메뉴 건너뛰기




Volumn 8, Issue 7, 2012, Pages 2419-2433

The dentin organic matrix - Limitations of restorative dentistry hidden on the nanometer scale

Author keywords

Adhesion; Bonding; Collagen; Dentin; Polymers

Indexed keywords

COLLAGEN; DENTAL MATERIALS; DENTISTRY; FILLING; MOLECULES; RESTORATION; SUPRAMOLECULAR CHEMISTRY;

EID: 84861610026     PISSN: 17427061     EISSN: 18787568     Source Type: Journal    
DOI: 10.1016/j.actbio.2012.02.022     Document Type: Review
Times cited : (157)

References (148)
  • 1
    • 24044515570 scopus 로고    scopus 로고
    • Surveillance for dental caries, dental sealants, tooth retention, edentulism, and enamel fluorosis -United States, 1988-1994 and 1999-2002
    • Atlanta, GA: Centers for Disease Control and, Prevention
    • Beltran-Aguilar ED, Barker LK, Canto MT, Dye BA, Gooch BF, Griffin SO, et al. Surveillance for dental caries, dental sealants, tooth retention, edentulism, and enamel fluorosis -United States, 1988-1994 and 1999-2002. Surveillance Summaries 54: MMWR. Atlanta, GA: Centers for Disease Control and, Prevention; 2005. p. 1-13.
    • (2005) Surveillance Summaries 54: MMWR , pp. 1-13
    • Beltran-Aguilar, E.D.1    Barker, L.K.2    Canto, M.T.3    Dye, B.A.4    Gooch, B.F.5    Griffin, S.O.6
  • 2
    • 84861613586 scopus 로고    scopus 로고
    • NHEA Washington, DC: US Department of Health and Human Services
    • NHEA. National health expenditure projections 2009-2019. Washington, DC: US Department of Health and Human Services; 2006.
    • (2006) National Health Expenditure Projections 2009-2019
  • 3
    • 77956441254 scopus 로고    scopus 로고
    • Nanomaterials in preventive dentistry
    • M. Hannig, and C. Hannig Nanomaterials in preventive dentistry Nat Nanotechnol 5 2010 565 569
    • (2010) Nat Nanotechnol , vol.5 , pp. 565-569
    • Hannig, M.1    Hannig, C.2
  • 4
    • 78651229763 scopus 로고    scopus 로고
    • Resin composite- state of the art
    • J.L. Ferracane Resin composite- state of the art Dent Mater 27 2011 29 38
    • (2011) Dent Mater , vol.27 , pp. 29-38
    • Ferracane, J.L.1
  • 6
    • 0036617770 scopus 로고    scopus 로고
    • Dental adhesives of the future
    • F.R. Tay, and D.H. Pashley Dental adhesives of the future J Adhes Dent 4 2002 91 103
    • (2002) J Adhes Dent , vol.4 , pp. 91-103
    • Tay, F.R.1    Pashley, D.H.2
  • 7
    • 79959916108 scopus 로고    scopus 로고
    • Advances in dental materials
    • R.M. Vaderhobli Advances in dental materials Dent Clin Nor Am 55 2011 619 625
    • (2011) Dent Clin Nor Am , vol.55 , pp. 619-625
    • Vaderhobli, R.M.1
  • 8
    • 4644263809 scopus 로고    scopus 로고
    • Buonocore Memorial Lecture. Review of the clinical survival of direct and indirect restorations in posterior teeth of the permanent dentition
    • J. Manhart, H. Chen, G. Hamm, and R. Hickel Buonocore Memorial Lecture. Review of the clinical survival of direct and indirect restorations in posterior teeth of the permanent dentition Oper Dent 29 2004 481 508
    • (2004) Oper Dent , vol.29 , pp. 481-508
    • Manhart, J.1    Chen, H.2    Hamm, G.3    Hickel, R.4
  • 9
    • 78649981891 scopus 로고    scopus 로고
    • Nanotechnology in dental sciences: Moving towards a finer way of doing dentistry
    • V. Uskoković, and L.E. Bertassoni Nanotechnology in dental sciences: moving towards a finer way of doing dentistry Materials 3 2010 1674 1691
    • (2010) Materials , vol.3 , pp. 1674-1691
    • Uskoković, V.1    Bertassoni, L.E.2
  • 11
    • 79953253939 scopus 로고    scopus 로고
    • Limitations in bonding to dentin and experimental strategies to prevent bond degradation
    • Y. Liu, L. Tjaderhane, L. Breschi, A. Mazzoni, N. Li, and J. Mao Limitations in bonding to dentin and experimental strategies to prevent bond degradation J Dent Res 90 2011 953 968
    • (2011) J Dent Res , vol.90 , pp. 953-968
    • Liu, Y.1    Tjaderhane, L.2    Breschi, L.3    Mazzoni, A.4    Li, N.5    Mao, J.6
  • 12
    • 0031267556 scopus 로고    scopus 로고
    • The dentin substrate: Structure and properties related to bonding
    • G.W. Marshall, S.J. Marshall, J.H. Kinney, and M. Balooch The dentin substrate: structure and properties related to bonding J Dent 25 1997 441 458
    • (1997) J Dent , vol.25 , pp. 441-458
    • Marshall, G.W.1    Marshall, S.J.2    Kinney, J.H.3    Balooch, M.4
  • 13
    • 84855238638 scopus 로고    scopus 로고
    • Insights into the structure and composition of the peritubular dentin organic matrix and the lamina limitans
    • L.E. Bertassoni, K. Stankoska, and M.V. Swain Insights into the structure and composition of the peritubular dentin organic matrix and the lamina limitans Micron 43 2012 229 236
    • (2012) Micron , vol.43 , pp. 229-236
    • Bertassoni, L.E.1    Stankoska, K.2    Swain, M.V.3
  • 14
    • 0015805342 scopus 로고
    • Structure and function of bone collagen fibrils
    • E.P. Katz, and S.T. Li Structure and function of bone collagen fibrils J Mol Biol 80 1973 1 15
    • (1973) J Mol Biol , vol.80 , pp. 1-15
    • Katz, E.P.1    Li, S.T.2
  • 16
    • 0030427960 scopus 로고    scopus 로고
    • Mineral characterization in calcifying tissues: Atomic, molecular and macromolecular perspectives
    • W.J. Landis Mineral characterization in calcifying tissues: atomic, molecular and macromolecular perspectives Connect Tissue Res 34 1996 239 246
    • (1996) Connect Tissue Res , vol.34 , pp. 239-246
    • Landis, W.J.1
  • 17
    • 44549083018 scopus 로고    scopus 로고
    • Mechanical properties of mineralized collagen fibrils as influenced by demineralization
    • M. Balooch, S. Habelitz, J.H. Kinney, S.J. Marshall, and G.W. Marshall Mechanical properties of mineralized collagen fibrils as influenced by demineralization J Struct Biol 162 2008 404 410
    • (2008) J Struct Biol , vol.162 , pp. 404-410
    • Balooch, M.1    Habelitz, S.2    Kinney, J.H.3    Marshall, S.J.4    Marshall, G.W.5
  • 18
    • 0030199347 scopus 로고    scopus 로고
    • Mineralization of collagen may occur on fibril surfaces: Evidence from conventional and high-voltage electron microscopy and three-dimensional imaging
    • W.J. Landis, K.J. Hodgens, M.J. Song, J. Arena, S. Kiyonaga, and M. Marko Mineralization of collagen may occur on fibril surfaces: evidence from conventional and high-voltage electron microscopy and three-dimensional imaging J Struct Biol 117 1996 24 35
    • (1996) J Struct Biol , vol.117 , pp. 24-35
    • Landis, W.J.1    Hodgens, K.J.2    Song, M.J.3    Arena, J.4    Kiyonaga, S.5    Marko, M.6
  • 19
    • 0026043222 scopus 로고
    • Total etch-the rational dentin bonding protocol
    • R.L. Bertolotti Total etch-the rational dentin bonding protocol J Esthet Dent 3 1991 1 6
    • (1991) J Esthet Dent , vol.3 , pp. 1-6
    • Bertolotti, R.L.1
  • 20
    • 0030178905 scopus 로고    scopus 로고
    • Morphological field emission-SEM study of the effect of six phosphoric acid etching agents on human dentin
    • J. Perdigao, P. Lambrechts, B. van Meerbeek, A.R. Tome, G. Vanherle, and A.B. Lopes Morphological field emission-SEM study of the effect of six phosphoric acid etching agents on human dentin Dent Mater 12 1996 262 271
    • (1996) Dent Mater , vol.12 , pp. 262-271
    • Perdigao, J.1    Lambrechts, P.2    Van Meerbeek, B.3    Tome, A.R.4    Vanherle, G.5    Lopes, A.B.6
  • 21
    • 0020137778 scopus 로고
    • The promotion of adhesion by the infiltration of monomers into tooth substrates
    • N. Nakabayashi, K. Kojima, and E. Masuhara The promotion of adhesion by the infiltration of monomers into tooth substrates J Biomed Mater Res 16 1982 265 273
    • (1982) J Biomed Mater Res , vol.16 , pp. 265-273
    • Nakabayashi, N.1    Kojima, K.2    Masuhara, E.3
  • 22
    • 0028398530 scopus 로고
    • Microporous dentin zone beneath resin-impregnated layer
    • H. Sano, T. Shono, T. Takatsu, and H. Hosoda Microporous dentin zone beneath resin-impregnated layer Oper Dent 19 1994 59 64
    • (1994) Oper Dent , vol.19 , pp. 59-64
    • Sano, H.1    Shono, T.2    Takatsu, T.3    Hosoda, H.4
  • 23
    • 0027546912 scopus 로고
    • Comparative SEM and TEM examination of the ultrastructure of the resin-dentin interdiffusion zone
    • B. Van Meerbeek, A. Dhem, M. Goret-Nicaise, M. Braem, P. Lambrechts, and G. VanHerle Comparative SEM and TEM examination of the ultrastructure of the resin-dentin interdiffusion zone J Dent Res 72 1993 495 501
    • (1993) J Dent Res , vol.72 , pp. 495-501
    • Van Meerbeek, B.1    Dhem, A.2    Goret-Nicaise, M.3    Braem, M.4    Lambrechts, P.5    Vanherle, G.6
  • 24
    • 0038122968 scopus 로고    scopus 로고
    • In vitro degradation of resin-dentin bonds analyzed by microtensile bond test, scanning and transmission electron microscopy
    • M. Hashimoto, H. Ohno, H. Sano, M. Kaga, and H. Oguchi In vitro degradation of resin-dentin bonds analyzed by microtensile bond test, scanning and transmission electron microscopy Biomaterials 24 2003 3795 3803
    • (2003) Biomaterials , vol.24 , pp. 3795-3803
    • Hashimoto, M.1    Ohno, H.2    Sano, H.3    Kaga, M.4    Oguchi, H.5
  • 25
    • 33644976505 scopus 로고    scopus 로고
    • Microtensile testing, nanoleakage, and biodegradation of resin-dentin bonds
    • H. Sano Microtensile testing, nanoleakage, and biodegradation of resin-dentin bonds J Dent Res 85 2006 11 14
    • (2006) J Dent Res , vol.85 , pp. 11-14
    • Sano, H.1
  • 28
    • 0027425120 scopus 로고
    • Dentine proteoglycans: Composition, ultrastructure and functions
    • M. Goldberg, and M. Takagi Dentine proteoglycans: composition, ultrastructure and functions Histochem J 25 1993 781 806
    • (1993) Histochem J , vol.25 , pp. 781-806
    • Goldberg, M.1    Takagi, M.2
  • 29
    • 0024080689 scopus 로고
    • Quantitative assessment of collagen crosslinks in dissected predentin and dentin
    • A. Linde, and S.P. Robins Quantitative assessment of collagen crosslinks in dissected predentin and dentin Coll Relat Res 8 1988 443 450
    • (1988) Coll Relat Res , vol.8 , pp. 443-450
    • Linde, A.1    Robins, S.P.2
  • 30
    • 0025884785 scopus 로고
    • The role of extracellular matrix components in dentin mineralization
    • A.L. Boskey The role of extracellular matrix components in dentin mineralization Crit Rev Oral Biol Med 2 1991 369 387
    • (1991) Crit Rev Oral Biol Med , vol.2 , pp. 369-387
    • Boskey, A.L.1
  • 31
    • 0034915508 scopus 로고    scopus 로고
    • Collagen orientation and crystallite size in human dentin: A small angle X-ray scattering study
    • J.H. Kinney, J.A. Pople, G.W. Marshall, and S.J. Marshall Collagen orientation and crystallite size in human dentin: a small angle X-ray scattering study Calcif Tissue Int 69 2001 31 37
    • (2001) Calcif Tissue Int , vol.69 , pp. 31-37
    • Kinney, J.H.1    Pople, J.A.2    Marshall, G.W.3    Marshall, S.J.4
  • 32
    • 0027523135 scopus 로고
    • Scanning electron microscopy of type i collagen at the dentin-enamel junction of human teeth
    • C.P. Lin, W.H. Douglas, and S.L. Erlandsen Scanning electron microscopy of type I collagen at the dentin-enamel junction of human teeth J Histochem Cytochem 41 1993 381 388
    • (1993) J Histochem Cytochem , vol.41 , pp. 381-388
    • Lin, C.P.1    Douglas, W.H.2    Erlandsen, S.L.3
  • 33
    • 0033201994 scopus 로고    scopus 로고
    • An ultra-morphological characterization of collagen-depleted etched dentin
    • J. Perdigao, J.Y. Thompson, M. Toledano, and R. Osorio An ultra-morphological characterization of collagen-depleted etched dentin Am J Dent 12 1999 250 255
    • (1999) Am J Dent , vol.12 , pp. 250-255
    • Perdigao, J.1    Thompson, J.Y.2    Toledano, M.3    Osorio, R.4
  • 36
    • 28544440090 scopus 로고    scopus 로고
    • Ultrastructural examination of dentin using focused ion-beam cross-sectioning and transmission electron microscopy
    • R.K. Nalla, A.E. Porter, C. Daraio, A.M. Minor, V. Radmilovic, and E.A. Stach Ultrastructural examination of dentin using focused ion-beam cross-sectioning and transmission electron microscopy Micron 36 2005 672 680
    • (2005) Micron , vol.36 , pp. 672-680
    • Nalla, R.K.1    Porter, A.E.2    Daraio, C.3    Minor, A.M.4    Radmilovic, V.5    Stach, E.A.6
  • 37
    • 0036427708 scopus 로고    scopus 로고
    • In situ atomic force microscopy of partially demineralized human dentin collagen fibrils
    • S. Habelitz, M. Balooch, S.J. Marshall, G. Balooch, and G.W. Marshall In situ atomic force microscopy of partially demineralized human dentin collagen fibrils J Struct Biol 138 2002 227 236
    • (2002) J Struct Biol , vol.138 , pp. 227-236
    • Habelitz, S.1    Balooch, M.2    Marshall, S.J.3    Balooch, G.4    Marshall, G.W.5
  • 40
    • 78649298159 scopus 로고    scopus 로고
    • Evaluation of surface structural and mechanical changes following remineralization of dentin
    • L.E. Bertassoni, S. Habelitz, M. Pugach, P.C. Soares, S.J. Marshall, and G.W. Marshall Evaluation of surface structural and mechanical changes following remineralization of dentin Scanning 32 2010 312 319
    • (2010) Scanning , vol.32 , pp. 312-319
    • Bertassoni, L.E.1    Habelitz, S.2    Pugach, M.3    Soares, P.C.4    Marshall, S.J.5    Marshall, G.W.6
  • 41
    • 0031240103 scopus 로고    scopus 로고
    • Interfacial micromorphology and shear bond strength of single-bottle primer/adhesives
    • M.A. Vargas, D.S. Cobb, and G.E. Denehy Interfacial micromorphology and shear bond strength of single-bottle primer/adhesives Dent Mater 13 1997 316 324
    • (1997) Dent Mater , vol.13 , pp. 316-324
    • Vargas, M.A.1    Cobb, D.S.2    Denehy, G.E.3
  • 42
    • 0017070551 scopus 로고
    • Scanning electron microscopic investigation of human dentinal tubules
    • R. Garberoglio, and M. Brannstrom Scanning electron microscopic investigation of human dentinal tubules Arch Oral Biol 21 1976 355 362
    • (1976) Arch Oral Biol , vol.21 , pp. 355-362
    • Garberoglio, R.1    Brannstrom, M.2
  • 43
    • 0026290459 scopus 로고
    • Clinical correlations of dentin structure and function
    • D.H. Pashley Clinical correlations of dentin structure and function J Prosthet Dent 66 1991 777 781
    • (1991) J Prosthet Dent , vol.66 , pp. 777-781
    • Pashley, D.H.1
  • 46
    • 78650748366 scopus 로고    scopus 로고
    • Molecular and structural mapping of collagen fibril interactions
    • JP. Orgel, JD. San Antonio, and O. Antipova Molecular and structural mapping of collagen fibril interactions Connect Tissue Res 52 2011 2 17
    • (2011) Connect Tissue Res , vol.52 , pp. 2-17
    • Orgel, J.P.1    San Antonio, J.D.2    Antipova, O.3
  • 47
    • 78650733361 scopus 로고    scopus 로고
    • Collagen fibril surface displays a constellation of sites capable of promoting fibril assembly, stability, and hemostasis
    • JP. Orgel, O. Antipova, I. Sagi, A. Bitler, D. Qiu, and R. Wang Collagen fibril surface displays a constellation of sites capable of promoting fibril assembly, stability, and hemostasis Connect Tissue Res 52 2011 18 24
    • (2011) Connect Tissue Res , vol.52 , pp. 18-24
    • Orgel, J.P.1    Antipova, O.2    Sagi, I.3    Bitler, A.4    Qiu, D.5    Wang, R.6
  • 48
    • 70349330118 scopus 로고    scopus 로고
    • Decorin core protein (decoron) shape complements collagen fibril surface structure and mediates its binding
    • J.P. Orgel, A. Eid, O. Antipova, J. Bella, and J.E. Scott Decorin core protein (decoron) shape complements collagen fibril surface structure and mediates its binding PLoS One 4 2009 e7028
    • (2009) PLoS One , vol.4 , pp. 7028
    • Orgel, J.P.1    Eid, A.2    Antipova, O.3    Bella, J.4    Scott, J.E.5
  • 49
    • 42949135530 scopus 로고    scopus 로고
    • Collagen fibril architecture, domain organization, and triple-helical conformation govern its proteolysis
    • S. Perumal, O. Antipova, and J.P. Orgel Collagen fibril architecture, domain organization, and triple-helical conformation govern its proteolysis Proc Natl Acad Sci USA 105 2008 2824 2829
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 2824-2829
    • Perumal, S.1    Antipova, O.2    Orgel, J.P.3
  • 52
    • 0034651554 scopus 로고    scopus 로고
    • The in situ conformation and axial location of the intermolecular cross-linked non-helical telopeptides of type i collagen
    • J.P. Orgel, T.J. Wess, and A. Miller The in situ conformation and axial location of the intermolecular cross-linked non-helical telopeptides of type I collagen Structure 8 2000 137 142
    • (2000) Structure , vol.8 , pp. 137-142
    • Orgel, J.P.1    Wess, T.J.2    Miller, A.3
  • 53
    • 0035197704 scopus 로고    scopus 로고
    • Tapping-mode atomic force microscopy in fluid of hydrated extracellular matrix
    • M. Raspanti, T. Congiu, and S. Guizzardi Tapping-mode atomic force microscopy in fluid of hydrated extracellular matrix Matrix Biol 20 2001 601 604
    • (2001) Matrix Biol , vol.20 , pp. 601-604
    • Raspanti, M.1    Congiu, T.2    Guizzardi, S.3
  • 54
    • 0024814789 scopus 로고
    • Different architectures of the collagen fibril: Morphological aspects and functional implications
    • M. Raspanti, V. Ottani, and A. Ruggeri Different architectures of the collagen fibril: morphological aspects and functional implications Int J Biol Macromol 11 1989 367 371
    • (1989) Int J Biol Macromol , vol.11 , pp. 367-371
    • Raspanti, M.1    Ottani, V.2    Ruggeri, A.3
  • 55
    • 0019020571 scopus 로고
    • Model of sorption of simple molecules in polymers
    • Pace RJ, Datyner A. Model of sorption of simple molecules in polymers. J Polym Sci Polym Phys 1980;18.
    • (1980) J Polym Sci Polym Phys , pp. 18
    • Pace, R.J.1    Datyner, A.2
  • 56
    • 0035434592 scopus 로고    scopus 로고
    • Nanoleakage at the composite-dentin interface. A review
    • T. Pioch, H.J. Staehle, H. Duschner, and F. Garcia-Godoy Nanoleakage at the composite-dentin interface. a review Am J Dent 14 2001 252 258
    • (2001) Am J Dent , vol.14 , pp. 252-258
    • Pioch, T.1    Staehle, H.J.2    Duschner, H.3    Garcia-Godoy, F.4
  • 57
    • 0027996196 scopus 로고
    • Crystal and molecular structure of a collagen-like peptide at 1.9 Å resolution
    • Bella J, Eaton M, Brodsky B, Berman HM. Crystal and molecular structure of a collagen-like peptide at 1.9 Å resolution. Science 1994;266:75-81.
    • (1994) Science , vol.266 , pp. 75-81
    • Bella, J.1    Eaton, M.2    Brodsky, B.3    Berman, H.M.4
  • 58
    • 0001113489 scopus 로고
    • A subunit model for the tropocollagenmacromolecule
    • Petruska JA, Hodge AJ. A subunit model for the tropocollagenmacromolecule. Proc Natl Acad Sci USA 1964;51:871-6.
    • (1964) Proc Natl Acad Sci USA , vol.51 , pp. 871-876
    • Petruska, J.A.1    Hodge, A.J.2
  • 59
    • 0014412958 scopus 로고
    • Molecular pattern in native collagen
    • J.W. Smith Molecular pattern in native collagen Nature 219 1968 157 158
    • (1968) Nature , vol.219 , pp. 157-158
    • Smith, J.W.1
  • 61
    • 0035218932 scopus 로고    scopus 로고
    • Collagen structure and functional implications
    • V. Ottani, M. Raspanti, and A. Ruggeri Collagen structure and functional implications Micron 32 2001 251 260
    • (2001) Micron , vol.32 , pp. 251-260
    • Ottani, V.1    Raspanti, M.2    Ruggeri, A.3
  • 62
    • 78650748366 scopus 로고    scopus 로고
    • Molecular and structural mapping of collagen fibril interactions
    • J.P. Orgel, J.D. San Antonio, and O. Antipova Molecular and structural mapping of collagen fibril interactions Connect Tissue Res 52 2011 2 17
    • (2011) Connect Tissue Res , vol.52 , pp. 2-17
    • Orgel, J.P.1    San Antonio, J.D.2    Antipova, O.3
  • 63
    • 0025214344 scopus 로고
    • Proteoglycan: Collagen interactions and subfibrillar structure in collagen fibrils. Implications in the development and ageing of connective tissues
    • J.E. Scott Proteoglycan: collagen interactions and subfibrillar structure in collagen fibrils. Implications in the development and ageing of connective tissues J Anat 169 1990 23 35
    • (1990) J Anat , vol.169 , pp. 23-35
    • Scott, J.E.1
  • 64
    • 0033910740 scopus 로고    scopus 로고
    • The subfibrillar arrangement of corneal and scleral collagen fibrils as revealed by scanning electron and atomic force microscopy
    • S. Yamamoto, H. Hashizume, J. Hitomi, M. Shigeno, S. Sawaguchi, and H. Abe The subfibrillar arrangement of corneal and scleral collagen fibrils as revealed by scanning electron and atomic force microscopy Arch Histol Cytol 63 2000 127 135
    • (2000) Arch Histol Cytol , vol.63 , pp. 127-135
    • Yamamoto, S.1    Hashizume, H.2    Hitomi, J.3    Shigeno, M.4    Sawaguchi, S.5    Abe, H.6
  • 65
    • 34547132546 scopus 로고    scopus 로고
    • Collagen fibril structure is affected by collagen concentration and decorin
    • M. Raspanti, M. Viola, M. Sonaggere, M.E. Tira, and R. Tenni Collagen fibril structure is affected by collagen concentration and decorin Biomacromolecules 8 2007 2087 2091
    • (2007) Biomacromolecules , vol.8 , pp. 2087-2091
    • Raspanti, M.1    Viola, M.2    Sonaggere, M.3    Tira, M.E.4    Tenni, R.5
  • 66
    • 0018568324 scopus 로고
    • Type i collagen fibrillogenesis: Initiation via reversible linear and lateral growth steps
    • F.H. Silver, K.H. Langley, and R.L. Trelstad Type I collagen fibrillogenesis: initiation via reversible linear and lateral growth steps Biopolymers 18 1979 2523 2535
    • (1979) Biopolymers , vol.18 , pp. 2523-2535
    • Silver, F.H.1    Langley, K.H.2    Trelstad, R.L.3
  • 67
    • 77951231955 scopus 로고    scopus 로고
    • In situ D-periodic molecular structure of type II collagen
    • O. Antipova, and J.P. Orgel In situ D-periodic molecular structure of type II collagen J Biol Chem 285 2010 7087 7096
    • (2010) J Biol Chem , vol.285 , pp. 7087-7096
    • Antipova, O.1    Orgel, J.P.2
  • 68
    • 0018597290 scopus 로고
    • Quasi-hexagonal molecular packing in collagen fibrils
    • D.J. Hulmes, and A. Miller Quasi-hexagonal molecular packing in collagen fibrils Nature 282 1979 878 880
    • (1979) Nature , vol.282 , pp. 878-880
    • Hulmes, D.J.1    Miller, A.2
  • 69
    • 51049121850 scopus 로고    scopus 로고
    • Candidate cell and matrix interaction domains on the collagen fibril, the predominant protein of vertebrates
    • S.M. Sweeney, J.P. Orgel, A. Fertala, J.D. McAuliffe, K.R. Turner, and G.A. Di Lullo Candidate cell and matrix interaction domains on the collagen fibril, the predominant protein of vertebrates J Biol Chem 283 2008 21187 21197
    • (2008) J Biol Chem , vol.283 , pp. 21187-21197
    • Sweeney, S.M.1    Orgel, J.P.2    Fertala, A.3    McAuliffe, J.D.4    Turner, K.R.5    Di Lullo, G.A.6
  • 70
    • 36949016403 scopus 로고    scopus 로고
    • Type i collagen and collagen mimetics as angiogenesis promoting superpolymers
    • T. Twardowski, A. Fertala, J.P. Orgel, and J.D. San Antonio Type I collagen and collagen mimetics as angiogenesis promoting superpolymers Curr Pharm Des 13 2007 3608 3621
    • (2007) Curr Pharm des , vol.13 , pp. 3608-3621
    • Twardowski, T.1    Fertala, A.2    Orgel, J.P.3    San Antonio, J.D.4
  • 71
    • 0028910961 scopus 로고
    • Radial packing, order, and disorder in collagen fibrils
    • D.J. Hulmes, T.J. Wess, D.J. Prockop, and P. Fratzl Radial packing, order, and disorder in collagen fibrils Biophys J 68 1995 1661 1670
    • (1995) Biophys J , vol.68 , pp. 1661-1670
    • Hulmes, D.J.1    Wess, T.J.2    Prockop, D.J.3    Fratzl, P.4
  • 72
    • 0029645406 scopus 로고
    • Hydration structure of a collagen peptide
    • J. Bella, B. Brodsky, and H.M. Berman Hydration structure of a collagen peptide Structure 3 1995 893 906
    • (1995) Structure , vol.3 , pp. 893-906
    • Bella, J.1    Brodsky, B.2    Berman, H.M.3
  • 74
    • 84981666520 scopus 로고
    • Hydration structure of fibrous macromolecules
    • H.J.C. Berendsen, and C. Migchelsen Hydration structure of fibrous macromolecules Ann NY Acad Sci 125 1965 365 379
    • (1965) Ann NY Acad Sci , vol.125 , pp. 365-379
    • Berendsen, H.J.C.1    Migchelsen, C.2
  • 75
    • 0018394222 scopus 로고
    • The molecular details of collagen hydration
    • J.R. Grigera, and H.J.C. Berendsen The molecular details of collagen hydration Biopolymers 18 1979 47 57
    • (1979) Biopolymers , vol.18 , pp. 47-57
    • Grigera, J.R.1    Berendsen, H.J.C.2
  • 77
    • 0021380631 scopus 로고
    • Variation of longitudinal acoustic velocity at gigahertz frequencies with water content in rat-tail tendon fibers
    • S. Cusack, and S. Lees Variation of longitudinal acoustic velocity at gigahertz frequencies with water content in rat-tail tendon fibers Biopolymers 23 1984 337 351
    • (1984) Biopolymers , vol.23 , pp. 337-351
    • Cusack, S.1    Lees, S.2
  • 78
    • 0025022719 scopus 로고
    • Structure and dynamics of water in tendon from NMR relaxation measurements
    • S. Peto, P. Gillis, and V.P. Henri Structure and dynamics of water in tendon from NMR relaxation measurements Biophys J 57 1990 71 84
    • (1990) Biophys J , vol.57 , pp. 71-84
    • Peto, S.1    Gillis, P.2    Henri, V.P.3
  • 79
    • 0016264117 scopus 로고
    • The structure of water absorbed in collagen. I. The dielectric properties
    • C.A. Hoeve, and P.C. Lue The structure of water absorbed in collagen. I. The dielectric properties Biopolymers 13 1974 1661 1680
    • (1974) Biopolymers , vol.13 , pp. 1661-1680
    • Hoeve, C.A.1    Lue, P.C.2
  • 80
    • 32044441450 scopus 로고    scopus 로고
    • Hygroscopic and hydrolytic effects in dental polymer networks
    • J.L. Ferracane Hygroscopic and hydrolytic effects in dental polymer networks Dent Mater 22 2006 211 222
    • (2006) Dent Mater , vol.22 , pp. 211-222
    • Ferracane, J.L.1
  • 81
    • 25444484372 scopus 로고    scopus 로고
    • Bonding to dentin and enamel where does it stand in 2005?
    • G.J. Christensen Bonding to dentin and enamel where does it stand in 2005? J Am Dent Assoc 136 2005 1299 1302
    • (2005) J Am Dent Assoc , vol.136 , pp. 1299-1302
    • Christensen, G.J.1
  • 82
    • 0031112093 scopus 로고    scopus 로고
    • Resin composites in dentistry: The monomer systems
    • A. Peutzfeldt Resin composites in dentistry: the monomer systems Eur J Oral Sci 105 1997 97 116
    • (1997) Eur J Oral Sci , vol.105 , pp. 97-116
    • Peutzfeldt, A.1
  • 83
    • 0026245543 scopus 로고
    • NIR-spectroscopic investigation of water sorption characteristics of dental resins and composites
    • S. Venz, and B. Dickens NIR-spectroscopic investigation of water sorption characteristics of dental resins and composites J Biomed Mater Res 25 1991 1231 1248
    • (1991) J Biomed Mater Res , vol.25 , pp. 1231-1248
    • Venz, S.1    Dickens, B.2
  • 84
    • 0033278081 scopus 로고    scopus 로고
    • Biodegradation of commercial dental composites by cholesterol esterase
    • J.P. Santerre, L. Shajii, and H. Tsang Biodegradation of commercial dental composites by cholesterol esterase J Dent Res 78 1999 1459 1468
    • (1999) J Dent Res , vol.78 , pp. 1459-1468
    • Santerre, J.P.1    Shajii, L.2    Tsang, H.3
  • 85
    • 84989592217 scopus 로고
    • Enzymatic hydrolysis of (di)methacrylates and their polymers
    • E.C. Munksgaard, and M. Freund Enzymatic hydrolysis of (di)methacrylates and their polymers Scand J Dent Res 98 1990 261 267
    • (1990) Scand J Dent Res , vol.98 , pp. 261-267
    • Munksgaard, E.C.1    Freund, M.2
  • 86
    • 0027955525 scopus 로고
    • Effect of esterase on methacrylates and methacrylate polymers in an enzyme simulator for biodurability and biocompatibility testing
    • T.A. Bean, W.C. Zhuang, P.Y. Tong, J.D. Eick, and D.M. Yourtee Effect of esterase on methacrylates and methacrylate polymers in an enzyme simulator for biodurability and biocompatibility testing J Biomed Mater Res 28 1994 59 63
    • (1994) J Biomed Mater Res , vol.28 , pp. 59-63
    • Bean, T.A.1    Zhuang, W.C.2    Tong, P.Y.3    Eick, J.D.4    Yourtee, D.M.5
  • 87
    • 0035011396 scopus 로고    scopus 로고
    • Relation of dental composite formulations to their degradation and the release of hydrolyzed polymeric-resin-derived products
    • J.P. Santerre, L. Shajii, and B.W. Leung Relation of dental composite formulations to their degradation and the release of hydrolyzed polymeric-resin-derived products Crit Rev Oral Biol Med 12 2001 136 151
    • (2001) Crit Rev Oral Biol Med , vol.12 , pp. 136-151
    • Santerre, J.P.1    Shajii, L.2    Leung, B.W.3
  • 88
    • 1842780854 scopus 로고    scopus 로고
    • The influence of resin chemistry on a dental composite's biodegradation
    • Y. Finer, and J.P. Santerre The influence of resin chemistry on a dental composite's biodegradation J Biomed Mater Res A 69 2004 233 246
    • (2004) J Biomed Mater Res A , vol.69 , pp. 233-246
    • Finer, Y.1    Santerre, J.P.2
  • 89
    • 0033170814 scopus 로고    scopus 로고
    • The influence of oral bacteria on the surfaces of resin-based dental restorative materials-an in vitro study
    • B. Willershausen, A. Callaway, C.P. Ernst, and E. Stender The influence of oral bacteria on the surfaces of resin-based dental restorative materials-an in vitro study Int Dent J 49 1999 231 239
    • (1999) Int Dent J , vol.49 , pp. 231-239
    • Willershausen, B.1    Callaway, A.2    Ernst, C.P.3    Stender, E.4
  • 90
    • 0018449925 scopus 로고
    • Long term water sorption and solubility of composite filling materials
    • G.J. Pearson Long term water sorption and solubility of composite filling materials J Dent 7 1979 64 68
    • (1979) J Dent , vol.7 , pp. 64-68
    • Pearson, G.J.1
  • 92
    • 0022804472 scopus 로고
    • Water sorption and filler characteristics of composites for use in posterior teeth
    • H. Oysaed, and I.E. Ruyter Water sorption and filler characteristics of composites for use in posterior teeth J Dent Res 65 1986 1315 1318
    • (1986) J Dent Res , vol.65 , pp. 1315-1318
    • Oysaed, H.1    Ruyter, I.E.2
  • 93
    • 0035462096 scopus 로고    scopus 로고
    • Water sorption and mechanical behaviour of cosmetic direct restorative materials in artificial saliva
    • L. Musanje, M. Shu, and B.W. Darvell Water sorption and mechanical behaviour of cosmetic direct restorative materials in artificial saliva Dent Mater 17 2001 394 401
    • (2001) Dent Mater , vol.17 , pp. 394-401
    • Musanje, L.1    Shu, M.2    Darvell, B.W.3
  • 94
    • 0028472254 scopus 로고
    • Elution of leachable components from composites
    • J.L. Ferracane Elution of leachable components from composites J Oral Rehabil 21 1994 441 452
    • (1994) J Oral Rehabil , vol.21 , pp. 441-452
    • Ferracane, J.L.1
  • 95
    • 0016998052 scopus 로고
    • Diffusion of water in composite filling materials
    • M. Braden, E.E. Causton, and R.L. Clarke Diffusion of water in composite filling materials J Dent Res 55 1976 730 732
    • (1976) J Dent Res , vol.55 , pp. 730-732
    • Braden, M.1    Causton, E.E.2    Clarke, R.L.3
  • 96
    • 0038356543 scopus 로고    scopus 로고
    • On the surface elemental composition of non-corroded and corroded dental ceramic materials in vitro
    • P. Milleding, S. Karlsson, and L. Nyborg On the surface elemental composition of non-corroded and corroded dental ceramic materials in vitro J Mater Sci Mater Med 14 2003 557 566
    • (2003) J Mater Sci Mater Med , vol.14 , pp. 557-566
    • Milleding, P.1    Karlsson, S.2    Nyborg, L.3
  • 97
    • 3242872270 scopus 로고    scopus 로고
    • Water sorption and solubility of experimental dental composites
    • J.L. Ferracane Water sorption and solubility of experimental dental composites Polymer Preprints 38 1997 116 117
    • (1997) Polymer Preprints , vol.38 , pp. 116-117
    • Ferracane, J.L.1
  • 99
    • 76849103293 scopus 로고    scopus 로고
    • One-year stability of resin-dentin bonds created with a hydrophobic ethanol-wet bonding technique
    • F.T. Sadek, C.S. Castellan, R.R. Braga, S. Mai, L. Tjaderhane, and D.H. Pashley One-year stability of resin-dentin bonds created with a hydrophobic ethanol-wet bonding technique Dent Mater 26 2010 380 386
    • (2010) Dent Mater , vol.26 , pp. 380-386
    • Sadek, F.T.1    Castellan, C.S.2    Braga, R.R.3    Mai, S.4    Tjaderhane, L.5    Pashley, D.H.6
  • 100
    • 0037259123 scopus 로고    scopus 로고
    • Technique sensitivity in bonding to vital, acid-etched dentin
    • M. Ferrari, and F.R. Tay Technique sensitivity in bonding to vital, acid-etched dentin Oper Dent 28 2003 3 8
    • (2003) Oper Dent , vol.28 , pp. 3-8
    • Ferrari, M.1    Tay, F.R.2
  • 104
    • 0037693895 scopus 로고    scopus 로고
    • Matrix metalloproteinases and tissue inhibitors of metalloproteinases: Structure, function, and biochemistry
    • R. Visse, and H. Nagase Matrix metalloproteinases and tissue inhibitors of metalloproteinases: structure, function, and biochemistry Circ Res 92 2003 827 839
    • (2003) Circ Res , vol.92 , pp. 827-839
    • Visse, R.1    Nagase, H.2
  • 105
    • 0032223705 scopus 로고    scopus 로고
    • The activation and function of host matrix metalloproteinases in dentin matrix breakdown in caries lesions
    • L. Tjaderhane, H. Larjava, T. Sorsa, V.J. Uitto, M. Larmas, and T. Salo The activation and function of host matrix metalloproteinases in dentin matrix breakdown in caries lesions J Dent Res 77 1998 1622 1629
    • (1998) J Dent Res , vol.77 , pp. 1622-1629
    • Tjaderhane, L.1    Larjava, H.2    Sorsa, T.3    Uitto, V.J.4    Larmas, M.5    Salo, T.6
  • 109
    • 28444435436 scopus 로고    scopus 로고
    • Microtensile dentin bond strength of self-etching resins: Effect of a hydrophobic layer
    • W.W. Brackett, S. Ito, F.R. Tay, L.D. Haisch, and D.H. Pashley Microtensile dentin bond strength of self-etching resins: effect of a hydrophobic layer Oper Dent 30 2005 733 738
    • (2005) Oper Dent , vol.30 , pp. 733-738
    • Brackett, W.W.1    Ito, S.2    Tay, F.R.3    Haisch, L.D.4    Pashley, D.H.5
  • 111
    • 12344299287 scopus 로고    scopus 로고
    • Resin-dentin interfacial ultrastructure and microtensile dentin bond strength after five-year water storage
    • S.R. Armstrong, M.A. Vargas, I. Chung, D.H. Pashley, J.A. Campbell, and J.E. Laffoon Resin-dentin interfacial ultrastructure and microtensile dentin bond strength after five-year water storage Oper Dent 29 2004 705 712
    • (2004) Oper Dent , vol.29 , pp. 705-712
    • Armstrong, S.R.1    Vargas, M.A.2    Chung, I.3    Pashley, D.H.4    Campbell, J.A.5    Laffoon, J.E.6
  • 112
    • 0033393101 scopus 로고    scopus 로고
    • Studies of adhesion-dependent platelet activation: Distinct roles for different participating receptors can be dissociated by proteolysis of collagen
    • P. Siljander, and R. Lassila Studies of adhesion-dependent platelet activation: distinct roles for different participating receptors can be dissociated by proteolysis of collagen Arterioscler Thromb Vasc Biol 19 1999 3033 3043
    • (1999) Arterioscler Thromb Vasc Biol , vol.19 , pp. 3033-3043
    • Siljander, P.1    Lassila, R.2
  • 113
    • 33746593689 scopus 로고    scopus 로고
    • Migration of tumor cells in 3D matrices is governed by matrix stiffness along with cell-matrix adhesion and proteolysis
    • M.H. Zaman, L.M. Trapani, A.L. Sieminski, D. Mackellar, H. Gong, and R.D. Kamm Migration of tumor cells in 3D matrices is governed by matrix stiffness along with cell-matrix adhesion and proteolysis Proc Natl Acad Sci USA 103 2006 10889 10894
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 10889-10894
    • Zaman, M.H.1    Trapani, L.M.2    Sieminski, A.L.3    MacKellar, D.4    Gong, H.5    Kamm, R.D.6
  • 115
    • 0036300984 scopus 로고    scopus 로고
    • Localized unfolding of collagen explains collagenase cleavage near imino-poor sites
    • C.M. Stultz Localized unfolding of collagen explains collagenase cleavage near imino-poor sites J Mol Biol 319 2002 997 1003
    • (2002) J Mol Biol , vol.319 , pp. 997-1003
    • Stultz, C.M.1
  • 116
    • 81755174318 scopus 로고    scopus 로고
    • Matrix metalloproteinase-2 expression induced by two different adhesive systems on human pulp fibroblasts
    • G. Orsini, A. Mazzoni, M. Orciani, A. Putignano, M. Procaccini, and M. Falconi Matrix metalloproteinase-2 expression induced by two different adhesive systems on human pulp fibroblasts J Endod 37 2011 1663 1667
    • (2011) J Endod , vol.37 , pp. 1663-1667
    • Orsini, G.1    Mazzoni, A.2    Orciani, M.3    Putignano, A.4    Procaccini, M.5    Falconi, M.6
  • 117
    • 0025891309 scopus 로고
    • Identification of an abundant latent 94-kDa gelatin-degrading metalloprotease in human saliva which is activated by acid exposure: Implications for a role in digestion of collagenous proteins
    • G.E. Davis Identification of an abundant latent 94-kDa gelatin-degrading metalloprotease in human saliva which is activated by acid exposure: implications for a role in digestion of collagenous proteins Arch Biochem Biophys 286 1991 551 554
    • (1991) Arch Biochem Biophys , vol.286 , pp. 551-554
    • Davis, G.E.1
  • 121
    • 70450186303 scopus 로고    scopus 로고
    • Effects of chemical cross-linkers on caries-affected dentin bonding
    • G.V. Macedo, M. Yamauchi, and A.K. Bedran-Russo Effects of chemical cross-linkers on caries-affected dentin bonding J Dent Res 88 2009 1096 1100
    • (2009) J Dent Res , vol.88 , pp. 1096-1100
    • MacEdo, G.V.1    Yamauchi, M.2    Bedran-Russo, A.K.3
  • 122
    • 70349510610 scopus 로고    scopus 로고
    • Mechanical properties of tannic-acid-treated dentin matrix
    • A.K. Bedran-Russo, K.J. Yoo, K.C. Ema, and D.H. Pashley Mechanical properties of tannic-acid-treated dentin matrix J Dent Res 88 2009 807 811
    • (2009) J Dent Res , vol.88 , pp. 807-811
    • Bedran-Russo, A.K.1    Yoo, K.J.2    Ema, K.C.3    Pashley, D.H.4
  • 124
    • 77956172795 scopus 로고    scopus 로고
    • Mechanical characterization of proanthocyanidin-dentin matrix interaction
    • C.S. Castellan, P.N. Pereira, R.H. Grande, and A.K. Bedran-Russo Mechanical characterization of proanthocyanidin-dentin matrix interaction Dent Mater 26 2010 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
  • 128
    • 33747357877 scopus 로고    scopus 로고
    • Reactivation of inactivated endogenous proteolytic activities in phosphoric acid-etched dentine by etch-and-rinse adhesives
    • A. Mazzoni, D.H. Pashley, Y. Nishitani, L. Breschi, F. Mannello, and L. Tjaderhane Reactivation of inactivated endogenous proteolytic activities in phosphoric acid-etched dentine by etch-and-rinse adhesives Biomaterials 27 2006 4470 4476
    • (2006) Biomaterials , vol.27 , pp. 4470-4476
    • Mazzoni, A.1    Pashley, D.H.2    Nishitani, Y.3    Breschi, L.4    Mannello, F.5    Tjaderhane, L.6
  • 129
    • 68149108542 scopus 로고    scopus 로고
    • In vivo chlorhexidine stabilization of hybrid layers of an acetone-based dentin adhesive
    • M.G. Brackett, F.R. Tay, W.W. Brackett, A. Dib, F.A. Dipp, and S. Mai In vivo chlorhexidine stabilization of hybrid layers of an acetone-based dentin adhesive Oper Dent 34 2009 379 383
    • (2009) Oper Dent , vol.34 , pp. 379-383
    • Brackett, M.G.1    Tay, F.R.2    Brackett, W.W.3    Dib, A.4    Dipp, F.A.5    Mai, S.6
  • 131
    • 0031826531 scopus 로고    scopus 로고
    • The structure of interfibrillar proteoglycan bridges (shape modules) in extracellular matrix of fibrous connective tissues and their stability in various chemical environments
    • J.E. Scott, and A.M. Thomlinson The structure of interfibrillar proteoglycan bridges (shape modules) in extracellular matrix of fibrous connective tissues and their stability in various chemical environments J Anat 192 3 1998 391 405
    • (1998) J Anat , vol.192 , Issue.3 , pp. 391-405
    • Scott, J.E.1    Thomlinson, A.M.2
  • 133
    • 0026652062 scopus 로고
    • Supramolecular organization of extracellular matrix glycosaminoglycans, in vitro and in the tissues
    • J.E. Scott Supramolecular organization of extracellular matrix glycosaminoglycans, in vitro and in the tissues Faseb J 6 1992 2639 2645
    • (1992) Faseb J , vol.6 , pp. 2639-2645
    • Scott, J.E.1
  • 134
    • 0346242689 scopus 로고    scopus 로고
    • Elasticity in extracellular matrix 'shape modules' of tendon, cartilage, etc. A sliding proteoglycan-filament model
    • J.E. Scott Elasticity in extracellular matrix 'shape modules' of tendon, cartilage, etc. A sliding proteoglycan-filament model J Physiol 553 2003 335 343
    • (2003) J Physiol , vol.553 , pp. 335-343
    • Scott, J.E.1
  • 135
    • 52449100731 scopus 로고    scopus 로고
    • Cartilage is held together by elastic glycan strings. Physiological and pathological implications
    • J.E. Scott Cartilage is held together by elastic glycan strings. Physiological and pathological implications Biorheology 45 2008 209 217
    • (2008) Biorheology , vol.45 , pp. 209-217
    • Scott, J.E.1
  • 139
  • 140
    • 51549116865 scopus 로고    scopus 로고
    • Glycosaminoglycans show a specific periodic interaction with type i collagen fibrils
    • M. Raspanti, M. Viola, A. Forlino, R. Tenni, C. Gruppi, and M.E. Tira Glycosaminoglycans show a specific periodic interaction with type I collagen fibrils J Struct Biol 164 2008 134 139
    • (2008) J Struct Biol , vol.164 , pp. 134-139
    • Raspanti, M.1    Viola, M.2    Forlino, A.3    Tenni, R.4    Gruppi, C.5    Tira, M.E.6
  • 144
    • 79851488199 scopus 로고    scopus 로고
    • Hierarchical structure and nanomechanics of collagen microfibrils from the atomistic scale up
    • A. Gautieri, S. Vesentini, A. Redaelli, and M.J. Buehler Hierarchical structure and nanomechanics of collagen microfibrils from the atomistic scale up Nano Lett 11 2010 757 766
    • (2010) Nano Lett , vol.11 , pp. 757-766
    • Gautieri, A.1    Vesentini, S.2    Redaelli, A.3    Buehler, M.J.4
  • 145
    • 8144221077 scopus 로고    scopus 로고
    • Crystal structure of the dimeric protein core of decorin, the archetypal small leucine-rich repeat proteoglycan
    • P.G. Scott, P.A. McEwan, C.M. Dodd, E.M. Bergmann, P.N. Bishop, and J. Bella Crystal structure of the dimeric protein core of decorin, the archetypal small leucine-rich repeat proteoglycan Proc Natl Acad Sci USA 101 2004 15633 15638
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 15633-15638
    • Scott, P.G.1    McEwan, P.A.2    Dodd, C.M.3    Bergmann, E.M.4    Bishop, P.N.5    Bella, J.6
  • 146
    • 0018132542 scopus 로고
    • Chondroitin 4-sulfate: The structure of a sulfated glycosaminoglycan
    • W.T. Winter, S. Arnott, D.H. Isaac, and E.D. Atkins Chondroitin 4-sulfate: the structure of a sulfated glycosaminoglycan J Mol Biol 125 1978 1 19
    • (1978) J Mol Biol , vol.125 , pp. 1-19
    • Winter, W.T.1    Arnott, S.2    Isaac, D.H.3    Atkins, E.D.4
  • 147
    • 58949085391 scopus 로고    scopus 로고
    • Self-etching increases matrix metalloproteinase expression in the dentin-pulp complex
    • N. Lehmann, R. Debret, A. Romeas, H. Magloire, M. Degrange, and F. Bleicher Self-etching increases matrix metalloproteinase expression in the dentin-pulp complex J Dent Res 88 2009 77 82
    • (2009) J Dent Res , vol.88 , pp. 77-82
    • Lehmann, N.1    Debret, R.2    Romeas, A.3    Magloire, H.4    Degrange, M.5    Bleicher, F.6
  • 148
    • 79959379976 scopus 로고    scopus 로고
    • MMP-2 assay within the hybrid layer created by a two-step etch-and-rinse adhesive: Biochemical and immunohistochemical analysis
    • A. Mazzoni, M. Carrilho, V. Papa, L. Tjaderhane, P. Gobbi, and C. Nucci MMP-2 assay within the hybrid layer created by a two-step etch-and-rinse adhesive: biochemical and immunohistochemical analysis J Dent 39 2011 470 477
    • (2011) J Dent , vol.39 , pp. 470-477
    • Mazzoni, A.1    Carrilho, M.2    Papa, V.3    Tjaderhane, L.4    Gobbi, P.5    Nucci, C.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.