins and its significance in protein-mineral interaction: 1H-NMR photo-CIDNP study
    • Aoba T, Kawano K, Moreno EC 1990 Molecular conformation of porcine amelogenins and its significance in protein-mineral interaction: 1H-NMR photo-CIDNP study. J Biol Buccale 18:189-194
    • (1990) J Biol Buccale , vol.18 , pp. 189-194
    • Aoba, T.1    Kawano, K.2    Moreno, E.C.3
  • 3
    • 0021789457 scopus 로고
    • Morphological studies on the distribution of enamel matrix proteins using routine electron microscopy and freeze-fracture replicas in the rat incisor
    • Bai P, Warshawsky H 1985 Morphological studies on the distribution of enamel matrix proteins using routine electron microscopy and freeze-fracture replicas in the rat incisor. Anat Rec 212:1-16
    • (1985) Anat Rec , vol.212 , pp. 1-16
    • Bai, P.1    Warshawsky, H.2
  • 4
    • 0013805367 scopus 로고
    • Molecular structure of the neutral soluble proteins of embryonic bovine enamel in the solid state
    • Bonar LC, Glimcher MJ, Mechanic GL 1965 Molecular structure of the neutral soluble proteins of embryonic bovine enamel in the solid state. J Ultrastruct Res 13:308-317
    • (1965) J Ultrastruct Res , vol.13 , pp. 308-317
    • Bonar, L.C.1    Glimcher, M.J.2    Mechanic, G.L.3
  • 5
    • 0028800692 scopus 로고
    • Initial enamel crystals are not spatially associated with mineralized dentin
    • Diekwisch TGH, Berman BJ, Genter S, Slavkin HC 1995 Initial enamel crystals are not spatially associated with mineralized dentin. Cell Tissue Res 279:149-167
    • (1995) Cell Tissue Res , vol.279 , pp. 149-167
    • Diekwisch, T.G.H.1    Berman, B.J.2    Genter, S.3    Slavkin, H.C.4
  • 7
    • 0030435714 scopus 로고    scopus 로고
    • Comparative mass spectrometric analyses of enamel matrix proteins from five species suggest a common pathway of post-secretory proteolytic processing
    • in press
    • Fincham AG, Moradian-Oldak J 1996 Comparative mass spectrometric analyses of enamel matrix proteins from five species suggest a common pathway of post-secretory proteolytic processing. Connect Tiss Res, in press
    • (1996) Connect Tiss Res
    • Fincham, A.G.1    Moradian-Oldak, J.2
  • 8
    • 0345280028 scopus 로고
    • The matrix of enamel and related mineralized keratins
    • Fearnhead RW (ed) Wright Brothers, Bristol
    • Fincham AG, Graham GN, Pautard FGE 1965 The matrix of enamel and related mineralized keratins. In: Fearnhead RW (ed) Tooth enamel. Wright Brothers, Bristol, p 117-123
    • (1965) Tooth Enamel , pp. 117-123
    • Fincham, A.G.1    Graham, G.N.2    Pautard, F.G.E.3
  • 10
    • 0026039619 scopus 로고
    • Amelogenin post-secretory processing during biomineralization in the postnatal mouse molar tooth
    • Fincham AG, Hu Y, Lau EC, Slavkin HC, Snead ML 1991 Amelogenin post-secretory processing during biomineralization in the postnatal mouse molar tooth. Arch Oral Biol 36:305-317
    • (1991) Arch Oral Biol , vol.36 , pp. 305-317
    • Fincham, A.G.1    Hu, Y.2    Lau, E.C.3    Slavkin, H.C.4    Snead, M.L.5
  • 11
    • 0028360425 scopus 로고
    • Self-assembly of a recombinant amelogenin protein generates supramolecular structures
    • Fincham AG, Moradian-Oldak J, Simmer JP et al 1994 Self-assembly of a recombinant amelogenin protein generates supramolecular structures. J Struct Biol 112:103-109
    • (1994) J Struct Biol , vol.112 , pp. 103-109
    • Fincham, A.G.1    Moradian-Oldak, J.2    Simmer, J.P.3
  • 12
    • 0028825987 scopus 로고
    • Evidence for amelogenin 'nanospheres' as functional components of secretory-stage enamel matrix
    • Fincham AG, Moradian-Oldak J, Diekwisch TGH et al 1995 Evidence for amelogenin 'nanospheres' as functional components of secretory-stage enamel matrix. J Struct Biol 115:50-59
    • (1995) J Struct Biol , vol.115 , pp. 50-59
    • Fincham, A.G.1    Moradian-Oldak, J.2    Diekwisch, T.G.H.3
  • 14
    • 0026029107 scopus 로고
    • Identification of the leucine-rich amelogenin peptide (LRAP) as the translation product of an alternatively spliced transcript
    • Gibson CW, Golub E, Ding W et al 1991 Identification of the leucine-rich amelogenin peptide (LRAP) as the translation product of an alternatively spliced transcript. Biochem Biophys Res Commun 174:1306-1312
    • (1991) Biochem Biophys Res Commun , vol.174 , pp. 1306-1312
    • Gibson, C.W.1    Golub, E.2    Ding, W.3
  • 15
    • 0018442351 scopus 로고
    • Phosphopeptides of enamel matrix
    • Glimcher MJ 1979 Phosphopeptides of enamel matrix. J Dent Res 58:790B-806B
    • (1979) J Dent Res , vol.58
    • Glimcher, M.J.1
  • 16
    • 0027403490 scopus 로고
    • Molecular conformation of porcine amelogenin in solution: Three folding units at the N-terminal, central, and C-terminal regions
    • Goto Y, Kogure E, Takagi T, Aimoto S, Aoba T 1993 Molecular conformation of porcine amelogenin in solution: three folding units at the N-terminal, central, and C-terminal regions. J Biochem 113:55-60
    • (1993) J Biochem , vol.113 , pp. 55-60
    • Goto, Y.1    Kogure, E.2    Takagi, T.3    Aimoto, S.4    Aoba, T.5
  • 17
    • 33748606799 scopus 로고    scopus 로고
    • Cloning, DNA sequence and alternative splicing of opossum amelogenin mRNAs
    • in press
    • Hu CC, Zhang C, Qian Q 1996 Cloning, DNA sequence and alternative splicing of opossum amelogenin mRNAs. Calcif Tissue Res, in press
    • (1996) Calcif Tissue Res
    • Hu, C.C.1    Zhang, C.2    Qian, Q.3
  • 18
    • 0029965108 scopus 로고    scopus 로고
    • Full-length sequence, localization, and chromosomal mapping of ameloblastin: A novel tooth-specific gene
    • Krebsbach PH, Lee SK, Matsuki Y, Kozak CA, Yamada RM, Yamada Y 1996 Full-length sequence, localization, and chromosomal mapping of ameloblastin: a novel tooth-specific gene. J Biol Chem 271:4431-4435
    • (1996) J Biol Chem , vol.271 , pp. 4431-4435
    • Krebsbach, P.H.1    Lee, S.K.2    Matsuki, Y.3    Kozak, C.A.4    Yamada, R.M.5    Yamada, Y.6
  • 20
    • 0028921003 scopus 로고
    • Amelogenin signal peptide mutation: Correlation between mutations in the amelogenin gene (AMGX) and manifestations of the X-linked amelogenesis imperfecta
    • Lagerström-Fermér M, Nilsson M, Bäckman B et al 1995 Amelogenin signal peptide mutation: correlation between mutations in the amelogenin gene (AMGX) and manifestations of the X-linked amelogenesis imperfecta. Genomics 26:159-162
    • (1995) Genomics , vol.26 , pp. 159-162
    • Lagerström-Fermér, M.1    Nilsson, M.2    Bäckman, B.3
  • 21
    • 0026483347 scopus 로고
    • Alternative splicing of the mouse amelogenin primary RNA transcript contributes to amelogenin heterogeneity
    • Lau EC, Simmer JP, Bringas P et al 1992 Alternative splicing of the mouse amelogenin primary RNA transcript contributes to amelogenin heterogeneity. Biochem Biophys Res Commun 188:1253-1260
    • (1992) Biochem Biophys Res Commun , vol.188 , pp. 1253-1260
    • Lau, E.C.1    Simmer, J.P.2    Bringas, P.3
  • 23
    • 0028846708 scopus 로고
    • A synthetic, chemically modified ribozyme eliminates amelogenin, the major translation product in developing mouse enamel in vivo
    • in press
    • Lyngstadaas SP, Risnes S, Sproat BS, Thrane P, Prydz HP 1995 A synthetic, chemically modified ribozyme eliminates amelogenin, the major translation product in developing mouse enamel in vivo. EMBO J, in press
    • (1995) EMBO J
    • Lyngstadaas, S.P.1    Risnes, S.2    Sproat, B.S.3    Thrane, P.4    Prydz, H.P.5
  • 24
    • 0028484081 scopus 로고
    • Specific cleavage of a recombinant murine amelogenin by a proteinase fraction isolated from bovine tooth enamel
    • Moradian-Oldak J, Simmer JP, Sarte PE, Zeichner-David M, Fincham AG 1994a Specific cleavage of a recombinant murine amelogenin by a proteinase fraction isolated from bovine tooth enamel. Arch Oral Biol 39:647-656
    • (1994) Arch Oral Biol , vol.39 , pp. 647-656
    • Moradian-Oldak, J.1    Simmer, J.P.2    Sarte, P.E.3    Zeichner-David, M.4    Fincham, A.G.5
  • 27
    • 0345240473 scopus 로고
    • The nature of the protein matrix of human enamel
    • IADR
    • Piez KA 1960 The nature of the protein matrix of human enamel. J Dental Res Abstracts, IADR 39:712
    • (1960) J Dental Res Abstracts , vol.39 , pp. 712
    • Piez, K.A.1
  • 28
    • 0024500210 scopus 로고
    • Tooth enamel protein, amelogenin, has a probable β-spiral internal channel, GLN112-LEU138, within a single polypeptide chain: Preliminary molecular mechanics and dynamics studies
    • Renugopalakrishnan V, Pattabiraman N, Prabhakaran M, Strawich E, Glimcher MJ 1989 Tooth enamel protein, amelogenin, has a probable β-spiral internal channel, GLN112-LEU138, within a single polypeptide chain: preliminary molecular mechanics and dynamics studies. Biopolymers 28:297-303
    • (1989) Biopolymers , vol.28 , pp. 297-303
    • Renugopalakrishnan, V.1    Pattabiraman, N.2    Prabhakaran, M.3    Strawich, E.4    Glimcher, M.J.5
  • 29
    • 0000086238 scopus 로고
    • The appearance of developing rat incisor enamel using a freeze-fracture technique
    • Robinson C, Fuchs P, Weatherell JA 1981 The appearance of developing rat incisor enamel using a freeze-fracture technique. J Crystal Growth 53:160-165
    • (1981) J Crystal Growth , vol.53 , pp. 160-165
    • Robinson, C.1    Fuchs, P.2    Weatherell, J.A.3
  • 30
  • 31
    • 0026541083 scopus 로고
    • The human enamel protein gene amelogenin is expressed from both the X and the Y chromosomes
    • Salido EC, Yen PH, Koprivnikar K, Yu L-C, Shapiro LJ 1992 The human enamel protein gene amelogenin is expressed from both the X and the Y chromosomes. Am J Hum Genet 50: 303-316
    • (1992) Am J Hum Genet , vol.50 , pp. 303-316
    • Salido, E.C.1    Yen, P.H.2    Koprivnikar, K.3    Yu, L.-C.4    Shapiro, L.J.5
  • 32
    • 0029079604 scopus 로고
    • Molecular mechanisms of dental enamel formation
    • Simmer J P, Fincham AG 1995 Molecular mechanisms of dental enamel formation. Crit Rev Oral Biol Med 6:84-108
    • (1995) Crit Rev Oral Biol Med , vol.6 , pp. 84-108
    • Simmer, J.P.1    Fincham, A.G.2
  • 33
    • 85053649481 scopus 로고
    • Molecular biology of the amelogenin gene
    • Robinson C, Kirkham J, Shore RC (eds) CRC Press, Boca Raton, FL
    • Simmer JP, Snead ML 1995 Molecular biology of the amelogenin gene. In: Robinson C, Kirkham J, Shore RC (eds) Dental enamel: formation to destruction. CRC Press, Boca Raton, FL, p 59-84
    • (1995) Dental Enamel: Formation to Destruction , pp. 59-84
    • Simmer, J.P.1    Snead, M.L.2
  • 34
    • 0028222888 scopus 로고
    • Isolation and characterization of a mouse amelogenin expressed in Escherichia coli
    • Simmer JP, Lau EC, Hu C-C et al 1994 Isolation and characterization of a mouse amelogenin expressed in Escherichia coli. Calcif Tissue Int 54:312-319
    • (1994) Calcif Tissue Int , vol.54 , pp. 312-319
    • Simmer, J.P.1    Lau, E.C.2    Hu, C.-C.3
  • 35
    • 0016828309 scopus 로고
    • Structural sub-units in prisms of immature rat enamel
    • Smales FC 1975 Structural sub-units in prisms of immature rat enamel. Nature 258:772-774
    • (1975) Nature , vol.258 , pp. 772-774
    • Smales, F.C.1
  • 37
    • 84985720076 scopus 로고
    • 1H Magnetic double-resonance study of fetal enamel matrix proteins
    • 1H Magnetic double-resonance study of fetal enamel matrix proteins. Biopolymers 19:741-750
    • (1980) Biopolymers , vol.19 , pp. 741-750
    • Termine, J.D.1    Torchia, D.A.2
  • 38
    • 0019205616 scopus 로고
    • Properties of dissociatively extracted fetal tooth matrix proteins. I. Principal molecular species in developing bovine enamel
    • Termine JD, Belcourt AB, Christner PJ, Conn KM, Nylen MU 1980 Properties of dissociatively extracted fetal tooth matrix proteins. I. Principal molecular species in developing bovine enamel. J Biol Chem 255:9760-9768
    • (1980) J Biol Chem , vol.255 , pp. 9760-9768
    • Termine, J.D.1    Belcourt, A.B.2    Christner, P.J.3    Conn, K.M.4    Nylen, M.U.5
  • 39
    • 0004280956 scopus 로고
    • Diffraction studies of enamel protein-mineral structural relations
    • Butler WT (ed) EBSCO Media, Birmingham, AL
    • Traub W, Jodaikin A, Weiner S 1985 Diffraction studies of enamel protein-mineral structural relations. In: Butler WT (ed) The chemistry and biology of mineralized tissues. EBSCO Media, Birmingham, AL, p 221-225
    • (1985) The Chemistry and Biology of Mineralized Tissues , pp. 221-225
    • Traub, W.1    Jodaikin, A.2    Weiner, S.3
  • 40
    • 78651157441 scopus 로고
    • The structure and organization of, and the relationship between, the organic matrix and the inorganic crystals of embryonic bovine enamel
    • Travis DF, Glimcher MJ 1964 The structure and organization of, and the relationship between, the organic matrix and the inorganic crystals of embryonic bovine enamel. J Cell Biol 23: 477-497
    • (1964) J Cell Biol , vol.23 , pp. 477-497
    • Travis, D.F.1    Glimcher, M.J.2
  • 41
    • 0029110869 scopus 로고
    • Elastic biomolecular machines
    • Urry DW 1995 Elastic biomolecular machines. Sci Am 272:64-69
    • (1995) Sci Am , vol.272 , pp. 64-69
    • Urry, D.W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.