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Volumn 194, Issue 2-4, 2011, Pages 284-290

Folding, assembly, and aggregation of recombinant murine amelogenins with T21I and P41T point mutations

Author keywords

Amelogenesis imperfecta; Amelogenin; Dynamic light scattering; Enamel; Fluorescence spectroscopy; Protein aggregation; Thermal denaturation

Indexed keywords

AMELOGENIN; MONOMER; OLIGOMER; TRYPTOPHAN;

EID: 80051800959     PISSN: 14226405     EISSN: 14226421     Source Type: Journal    
DOI: 10.1159/000324342     Document Type: Conference Paper
Times cited : (12)

References (13)
  • 2
    • 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
    • Collier, P.M., J.J. Sauk, J. Rosenbloom, Z.A. Yuan, C.W. Gibson (1997) An amelogenin gene defect associated with human X-linked amelogenesis imperfecta. Arch Oral Biol 42: 235-242. (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
  • 3
    • 0028019289 scopus 로고
    • Mass-spectrographic analysis of a porcine amelogenin identifies a single phosphorylated locus
    • DOI 10.1007/BF00299322
    • Fincham, A.G., J. Moradianoldak. P.E. Sarte (1994) Mass-spectrographic analysis of a porcine amelogenin identifies a single phosphorylated locus. Calcif Tissue Int 55: 398-400. (Pubitemid 24332750)
    • (1994) Calcified Tissue International , vol.55 , Issue.5 , pp. 398-400
    • Fincham, A.G.1    Moradian-Oldak, J.2    Sarte, P.E.3
  • 4
    • 78650412788 scopus 로고    scopus 로고
    • Perturbed amelogenin secondary structure leads to uncontrolled aggregation in amelogenesis imperfecta mutant proteins
    • Lakshminarayanan, R., K.M. Bromley, Y.P. Lei, M.L. Snead, J. Moradian-Oldak (2010) Perturbed amelogenin secondary structure leads to uncontrolled aggregation in amelogenesis imperfecta mutant proteins. J Biol Chem 285: 40593-40603.
    • (2010) J Biol Chem , Issue.285 , pp. 40593-40603
    • Lakshminarayanan, R.1    Bromley, K.M.2    Lei, Y.P.3    Snead, M.L.4    Moradian-Oldak, J.5
  • 5
    • 0028947327 scopus 로고
    • Characterization Of molecular defects in X-Linked amelogenesis imperfecta (Aih1)
    • Lench, N.J., G.B. Winter (1995) Characterization Of molecular defects in X-Linked amelogenesis imperfecta (Aih1). Hum Mutat 5: 251-259.
    • (1995) Hum Mutat , vol.5 , pp. 251-259
    • Lench, N.J.1    Winter, G.B.2
  • 6
    • 0034857932 scopus 로고    scopus 로고
    • Amelogenins: Assembly, processing and control of crystal morphology
    • DOI 10.1016/S0945-053X(01)00154-8, PII S0945053X01001548
    • Moradian-Oldak, J. (2001) Amelogenins: Assembly, processing and control of crystal morphology. Matrix Biol 20: 293-305. (Pubitemid 32846714)
    • (2001) Matrix Biology , vol.20 , Issue.5-6 , pp. 293-305
    • Moradian-Oldak, J.1
  • 7
    • 0033821661 scopus 로고    scopus 로고
    • Self-assembly properties of recombinant engineered amelogenin proteins analyzed by dynamic light scattering and atomic force microscopy
    • Moradian-Oldak, J., M.L. Paine, Y.P. Lei, A.G. Fincham, M.L. Snead (2000) Self-assembly properties of recombinant engineered amelogenin proteins analyzed by dynamic light scattering and atomic force microscopy. J Struct Biol 131: 27-37.
    • (2000) J Struct Biol , vol.131 , pp. 27-37
    • Moradian-Oldak, J.1    Paine, M.L.2    Lei, Y.P.3    Fincham, A.G.4    Snead, M.L.5
  • 8
    • 0037053346 scopus 로고    scopus 로고
    • Altered amelogenin self-assembly based on mutations observed in human X-linked amelogenesis imperfecta (AIH1)
    • DOI 10.1074/jbc.M110473200
    • Paine, M. L., Y.P. Lei, K. Dickerson, M.L. Snead (2002) Altered amelogenin self-assembly based on mutations observed in human Xlinked amelogenesis imperfecta (AIH1). J Biol Chem 277: 17112-17116. (Pubitemid 34967743)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.19 , pp. 17112-17116
    • Paine, M.L.1    Lei, Y.-P.2    Dickerson, K.3    Snead, M.L.4
  • 9
    • 0031034185 scopus 로고    scopus 로고
    • Protein interactions during assembly of the enamel organic extracellular matrix
    • DOI 10.1359/jbmr.1997.12.2.221
    • Paine, M.L., M.L. Snead (1997) Protein interactions during assembly of the enamel organic extracellular matrix. J Bone Miner Res 12: 221-227. (Pubitemid 27086302)
    • (1997) Journal of Bone and Mineral Research , vol.12 , Issue.2 , pp. 221-227
    • Paine, M.L.1    Snead, M.L.2
  • 10
    • 0029079604 scopus 로고
    • Molecular mechanisms of dental enamel formation
    • Simmer, J.P., A.G. Fincham (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
  • 12
    • 0036153571 scopus 로고    scopus 로고
    • What does it mean to be natively unfolded?
    • DOI 10.1046/j.0014-2956.2001.02649.x
    • Uversky, V.N. (2002) What does it mean to be natively unfolded? Eur J Biochem 269: 2-12. (Pubitemid 34107333)
    • (2002) European Journal of Biochemistry , vol.269 , Issue.1 , pp. 2-12
    • Uversky, V.N.1
  • 13
    • 33845277788 scopus 로고    scopus 로고
    • The molecular etiologies and associated phenotypes of amelogenesis imperfecta
    • DOI 10.1002/ajmg.a.31358
    • Wright, J.T. (2006) The molecular etiologies and associated phenotypes of amelogenesis imperfecta. Am J Med Genet A 140A: 2547-2555. (Pubitemid 44865082)
    • (2006) American Journal of Medical Genetics, Part A , vol.140 , Issue.23 , pp. 2547-2555
    • Wright, J.T.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.