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Volumn 100 B, Issue 4, 2012, Pages 1009-1016

Effect of dental tissue conditioners and matrix metalloproteinase inhibitors on type i collagen microstructure analyzed by Fourier transform infrared spectroscopy

Author keywords

collagen; Fourier Transform Infrared spectroscopy; matrix metalloproteinase; membrane; proanthocyanidin

Indexed keywords

COLLAGEN; ETHYLENEDIAMINETETRAACETIC ACID; FLAVONOIDS; HYDROGEN BONDS; HYDROXYPROLINE; MEMBRANES; MICROSTRUCTURE; PHOSPHORIC ACID; SUPERSATURATION; SURFACE TREATMENT;

EID: 84859583477     PISSN: 15524973     EISSN: 15524981     Source Type: Journal    
DOI: 10.1002/jbm.b.32666     Document Type: Article
Times cited : (35)

References (40)
  • 1
    • 0031267556 scopus 로고    scopus 로고
    • The dentin substrate: Structure and properties related to bonding
    • Marshall GW Jr, Marshall SJ, Kinney JH, Balooch M,. The dentin substrate: Structure and properties related to bonding. J Dent 1997; 25: 441-458.
    • (1997) J Dent , vol.25 , pp. 441-458
    • Marshall, Jr.G.W.1    Marshall, S.J.2    Kinney, J.H.3    Balooch, M.4
  • 2
    • 0017884054 scopus 로고
    • Phosphophoryns-Major noncollagenous proteins of rat incisor dentin
    • Dimuzio MT, Veis A,. Phosphophoryns-Major noncollagenous proteins of rat incisor dentin. Calcif Tissue Res 1978; 25: 169-178.
    • (1978) Calcif Tissue Res , vol.25 , pp. 169-178
    • Dimuzio, M.T.1    Veis, A.2
  • 3
    • 0020137778 scopus 로고
    • The promotion of adhesion by the infiltration of monomers into tooth substrates
    • Nakabayashi N, Kojima K, Masuhara E,. The promotion of adhesion by the infiltration of monomers into tooth substrates. J Biomed Mater Res 1982; 16: 265-273.
    • (1982) J Biomed Mater Res , vol.16 , pp. 265-273
    • Nakabayashi, N.1    Kojima, K.2    Masuhara, E.3
  • 8
    • 0034133331 scopus 로고    scopus 로고
    • Effects of acids and additives on the susceptibility of human dentine to denaturation
    • Agee K, Zhang Y, Pashley DH,. Effects of acids and additives on the susceptibility of human dentine to denaturation. J Oral Rehab 2000; 27: 136-141.
    • (2000) J Oral Rehab , vol.27 , pp. 136-141
    • Agee, K.1    Zhang, Y.2    Pashley, D.H.3
  • 9
    • 0018368995 scopus 로고
    • Changes in the dentine of human teeth following extraction and their implication for in-vitro studies of adhesion to tooth substance
    • Causton BE, Johnson NW,. Changes in the dentine of human teeth following extraction and their implication for in-vitro studies of adhesion to tooth substance. Arch Oral Biol 1979; 24: 229-232.
    • (1979) Arch Oral Biol , vol.24 , pp. 229-232
    • Causton, B.E.1    Johnson, N.W.2
  • 14
    • 77956172795 scopus 로고    scopus 로고
    • Mechanical characterization of proanthocyanidin-dentin matrix interaction
    • Castellan CS, Pereira PN, Grande RH, Bedran-Russo AK,. Mechanical characterization of proanthocyanidin-dentin matrix interaction. Dent Mater 2010; 26: 968-973.
    • (2010) Dent Mater , vol.26 , pp. 968-973
    • Castellan, C.S.1    Pereira, P.N.2    Grande, R.H.3    Bedran-Russo, A.K.4
  • 15
    • 0014516140 scopus 로고
    • O-Quinones formed in plant extracts. Their reactions with amino acids and peptides
    • Pierpoint WS,. o-Quinones formed in plant extracts. Their reactions with amino acids and peptides. Biochem J 1969; 112: 609-616.
    • (1969) Biochem J , vol.112 , pp. 609-616
    • Pierpoint, W.S.1
  • 16
    • 0016362991 scopus 로고
    • Overcoming problems of phenolics and quinones in the isolation of plant enzymes and organelles
    • Loomis WD,. Overcoming problems of phenolics and quinones in the isolation of plant enzymes and organelles. Methods Enzymol 1974; 31: 528-544.
    • (1974) Methods Enzymol , vol.31 , pp. 528-544
    • Loomis, W.D.1
  • 17
    • 0019876875 scopus 로고
    • The specificity of proanthocyanidin-protein interactions
    • Hagerman AE, Butler LG,. The specificity of proanthocyanidin-protein interactions. J Biol Chem 1981; 256: 4494-4497.
    • (1981) J Biol Chem , vol.256 , pp. 4494-4497
    • Hagerman, A.E.1    Butler, L.G.2
  • 18
    • 0041922601 scopus 로고    scopus 로고
    • Proanthocyanidin: A natural crosslinking reagent for stabilizing collagen matrices
    • Han B, Jaurequi J, Tang BW, Nimni ME,. Proanthocyanidin: A natural crosslinking reagent for stabilizing collagen matrices. J Biomed Mater Res A 2003; 65: 118-124.
    • (2003) J Biomed Mater Res A , vol.65 , pp. 118-124
    • Han, B.1    Jaurequi, J.2    Tang, B.W.3    Nimni, M.E.4
  • 20
    • 33847146643 scopus 로고    scopus 로고
    • Binding affinity of proanthocyanidin from waste Pinus radiata bark onto proline-rich bovine Achilles tendon collagen type i
    • Ku CS, Sathishkumar M, Mun SP,. Binding affinity of proanthocyanidin from waste Pinus radiata bark onto proline-rich bovine Achilles tendon collagen type I. Chemosphere 2007; 67: 1618-1627.
    • (2007) Chemosphere , vol.67 , pp. 1618-1627
    • Ku, C.S.1    Sathishkumar, M.2    Mun, S.P.3
  • 21
    • 0035545064 scopus 로고    scopus 로고
    • Molecular structure of acid-etched dentin smear layers-in situ study
    • Spencer P, Wang Y, Walker MP, Swafford JR,. Molecular structure of acid-etched dentin smear layers-in situ study. J Dent Res 2001; 80: 1802-1807.
    • (2001) J Dent Res , vol.80 , pp. 1802-1807
    • Spencer, P.1    Wang, Y.2    Walker, M.P.3    Swafford, J.R.4
  • 22
    • 0036857613 scopus 로고    scopus 로고
    • Obtenção e caracterizaçà £o de blendas colágeno-quitosana
    • Tonhi E, Plepis AMdG,. Obtenção e caracterização de blendas colágeno-quitosana. Química Nova 2002; 25: 943-948.
    • (2002) Química Nova , vol.25 , pp. 943-948
    • Tonhi, E.1    Plepis, A.2
  • 23
    • 0025921568 scopus 로고
    • FTIRS in water demonstrates that collagen monomers undergo a conformational transition prior to thermal self-assembly in vitro
    • George A, Veis A,. FTIRS in water demonstrates that collagen monomers undergo a conformational transition prior to thermal self-assembly in vitro. Biochemistry 1991; 30: 2372-2377.
    • (1991) Biochemistry , vol.30 , pp. 2372-2377
    • George, A.1    Veis, A.2
  • 25
    • 77958060714 scopus 로고    scopus 로고
    • Mid-infrared spectroscopy coupled with chemometrics: A tool for the analysis of intact food systems and the exploration of their molecular structure-quality relationships-A review
    • Karoui R, Downey G, Blecker C,. Mid-infrared spectroscopy coupled with chemometrics: A tool for the analysis of intact food systems and the exploration of their molecular structure-quality relationships-A review. Chem Rev 2010; 110: 6144-6168.
    • (2010) Chem Rev , vol.110 , pp. 6144-6168
    • Karoui, R.1    Downey, G.2    Blecker, C.3
  • 26
    • 0018858817 scopus 로고
    • Collagen: Molecular diversity in the body's protein scaffold
    • Eyre D,. Collagen: Molecular diversity in the body's protein scaffold. Science 1980; 207: 1315-1322.
    • (1980) Science , vol.207 , pp. 1315-1322
    • Eyre, D.1
  • 27
    • 34347251868 scopus 로고    scopus 로고
    • FTIR studies of collagen model peptides: Complementary experimental and simulation approaches to conformation and unfolding
    • Bryan MA, Brauner JW, Anderle G, Flach CR, Brodsky B, Mendelsohn R,. FTIR studies of collagen model peptides: Complementary experimental and simulation approaches to conformation and unfolding. J Am Chem Soc 2007; 129: 7877-7884.
    • (2007) J Am Chem Soc , vol.129 , pp. 7877-7884
    • Bryan, M.A.1    Brauner, J.W.2    Anderle, G.3    Flach, C.R.4    Brodsky, B.5    Mendelsohn, R.6
  • 28
    • 0019882126 scopus 로고
    • Determination of the secondary structure of proteins from the amide i band of the laser Raman spectrum
    • Williams RW, Dunker AK,. Determination of the secondary structure of proteins from the amide I band of the laser Raman spectrum. J Mol Biol 1981; 152: 783-813.
    • (1981) J Mol Biol , vol.152 , pp. 783-813
    • Williams, R.W.1    Dunker, A.K.2
  • 29
    • 0015438002 scopus 로고
    • Infrared spectroscopy-Conformation
    • Susi H,. Infrared spectroscopy-Conformation. Methods Enzymol 1972; 26 PtC: 455-472.
    • (1972) Methods Enzymol , vol.26 , Issue.PART C , pp. 455-472
    • Susi, H.1
  • 32
    • 60749099355 scopus 로고    scopus 로고
    • 4/NaOCl dentine treatments may increase hybrid layers' resistance to degradation: A microtensile bond strength and confocal-micropermeability study
    • 4/NaOCl dentine treatments may increase hybrid layers' resistance to degradation: A microtensile bond strength and confocal-micropermeability study. J Dent 2009; 37: 279-288.
    • (2009) J Dent , vol.37 , pp. 279-288
    • Sauro, S.1    Mannocci, F.2    Toledano, M.3    Osorio, R.4    Pashley, D.H.5    Watson, T.F.6
  • 34
    • 79959701203 scopus 로고    scopus 로고
    • Review of matrix metalloproteinases' effect on the hybrid dentin bond layer stability and chlorhexidine clinical use to prevent bond failure
    • Moon PC, Weaver J, Brooks CN,. Review of matrix metalloproteinases' effect on the hybrid dentin bond layer stability and chlorhexidine clinical use to prevent bond failure. Open Dent J 2010; 4: 147-152.
    • (2010) Open Dent J , vol.4 , pp. 147-152
    • Moon, P.C.1    Weaver, J.2    Brooks, C.N.3
  • 35
    • 0028533778 scopus 로고
    • Interaction of chlorhexidine digluconate with and adsorption of chlorhexidine on hydroxyapatite
    • Misra DN,. Interaction of chlorhexidine digluconate with and adsorption of chlorhexidine on hydroxyapatite. J Biomed Mater Res 1994; 28: 1375-1381.
    • (1994) J Biomed Mater Res , vol.28 , pp. 1375-1381
    • Misra, D.N.1
  • 36
    • 0032911382 scopus 로고    scopus 로고
    • Inhibition of the activities of matrix metalloproteinases 2, 8, and 9 by chlorhexidine
    • Gendron R, Grenier D, Sorsa T, Mayrand D,. Inhibition of the activities of matrix metalloproteinases 2, 8, and 9 by chlorhexidine. Clin Diagn Lab Immunol 1999; 6: 437-439.
    • (1999) Clin Diagn Lab Immunol , vol.6 , pp. 437-439
    • Gendron, R.1    Grenier, D.2    Sorsa, T.3    Mayrand, D.4
  • 39
    • 0024402770 scopus 로고
    • Collagen banded fibril structure and the collagen-platelet reaction
    • Sylvester MF, Yannas IV, Salzman EW, Forbes MJ,. Collagen banded fibril structure and the collagen-platelet reaction. Thromb Res 1989; 55: 135-148.
    • (1989) Thromb Res , vol.55 , pp. 135-148
    • Sylvester, M.F.1    Yannas, I.V.2    Salzman, E.W.3    Forbes, M.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.