메뉴 건너뛰기




Volumn 39, Issue , 2013, Pages 108-117

A structural and functional model for human bone sialoprotein

Author keywords

Biomineralization; Hydroxyapatite; Molecular modelling; Osteogenesis; SIBLING proteins

Indexed keywords

3D STRUCTURAL MODEL; 3D STRUCTURE; ACIDIC SURFACE; ESSENTIAL COMPONENT; EXPERIMENTAL CHARACTERIZATION; EXTRACELLULAR MATRICES; FUNCTIONAL MODEL; GLYCANS; HUMAN BONES; HYDROXYAPATITE CRYSTALS; IMPLICIT SOLVENT MODEL; LITERATURE DATA; MODELLING TECHNIQUES; O-LINKED; OSTEOGENESIS; POST-TRANSLATIONAL MODIFICATIONS; QUANTUM CALCULATION; STRONG BINDING; WEAK BINDING;

EID: 84871390719     PISSN: 10933263     EISSN: 18734243     Source Type: Journal    
DOI: 10.1016/j.jmgm.2012.10.007     Document Type: Article
Times cited : (30)

References (44)
  • 1
    • 57349158632 scopus 로고    scopus 로고
    • Phosphorylated proteins and control over apatite nucleation, crystal growth, and inhibition
    • A. George, and A. Veis Phosphorylated proteins and control over apatite nucleation, crystal growth, and inhibition Chemical Reviews 108 2008 4670 4693
    • (2008) Chemical Reviews , vol.108 , pp. 4670-4693
    • George, A.1    Veis, A.2
  • 2
    • 0035980257 scopus 로고    scopus 로고
    • Posttranslational modifications to human bone sialoprotein determined by mass spectrometry
    • J. Zaia, R. Boynton, D. Heinegård, and F. Barry Posttranslational modifications to human bone sialoprotein determined by mass spectrometry Biochemistry 40 2001 12983 12991
    • (2001) Biochemistry , vol.40 , pp. 12983-12991
    • Zaia, J.1    Boynton, R.2    Heinegård, D.3    Barry, F.4
  • 3
    • 0035965291 scopus 로고    scopus 로고
    • Structural characterization of human recombinant and bone-derived bone sialoprotein. Functional implications for cell attachment and hydroxyapatite binding
    • M. Wuttke, S. Müller, D.P. Nitsche, M. Paulsson, F.-G. Hanisch, and P. Maurer Structural characterization of human recombinant and bone-derived bone sialoprotein. Functional implications for cell attachment and hydroxyapatite binding Journal of Biological Chemistry 276 2001 36839 36848
    • (2001) Journal of Biological Chemistry , vol.276 , pp. 36839-36848
    • Wuttke, M.1    Müller, S.2    Nitsche, D.P.3    Paulsson, M.4    Hanisch, F.-G.5    Maurer, P.6
  • 5
    • 0030741640 scopus 로고    scopus 로고
    • Characterization of native and recombinant bone sialoprotein: Delineation of the mineral-binding and cell adhesion domains and structural analysis of the RGD domain
    • J.T. Stubbs, K.P. Mintz, E.D. Eanes, D.A. Torchia, and L.W. Fisher Characterization of native and recombinant bone sialoprotein: delineation of the mineral-binding and cell adhesion domains and structural analysis of the RGD domain Journal of Bone and Mineral Research 12 1997 1210 1222
    • (1997) Journal of Bone and Mineral Research , vol.12 , pp. 1210-1222
    • Stubbs, J.T.1    Mintz, K.P.2    Eanes, E.D.3    Torchia, D.A.4    Fisher, L.W.5
  • 8
    • 0022354869 scopus 로고
    • Isolation and characterization of two sialoproteins present only in bone calcified matrix
    • A. Franzén, and D. Heinegård Isolation and characterization of two sialoproteins present only in bone calcified matrix Biochemical Journal 232 1985 715 724
    • (1985) Biochemical Journal , vol.232 , pp. 715-724
    • Franzén, A.1    Heinegård, D.2
  • 10
    • 0028129454 scopus 로고
    • Modulation of crystal formation by bone phosphoproteins: Role of glutamic acid-rich sequences in the nucleation of hydroxyapatite by bone sialoprotein
    • G.K. Hunter, and H.A. Goldberg Modulation of crystal formation by bone phosphoproteins: role of glutamic acid-rich sequences in the nucleation of hydroxyapatite by bone sialoprotein Biochemical Journal 302 1994 175 179
    • (1994) Biochemical Journal , vol.302 , pp. 175-179
    • Hunter, G.K.1    Goldberg, H.A.2
  • 11
    • 17144401467 scopus 로고    scopus 로고
    • Identification of the type i collagen-binding domain of bone sialoprotein and characterization of the mechanism of interaction
    • C.E. Tye, G.K. Hunter, and H.A. Goldberg Identification of the type I collagen-binding domain of bone sialoprotein and characterization of the mechanism of interaction Journal of Biological Chemistry 280 2005 13487 13492
    • (2005) Journal of Biological Chemistry , vol.280 , pp. 13487-13492
    • Tye, C.E.1    Hunter, G.K.2    Goldberg, H.A.3
  • 13
    • 0035671826 scopus 로고    scopus 로고
    • Elevated serum bone sialoprotein and osteopontin in colon, breast, prostate, and lung cancer
    • N.S. Fedarko, A. Jain, A. Karadag, M.R. Van Eman, and L.W. Fisher Elevated serum bone sialoprotein and osteopontin in colon, breast, prostate, and lung cancer Clinical Cancer Research 7 2001 4060 4066
    • (2001) Clinical Cancer Research , vol.7 , pp. 4060-4066
    • Fedarko, N.S.1    Jain, A.2    Karadag, A.3    Van Eman, M.R.4    Fisher, L.W.5
  • 15
    • 0029863676 scopus 로고    scopus 로고
    • Bone sialoprotein expression in primary human breast cancer is associated with bone metastases development
    • A. Bellahcène, M. Kroll, F. Liebens, and V. Castronovo Bone sialoprotein expression in primary human breast cancer is associated with bone metastases development Journal of Bone and Mineral Research 11 1996 665 670
    • (1996) Journal of Bone and Mineral Research , vol.11 , pp. 665-670
    • Bellahcène, A.1    Kroll, M.2    Liebens, F.3    Castronovo, V.4
  • 18
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • N. Guex, and M.C. Peitsch SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling Electrophoresis 18 1997 2714 2723
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 21
    • 84961986752 scopus 로고    scopus 로고
    • New developments in the polarizable continuum model for quantum mechanical and classical calculations on molecules in solution
    • K. Cossi, G. Scalmani, N. Rega, and V. Barone New developments in the polarizable continuum model for quantum mechanical and classical calculations on molecules in solution Journal of Chemical Physics 117 2002 43 54
    • (2002) Journal of Chemical Physics , vol.117 , pp. 43-54
    • Cossi, K.1    Scalmani, G.2    Rega, N.3    Barone, V.4
  • 22
    • 66349120487 scopus 로고    scopus 로고
    • Universal solvation model based on solute electron density and on a continuum model of the solvent defined by the bulk dielectric constant and atomic surface tensions
    • A.V. Marenich, C.J. Cramer, and D.G. Truhlar Universal solvation model based on solute electron density and on a continuum model of the solvent defined by the bulk dielectric constant and atomic surface tensions Journal of Physical Chemistry B 113 2009 6378 6396
    • (2009) Journal of Physical Chemistry B , vol.113 , pp. 6378-6396
    • Marenich, A.V.1    Cramer, C.J.2    Truhlar, D.G.3
  • 23
    • 28544444249 scopus 로고    scopus 로고
    • Glycomics: An integrated systems approach to structure-function relationships of glycans
    • R. Raman, S. Raguram, G. Venkataraman, J.C. Paulson, and R. Sasisekharan Glycomics: an integrated systems approach to structure-function relationships of glycans Nature Methods 2 2005 817 824 http://www.functionalglycomics.org/fg/
    • (2005) Nature Methods , vol.2 , pp. 817-824
    • Raman, R.1    Raguram, S.2    Venkataraman, G.3    Paulson, J.C.4    Sasisekharan, R.5
  • 24
    • 74049090465 scopus 로고    scopus 로고
    • Isoform-specific O-glycosylation of osteopontin and bone sialoprotein by polypeptide N-acetylgalactosaminyltransferase-1
    • H.E. Miwa, T.A. Gerken, O. Jamison, and L.A. Tabak Isoform-specific O-glycosylation of osteopontin and bone sialoprotein by polypeptide N-acetylgalactosaminyltransferase-1 Journal of Biological Chemistry 285 2010 1208 1219
    • (2010) Journal of Biological Chemistry , vol.285 , pp. 1208-1219
    • Miwa, H.E.1    Gerken, T.A.2    Jamison, O.3    Tabak, L.A.4
  • 25
    • 13644257223 scopus 로고    scopus 로고
    • Prediction, conservation analysis and structural characterization of mammalian mucin-type O-glycosylation sites
    • K. Julenius, A. Mølgaard, R. Gupta, and S. Brunak Prediction, conservation analysis and structural characterization of mammalian mucin-type O-glycosylation sites Glycobiology 15 2005 153 164 http://www.cbs.dtu.dk/ services/NetOGlyc/
    • (2005) Glycobiology , vol.15 , pp. 153-164
    • Julenius, K.1    Mølgaard, A.2    Gupta, R.3    Brunak, S.4
  • 29
    • 2442461058 scopus 로고    scopus 로고
    • Complete topographical distribution of both the in vivo and in vitro phosphorylation sites of bone sialoprotein and their biological implications
    • E. Salih, and R. Flckiger Complete topographical distribution of both the in vivo and in vitro phosphorylation sites of bone sialoprotein and their biological implications Journal of Biological Chemistry 279 2004 19808 19815
    • (2004) Journal of Biological Chemistry , vol.279 , pp. 19808-19815
    • Salih, E.1    Flckiger, R.2
  • 31
    • 0033579464 scopus 로고    scopus 로고
    • Sequence- and structure-based prediction of eukaryotic protein phosphorylation sites
    • N. Blom, S. Gammeltoft, and S. Brunak Sequence- and structure-based prediction of eukaryotic protein phosphorylation sites Journal of Molecular Biology 294 1999 1351 1362 http://www.cbs.dtu.dk/services/NetPhos/
    • (1999) Journal of Molecular Biology , vol.294 , pp. 1351-1362
    • Blom, N.1    Gammeltoft, S.2    Brunak, S.3
  • 33
    • 0033402315 scopus 로고    scopus 로고
    • Rietveld refinement of the crystallographic structure of human dental enamel apatites
    • R.M. Wilson, J.C. Elliot, and S.E.P. Dowker Rietveld refinement of the crystallographic structure of human dental enamel apatites American Mineralogist 84 1999 1406 1414
    • (1999) American Mineralogist , vol.84 , pp. 1406-1414
    • Wilson, R.M.1    Elliot, J.C.2    Dowker, S.E.P.3
  • 34
    • 0003187567 scopus 로고    scopus 로고
    • The atomic structure of protein-protein recognition sites
    • L. Lo Conte, C. Chothia, and J. Janin The atomic structure of protein-protein recognition sites Journal of Molecular Biology 285 1999 2177 2198
    • (1999) Journal of Molecular Biology , vol.285 , pp. 2177-2198
    • Lo Conte, L.1    Chothia, C.2    Janin, J.3
  • 35
    • 77956085282 scopus 로고    scopus 로고
    • How does bone sialoprotein promote the nucleation of hydroxyapatite? A molecular dynamics study using model peptides of different conformations
    • Y. Yang, Q. Cui, and N. Sahai How does bone sialoprotein promote the nucleation of hydroxyapatite? A molecular dynamics study using model peptides of different conformations Langmuir 26 2010 9848 9859
    • (2010) Langmuir , vol.26 , pp. 9848-9859
    • Yang, Y.1    Cui, Q.2    Sahai, N.3
  • 36
    • 80051791848 scopus 로고    scopus 로고
    • Theoretical study of bone sialoprotein in bone biomineralization
    • Y. Yang, D. Mkhonto, Q. Cui, and N. Sahai Theoretical study of bone sialoprotein in bone biomineralization Cells Tissues Organs 194 2011 182 187
    • (2011) Cells Tissues Organs , vol.194 , pp. 182-187
    • Yang, Y.1    Mkhonto, D.2    Cui, Q.3    Sahai, N.4
  • 38
    • 84857268098 scopus 로고    scopus 로고
    • Aqueous solutions of divalent chlorides: Ions hydration shell and water structure
    • F. Bruni, S. Imberti, R. Mancinelli, and M.A. Ricci Aqueous solutions of divalent chlorides: ions hydration shell and water structure Journal of Chemical Physics 136 2012 064520
    • (2012) Journal of Chemical Physics , vol.136 , pp. 064520
    • Bruni, F.1    Imberti, S.2    Mancinelli, R.3    Ricci, M.A.4
  • 41
    • 37049070010 scopus 로고
    • Thermodynamics of solvation of ions part 5. Gibbs free energy of hydration at 298.15 K
    • Y. Marcus Thermodynamics of solvation of ions part 5. Gibbs free energy of hydration at 298.15 K Journal of the Chemical Society, Faraday Transactions 87 1991 2995 2999
    • (1991) Journal of the Chemical Society, Faraday Transactions , vol.87 , pp. 2995-2999
    • Marcus, Y.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.