메뉴 건너뛰기




Volumn 416, Issue , 2014, Pages 69-79

Proteome degradation in ancient bone: Diagenesis and phylogenetic potential

Author keywords

Albumin; Ancient proteins; Fetuin A; Non collagenous proteins; Palaeoproteomics; Secreted phosphoprotein 24

Indexed keywords

ARCHAEOLOGICAL EVIDENCE; BIOMINERALIZATION; BONE; COLLAGEN; DATING METHOD; DNA; GEOLOGICAL RECORD; MOLECULAR ANALYSIS; PALEONTOLOGY; PHYLOGENETICS; PROTEOMICS; SURVIVORSHIP;

EID: 84910593381     PISSN: 00310182     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.palaeo.2014.06.026     Document Type: Article
Times cited : (60)

References (141)
  • 1
    • 75249102809 scopus 로고    scopus 로고
    • Chronological distribution of Pleistocene cold-adapted large mammal faunas in the Iberian Peninsula
    • Álvarez-Lao D.J., García N. Chronological distribution of Pleistocene cold-adapted large mammal faunas in the Iberian Peninsula. Quat. Int. 2010, 212:120-128.
    • (2010) Quat. Int. , vol.212 , pp. 120-128
    • Álvarez-Lao, D.J.1    García, N.2
  • 3
    • 0030587432 scopus 로고    scopus 로고
    • Complement proteins are present in developing endochondral bone and may mediate cartilage cell death and vascularization
    • Andrades J.A., Nimni M.E., Becerra J., Eisenstein R., Davis M., Sorgente N. Complement proteins are present in developing endochondral bone and may mediate cartilage cell death and vascularization. Exp. Cell Res. 1996, 227:208-213.
    • (1996) Exp. Cell Res. , vol.227 , pp. 208-213
    • Andrades, J.A.1    Nimni, M.E.2    Becerra, J.3    Eisenstein, R.4    Davis, M.5    Sorgente, N.6
  • 5
    • 0033613644 scopus 로고    scopus 로고
    • Preservation of key biomolecules in the fossil record: current knowledge and future challenges
    • Bada J., Wang X., Hamilton H. Preservation of key biomolecules in the fossil record: current knowledge and future challenges. R. Soc. Lond. Philos. Trans. B Biol. Sci. 1999, 354:77-86.
    • (1999) R. Soc. Lond. Philos. Trans. B Biol. Sci. , vol.354 , pp. 77-86
    • Bada, J.1    Wang, X.2    Hamilton, H.3
  • 6
    • 14844366668 scopus 로고    scopus 로고
    • The application of ancient DNA analysis to identify Neolithic caprinae: a case study from the site of Hatoula, Israel
    • Bar-Gal G.K., Ducos P., Horwitz L.K. The application of ancient DNA analysis to identify Neolithic caprinae: a case study from the site of Hatoula, Israel. Int. J. Osteoarchaeol. 2003, 13:120-131.
    • (2003) Int. J. Osteoarchaeol. , vol.13 , pp. 120-131
    • Bar-Gal, G.K.1    Ducos, P.2    Horwitz, L.K.3
  • 7
    • 0030607184 scopus 로고    scopus 로고
    • The speed of post mortem change to the human skeleton and its taphonomic significance
    • Bell L.S., Skinner M.F., Jones S.J. The speed of post mortem change to the human skeleton and its taphonomic significance. Forensic Sci. Int. 1996, 82:129-140.
    • (1996) Forensic Sci. Int. , vol.82 , pp. 129-140
    • Bell, L.S.1    Skinner, M.F.2    Jones, S.J.3
  • 8
    • 1942451825 scopus 로고    scopus 로고
    • Characterization of the human secreted phosphoprotein 24 gene (SPP2) and comparison of the protein sequence in nine species
    • Bennett C.S., Khorram Khorshid H.R., Alexandra Kitchen J., Arteta D., Dalgleish R. Characterization of the human secreted phosphoprotein 24 gene (SPP2) and comparison of the protein sequence in nine species. Matrix Biol. 2004, 22:641-651.
    • (2004) Matrix Biol. , vol.22 , pp. 641-651
    • Bennett, C.S.1    Khorram Khorshid, H.R.2    Alexandra Kitchen, J.3    Arteta, D.4    Dalgleish, R.5
  • 9
    • 3042702591 scopus 로고    scopus 로고
    • Solubilities of bone mineral from archaeological sites: the recrystalization window
    • Berna F., Matthew A., Weiner S. Solubilities of bone mineral from archaeological sites: the recrystalization window. J. Archaeol. Sci. 2004, 31:867-882.
    • (2004) J. Archaeol. Sci. , vol.31 , pp. 867-882
    • Berna, F.1    Matthew, A.2    Weiner, S.3
  • 10
    • 0025110119 scopus 로고
    • Expression and localization of the two small proteoglycans biglycan and decorin in developing human skeletal and non-skeletal tissues
    • Bianco P., Fisher L.W., Young M.F., Termine J.D., Robey P.G. Expression and localization of the two small proteoglycans biglycan and decorin in developing human skeletal and non-skeletal tissues. J. Histochem. Cytochem. 1990, 38:1549-1563.
    • (1990) J. Histochem. Cytochem. , vol.38 , pp. 1549-1563
    • Bianco, P.1    Fisher, L.W.2    Young, M.F.3    Termine, J.D.4    Robey, P.G.5
  • 13
    • 38549145989 scopus 로고    scopus 로고
    • Mineralization of bones and teeth
    • Boskey A.L. Mineralization of bones and teeth. Elements 2007, 3:385-391.
    • (2007) Elements , vol.3 , pp. 385-391
    • Boskey, A.L.1
  • 14
    • 77955892561 scopus 로고    scopus 로고
    • Carboxy terminus of secreted phosphoprotein-24kDa (spp24) is essential for full inhibition of BMP-2 activity
    • Brochmann E.J., Simon R.J., Jawien J., Behnam K., Sintuu C., Wang J.C., Murray S.S. Carboxy terminus of secreted phosphoprotein-24kDa (spp24) is essential for full inhibition of BMP-2 activity. J. Orthop. Res. 2010, 28:1200-1207.
    • (2010) J. Orthop. Res. , vol.28 , pp. 1200-1207
    • Brochmann, E.J.1    Simon, R.J.2    Jawien, J.3    Behnam, K.4    Sintuu, C.5    Wang, J.C.6    Murray, S.S.7
  • 16
    • 84875443817 scopus 로고    scopus 로고
    • A molecular phylogeny of Plesiorycteropus reassigns the extinct mammalian order 'Bibymalagasia'
    • Buckley M. A molecular phylogeny of Plesiorycteropus reassigns the extinct mammalian order 'Bibymalagasia'. PloS One 2013, 8:e59614.
    • (2013) PloS One , vol.8 , pp. e59614
    • Buckley, M.1
  • 17
    • 84856225583 scopus 로고    scopus 로고
    • Collagen survival and its use for species identification in Holocene-lower Pleistocene bone fragments from British archaeological and paleontological sites
    • Buckley M., Collins M.J. Collagen survival and its use for species identification in Holocene-lower Pleistocene bone fragments from British archaeological and paleontological sites. Antiqua 2011, 1:e1.
    • (2011) Antiqua , vol.1 , pp. e1
    • Buckley, M.1    Collins, M.J.2
  • 18
    • 84872476201 scopus 로고    scopus 로고
    • Collagen fingerprinting of archaeological bone and teeth remains from Domuztepe, South Eastern Turkey
    • Buckley M., Kansa S.W. Collagen fingerprinting of archaeological bone and teeth remains from Domuztepe, South Eastern Turkey. Archaeol. Anthropol. Sci. 2011, 3:271-280.
    • (2011) Archaeol. Anthropol. Sci. , vol.3 , pp. 271-280
    • Buckley, M.1    Kansa, S.W.2
  • 20
    • 39149092338 scopus 로고    scopus 로고
    • A method of isolating the collagen (I) alpha 2 chain carboxytelopeptide for species identification in bone fragments
    • Buckley M., Collins M.J., Thomas-Oates J. A method of isolating the collagen (I) alpha 2 chain carboxytelopeptide for species identification in bone fragments. Anal. Biochem. 2008, 374:325-334.
    • (2008) Anal. Biochem. , vol.374 , pp. 325-334
    • Buckley, M.1    Collins, M.J.2    Thomas-Oates, J.3
  • 21
    • 71949102106 scopus 로고    scopus 로고
    • Species identification by analysis of bone collagen using matrix-assisted laser desorption/ionisation time-of-flight mass spectrometry
    • Buckley M., Collins M.J., Thomas-Oates J., Wilson J. Species identification by analysis of bone collagen using matrix-assisted laser desorption/ionisation time-of-flight mass spectrometry. Rapid Commun. Mass Spectrom. 2009, 23(23):3843-3854.
    • (2009) Rapid Commun. Mass Spectrom. , vol.23 , Issue.23 , pp. 3843-3854
    • Buckley, M.1    Collins, M.J.2    Thomas-Oates, J.3    Wilson, J.4
  • 23
    • 79952444146 scopus 로고    scopus 로고
    • Mammoth and Mastodon collagen sequences; survival and utility
    • Buckley M., Larkin N., Collins M. Mammoth and Mastodon collagen sequences; survival and utility. Geochim. Cosmochim. Acta 2011, 75:2007-2016.
    • (2011) Geochim. Cosmochim. Acta , vol.75 , pp. 2007-2016
    • Buckley, M.1    Larkin, N.2    Collins, M.3
  • 25
    • 0242650635 scopus 로고    scopus 로고
    • Species determination using species-discriminating PCR-RFLP of ancient DNA from prehistoric skeletal remains
    • Burger J., Schoon R., Zeike B., Hummel S., Herrmann B. Species determination using species-discriminating PCR-RFLP of ancient DNA from prehistoric skeletal remains. Anc. Biomol. 2001, 4:19-23.
    • (2001) Anc. Biomol. , vol.4 , pp. 19-23
    • Burger, J.1    Schoon, R.2    Zeike, B.3    Hummel, S.4    Herrmann, B.5
  • 26
    • 0030062183 scopus 로고    scopus 로고
    • Association of thrombospondin-1 with osteogenic differentiation of retinal pericytes in vitro
    • Canfield A.E., Sutton A.B., Hoyland J.A., Schor A.M. Association of thrombospondin-1 with osteogenic differentiation of retinal pericytes in vitro. J. Cell Sci. 1996, 109:343-353.
    • (1996) J. Cell Sci. , vol.109 , pp. 343-353
    • Canfield, A.E.1    Sutton, A.B.2    Hoyland, J.A.3    Schor, A.M.4
  • 29
    • 0026543856 scopus 로고
    • Reliable identification of human albumin in ancient bone using ELISA and monoclonal-antibodies
    • Cattaneo C., Gelsthorpe K., Phillips P., Sokol R.J. Reliable identification of human albumin in ancient bone using ELISA and monoclonal-antibodies. Am. J. Phys. Anthropol. 1992, 87:365-372.
    • (1992) Am. J. Phys. Anthropol. , vol.87 , pp. 365-372
    • Cattaneo, C.1    Gelsthorpe, K.2    Phillips, P.3    Sokol, R.J.4
  • 31
    • 0003386478 scopus 로고
    • Microbial attack on collagen
    • BirkhŠuser Verlag, Basel, E. Pernicka, G.A. Wagner (Eds.)
    • Child A.M., Pollard A.M. Microbial attack on collagen. Archaeometry '90 1991, 617-626. BirkhŠuser Verlag, Basel. E. Pernicka, G.A. Wagner (Eds.).
    • (1991) Archaeometry '90 , pp. 617-626
    • Child, A.M.1    Pollard, A.M.2
  • 33
    • 0000745015 scopus 로고
    • A basic mathematical simulation of the chemical degradation of ancient collagen
    • Collins M.J., Riley M.S., Child A.M., Turner-Walker G. A basic mathematical simulation of the chemical degradation of ancient collagen. J. Archaeol. Sci. 1995, 22:175-183.
    • (1995) J. Archaeol. Sci. , vol.22 , pp. 175-183
    • Collins, M.J.1    Riley, M.S.2    Child, A.M.3    Turner-Walker, G.4
  • 34
    • 84874987797 scopus 로고    scopus 로고
    • Slow rates of degradation of osteocalcin: green light for fossil bone protein?
    • Collins M.J., Gernaey A.M., Nielsen-Marsh C.M., Vermeer C., Westbroek P. Slow rates of degradation of osteocalcin: green light for fossil bone protein?. Geology 2000, 28:1139-1142.
    • (2000) Geology , vol.28 , pp. 1139-1142
    • Collins, M.J.1    Gernaey, A.M.2    Nielsen-Marsh, C.M.3    Vermeer, C.4    Westbroek, P.5
  • 37
    • 38249030898 scopus 로고
    • The use and meaning of species diversity and richness in archaeological faunas
    • Cruz-Uribe K. The use and meaning of species diversity and richness in archaeological faunas. J. Archaeol. Sci. 1988, 15:179-196.
    • (1988) J. Archaeol. Sci. , vol.15 , pp. 179-196
    • Cruz-Uribe, K.1
  • 38
    • 59349097182 scopus 로고    scopus 로고
    • The reconstruction of past environments through small mammals: from the Mousterian to the Bronze Age in El Mirón Cave (Cantabria, Spain)
    • Cuenca-Bescós G., Straus L.G., González Morales M.R., García Pimienta J.C. The reconstruction of past environments through small mammals: from the Mousterian to the Bronze Age in El Mirón Cave (Cantabria, Spain). J. Archaeol. Sci. 2009, 36:947-955.
    • (2009) J. Archaeol. Sci. , vol.36 , pp. 947-955
    • Cuenca-Bescós, G.1    Straus, L.G.2    González Morales, M.R.3    García Pimienta, J.C.4
  • 39
    • 0034758268 scopus 로고    scopus 로고
    • A formal mammalian biostratigraphy for the Late Pleistocene of Britain
    • Currant A., Jacobi R. A formal mammalian biostratigraphy for the Late Pleistocene of Britain. Quat. Sci. Rev. 2001, 20:1707-1716.
    • (2001) Quat. Sci. Rev. , vol.20 , pp. 1707-1716
    • Currant, A.1    Jacobi, R.2
  • 41
    • 0010381849 scopus 로고
    • Amino acids and proteins from fossils
    • Paleontological Society, G. Eglinton, G.B. Curry (Eds.)
    • Curry G.B. Amino acids and proteins from fossils. Molecular Evolution and the Fossil Record 1988, 20-33. Paleontological Society. G. Eglinton, G.B. Curry (Eds.).
    • (1988) Molecular Evolution and the Fossil Record , pp. 20-33
    • Curry, G.B.1
  • 42
    • 0037211159 scopus 로고    scopus 로고
    • Biochemical markers of nutrition and bone mineral density in the elderly
    • Di Monaco M., Vallero F., Di Monaco R., Mautino F., Cavanna A. Biochemical markers of nutrition and bone mineral density in the elderly. Gerontology 2003, 49:50-54.
    • (2003) Gerontology , vol.49 , pp. 50-54
    • Di Monaco, M.1    Vallero, F.2    Di Monaco, R.3    Mautino, F.4    Cavanna, A.5
  • 43
    • 0018415278 scopus 로고
    • Characterization of protein S, a gamma-carboxyglutamic acid containing protein from bovine and human plasma
    • DiScipio R.G., Davie E.W. Characterization of protein S, a gamma-carboxyglutamic acid containing protein from bovine and human plasma. Biochemistry 1979, 18:899-904.
    • (1979) Biochemistry , vol.18 , pp. 899-904
    • DiScipio, R.G.1    Davie, E.W.2
  • 47
    • 0033027858 scopus 로고    scopus 로고
    • VEGF couples hypertrophic cartilage remodeling, ossification and angiogenesis during endochondral bone formation
    • Gerber H.P., Vu T.H., Ryan A.M., Kowalski J., Werb Z., Ferrara N. VEGF couples hypertrophic cartilage remodeling, ossification and angiogenesis during endochondral bone formation. Nat. Med. 1999, 5(6):623-628.
    • (1999) Nat. Med. , vol.5 , Issue.6 , pp. 623-628
    • Gerber, H.P.1    Vu, T.H.2    Ryan, A.M.3    Kowalski, J.4    Werb, Z.5    Ferrara, N.6
  • 48
    • 33845972288 scopus 로고    scopus 로고
    • Bone: nature of the calcium phosphate crystals and cellular, structural, and physical chemical mechanisms in their formation
    • Glimcher M.J. Bone: nature of the calcium phosphate crystals and cellular, structural, and physical chemical mechanisms in their formation. Rev. Mineral. Geochem. 2006, 64:223-282.
    • (2006) Rev. Mineral. Geochem. , vol.64 , pp. 223-282
    • Glimcher, M.J.1
  • 49
    • 84897494657 scopus 로고    scopus 로고
    • Serine protease HTRA1 antagonizes Transforming Growth Factor-β signaling by cleaving its receptors and loss of HTRA1 in vitro enhances bone formation
    • Graham J.R., Chamberland A., Lin Q., Li X.J., Dai D., Zeng W., Ryan M.S., Rivera-Bemudez M.A., Flannery C.R., Yang Z. Serine protease HTRA1 antagonizes Transforming Growth Factor-β signaling by cleaving its receptors and loss of HTRA1 in vitro enhances bone formation. PloS One 2013, 8(9):e74094.
    • (2013) PloS One , vol.8 , Issue.9 , pp. e74094
    • Graham, J.R.1    Chamberland, A.2    Lin, Q.3    Li, X.J.4    Dai, D.5    Zeng, W.6    Ryan, M.S.7    Rivera-Bemudez, M.A.8    Flannery, C.R.9    Yang, Z.10
  • 50
    • 0040913297 scopus 로고    scopus 로고
    • Serum proteins in archaeological human bone
    • Grupe G., Turban-Just S. Serum proteins in archaeological human bone. Int. J. Osteoarchaeol. 1996, 6:300-308.
    • (1996) Int. J. Osteoarchaeol. , vol.6 , pp. 300-308
    • Grupe, G.1    Turban-Just, S.2
  • 51
    • 33846293781 scopus 로고
    • The crystallinity of bone mineral
    • Grynpas M. The crystallinity of bone mineral. J. Mater. Sci. 1976, 11(9):1691-1696.
    • (1976) J. Mater. Sci. , vol.11 , Issue.9 , pp. 1691-1696
    • Grynpas, M.1
  • 52
    • 0028272931 scopus 로고
    • Bone matrix RGD glycoproteins: immunolocalization and interaction with human primary osteoblastic bone cells in vitro
    • Grzesik W.J., Robey P.G. Bone matrix RGD glycoproteins: immunolocalization and interaction with human primary osteoblastic bone cells in vitro. J. Bone Miner. Res. 1994, 9:487-496.
    • (1994) J. Bone Miner. Res. , vol.9 , pp. 487-496
    • Grzesik, W.J.1    Robey, P.G.2
  • 53
    • 0242578620 scopus 로고    scopus 로고
    • A simple, fast, and accurate algorithm to estimate large phylogenies by maximum likelihood
    • Guindon S., Gascuel O. A simple, fast, and accurate algorithm to estimate large phylogenies by maximum likelihood. Syst. Biol. 2003, 52:696-704.
    • (2003) Syst. Biol. , vol.52 , pp. 696-704
    • Guindon, S.1    Gascuel, O.2
  • 54
    • 0019782379 scopus 로고
    • Microscopical focal destruction (tunnels) - in exhumed human bones
    • Hackett C.J. Microscopical focal destruction (tunnels) - in exhumed human bones. Med. Sci. Law 1981, 21:243-265.
    • (1981) Med. Sci. Law , vol.21 , pp. 243-265
    • Hackett, C.J.1
  • 55
    • 84872358077 scopus 로고    scopus 로고
    • The C-terminal peptide of chondroadherin modulates cellular activity by selectively binding to heparan sulfate chains
    • Haglund L., Tillgren V., Önnerfjord P., Heinegård D. The C-terminal peptide of chondroadherin modulates cellular activity by selectively binding to heparan sulfate chains. J. Biol. Chem. 2013, 288:995-1008.
    • (2013) J. Biol. Chem. , vol.288 , pp. 995-1008
    • Haglund, L.1    Tillgren, V.2    Önnerfjord, P.3    Heinegård, D.4
  • 56
    • 0001968748 scopus 로고
    • Organic geochemistry of bone and its relation to the survival of bone in the natural environment
    • Univ., of Chicago Press, A.K. Behrensmeyer, A.P. Hill (Eds.)
    • Hare P.E. Organic geochemistry of bone and its relation to the survival of bone in the natural environment. Fossils in the Making 1980, 208-219. Univ., of Chicago Press. A.K. Behrensmeyer, A.P. Hill (Eds.).
    • (1980) Fossils in the Making , pp. 208-219
    • Hare, P.E.1
  • 57
    • 0024370924 scopus 로고
    • Osteocalcin and matrix Gla protein: vitamin K-dependent proteins in bone
    • Hauschka P.V., Lian J.B., Cole D.E., Gundberg C.M. Osteocalcin and matrix Gla protein: vitamin K-dependent proteins in bone. Physiol. Rev. 1989, 69:990-1047.
    • (1989) Physiol. Rev. , vol.69 , pp. 990-1047
    • Hauschka, P.V.1    Lian, J.B.2    Cole, D.E.3    Gundberg, C.M.4
  • 58
    • 0036668895 scopus 로고    scopus 로고
    • Bone diagenesis: an overview of processes
    • Hedges R.E.M. Bone diagenesis: an overview of processes. Archaeometry 2002, 44:319-328.
    • (2002) Archaeometry , vol.44 , pp. 319-328
    • Hedges, R.E.M.1
  • 59
    • 0024847070 scopus 로고
    • Molecular models illustrating the possible distributions of 'holes' in simple systematically staggered arrays of type I collagen molecules in native-type fibrils
    • Hodge A.J. Molecular models illustrating the possible distributions of 'holes' in simple systematically staggered arrays of type I collagen molecules in native-type fibrils. Connect. Tissue Res. 1989, 21:137-147.
    • (1989) Connect. Tissue Res. , vol.21 , pp. 137-147
    • Hodge, A.J.1
  • 60
    • 84893428799 scopus 로고    scopus 로고
    • Cleaning up the masses: exclusion lists to reduce contamination with HPLC-MS/MS
    • Hodge K., Ten Have S., Hutton L., Lamond A. Cleaning up the masses: exclusion lists to reduce contamination with HPLC-MS/MS. J. Proteome 2013, 88(100):92-103.
    • (2013) J. Proteome , vol.88 , Issue.100 , pp. 92-103
    • Hodge, K.1    Ten Have, S.2    Hutton, L.3    Lamond, A.4
  • 62
    • 76449087928 scopus 로고    scopus 로고
    • Stable isotope analysis of the Middle Helladic population from two cemeteries at Asine: Barbouna and the east cemetery
    • Ingvarsson-Sundström A., Richards M., Voutsaki S. Stable isotope analysis of the Middle Helladic population from two cemeteries at Asine: Barbouna and the east cemetery. Mediterr. Archaeol. Archaeometry 2009, 9:1-14.
    • (2009) Mediterr. Archaeol. Archaeometry , vol.9 , pp. 1-14
    • Ingvarsson-Sundström, A.1    Richards, M.2    Voutsaki, S.3
  • 64
    • 34250846498 scopus 로고    scopus 로고
    • Method development of efficient protein extraction in bone tissue for proteome analysis
    • Jiang X., Ye M., Jiang X., Liu G., Feng S., Cui L., Zou H. Method development of efficient protein extraction in bone tissue for proteome analysis. J. Proteome Res. 2007, 6:2287-2294.
    • (2007) J. Proteome Res. , vol.6 , pp. 2287-2294
    • Jiang, X.1    Ye, M.2    Jiang, X.3    Liu, G.4    Feng, S.5    Cui, L.6    Zou, H.7
  • 65
    • 33748746585 scopus 로고    scopus 로고
    • Small leucine rich repeat proteoglycans (SLRPs) in the human sclera: identification of abundant levels of PRELP
    • Johnson J.M., Young T.L., Rada J. Small leucine rich repeat proteoglycans (SLRPs) in the human sclera: identification of abundant levels of PRELP. Mol. Vis. 2006, 12:1057-1066.
    • (2006) Mol. Vis. , vol.12 , pp. 1057-1066
    • Johnson, J.M.1    Young, T.L.2    Rada, J.3
  • 66
    • 0028679665 scopus 로고
    • Extracellular matrix 1: fibril-forming collagens
    • Kadler K. Extracellular matrix 1: fibril-forming collagens. Protein Profile 1994, 1:519-524.
    • (1994) Protein Profile , vol.1 , pp. 519-524
    • Kadler, K.1
  • 68
    • 0027408611 scopus 로고
    • Quantitative analyses of the interaction between calcium ions and human serum albumin
    • Kragh-Hansen U., Vorum H. Quantitative analyses of the interaction between calcium ions and human serum albumin. Clin. Chem. 1993, 39:202-208.
    • (1993) Clin. Chem. , vol.39 , pp. 202-208
    • Kragh-Hansen, U.1    Vorum, H.2
  • 69
    • 2142720271 scopus 로고    scopus 로고
    • Mineral characterization in calcifying tissues: atomic, molecular and macromolecular perspectives
    • Landis W.J. Mineral characterization in calcifying tissues: atomic, molecular and macromolecular perspectives. Connect. Tissue Res. 1996, 35:1-8.
    • (1996) Connect. Tissue Res. , vol.35 , pp. 1-8
    • Landis, W.J.1
  • 71
    • 0018681997 scopus 로고
    • A model for the distribution of HAP crystallites in bone - an hypothesis
    • Lees S. A model for the distribution of HAP crystallites in bone - an hypothesis. Calcif. Tissue Int. 1979, 27:53-56.
    • (1979) Calcif. Tissue Int. , vol.27 , pp. 53-56
    • Lees, S.1
  • 72
    • 0022871419 scopus 로고
    • Gene for human factor X: a blood coagulation factor whose gene organization is essentially identical with that of factor IX and protein C
    • Leytus S.P., Foster D.C., Kurachi K., Davie E.W. Gene for human factor X: a blood coagulation factor whose gene organization is essentially identical with that of factor IX and protein C. Biochemistry 1986, 25(18):5098-5102.
    • (1986) Biochemistry , vol.25 , Issue.18 , pp. 5098-5102
    • Leytus, S.P.1    Foster, D.C.2    Kurachi, K.3    Davie, E.W.4
  • 74
    • 0000296985 scopus 로고
    • Preservation of fossil leaf waxes in association with their source tissues, Clarkia, Northern Idaho, USA
    • Logan G.A., Smiley C.J., Eglinton G. Preservation of fossil leaf waxes in association with their source tissues, Clarkia, Northern Idaho, USA. Geochim. Cosmochim. Acta 1995, 59:751-763.
    • (1995) Geochim. Cosmochim. Acta , vol.59 , pp. 751-763
    • Logan, G.A.1    Smiley, C.J.2    Eglinton, G.3
  • 78
    • 0031698415 scopus 로고    scopus 로고
    • Serum albumin and bone mineral density in healthy older men and women: the Rancho Bernardo Study
    • Lunde A.V., Barrett-Connor E., Morton D.J. Serum albumin and bone mineral density in healthy older men and women: the Rancho Bernardo Study. Osteoporos. Int. 1998, 8:547-551.
    • (1998) Osteoporos. Int. , vol.8 , pp. 547-551
    • Lunde, A.V.1    Barrett-Connor, E.2    Morton, D.J.3
  • 79
    • 0026547723 scopus 로고
    • Protein-S, a vitamin K-dependent protein, is a bone matrix component synthesized and secreted by osteoblasts
    • Maillard C., Berruyer M., Serre C.M., Dechavanne M., Delmas P.D. Protein-S, a vitamin K-dependent protein, is a bone matrix component synthesized and secreted by osteoblasts. Endocrinology 1992, 130(3):1599-1604.
    • (1992) Endocrinology , vol.130 , Issue.3 , pp. 1599-1604
    • Maillard, C.1    Berruyer, M.2    Serre, C.M.3    Dechavanne, M.4    Delmas, P.D.5
  • 80
    • 0025311157 scopus 로고
    • Surface-dependent reactions of the vitamin K-dependent enzyme complexes
    • Mann K.G., Nesheim M.E., Church W.R., Haley P., Krishnaswamy S. Surface-dependent reactions of the vitamin K-dependent enzyme complexes. Blood 1990, 76(1):1-16.
    • (1990) Blood , vol.76 , Issue.1 , pp. 1-16
    • Mann, K.G.1    Nesheim, M.E.2    Church, W.R.3    Haley, P.4    Krishnaswamy, S.5
  • 81
    • 0023470462 scopus 로고
    • Preferential preservation of non-collagenous protein during bone diagenesis: implications for chronometric and stable isotopic measurements
    • Masters P.M. Preferential preservation of non-collagenous protein during bone diagenesis: implications for chronometric and stable isotopic measurements. Geochim. Cosmochim. Acta 1987, 51:3209-3214.
    • (1987) Geochim. Cosmochim. Acta , vol.51 , pp. 3209-3214
    • Masters, P.M.1
  • 82
    • 0037160083 scopus 로고    scopus 로고
    • Mapping the Type I collagen-binding site on pigment epithelium-derived factor implications for its antiangiogenic activity
    • Meyer C., Notari L., Becerra S.P. Mapping the Type I collagen-binding site on pigment epithelium-derived factor implications for its antiangiogenic activity. J. Biol. Chem. 2002, 277:45400-45407.
    • (2002) J. Biol. Chem. , vol.277 , pp. 45400-45407
    • Meyer, C.1    Notari, L.2    Becerra, S.P.3
  • 84
    • 0029814647 scopus 로고    scopus 로고
    • Bone chondroadherin promotes attachment of osteoblastic cells to solid-state substrates and shows affinity to collagen
    • Mizuno M., Fujisawa R., Kuboki Y. Bone chondroadherin promotes attachment of osteoblastic cells to solid-state substrates and shows affinity to collagen. Calcif. Tissue Int. 1996, 59:163-167.
    • (1996) Calcif. Tissue Int. , vol.59 , pp. 163-167
    • Mizuno, M.1    Fujisawa, R.2    Kuboki, Y.3
  • 85
    • 0001733072 scopus 로고
    • Albumin preserved in fossil bones and systematics of Malpaisolys insularis (Muridae, Rodentia), an extinct rodent of the Canary Islands
    • Montgelard C. Albumin preserved in fossil bones and systematics of Malpaisolys insularis (Muridae, Rodentia), an extinct rodent of the Canary Islands. Hist. Biol. 1992, 6:293-302.
    • (1992) Hist. Biol. , vol.6 , pp. 293-302
    • Montgelard, C.1
  • 86
    • 79954525957 scopus 로고    scopus 로고
    • Fetuin-A: a multifunctional protein. Recent patents on endocrine, metabolic & immune drug discovery 5
    • Mori, K., Emoto, M., Inaba, M., 2011. Fetuin-A: a multifunctional protein. Recent patents on endocrine, metabolic & immune drug discovery 5, 124-146.
    • (2011) , pp. 124-146
    • Mori, K.1    Emoto, M.2    Inaba, M.3
  • 88
    • 84910632426 scopus 로고    scopus 로고
    • Totty Pot, Cheddar, Somerset: the faunal remains
    • Murray Totty Pot, Cheddar, Somerset: the faunal remains. Proc. Univ. Bristol Spelaeol. Soc. 2010, 25(1):97-104.
    • (2010) Proc. Univ. Bristol Spelaeol. Soc. , vol.25 , Issue.1 , pp. 97-104
  • 89
    • 0345145682 scopus 로고    scopus 로고
    • The localization of CD44 and moesin in osteoclasts after calcitonin administration in mouse tibiae
    • Nakamura H., Yamada M., Fukae M., Ozawa H. The localization of CD44 and moesin in osteoclasts after calcitonin administration in mouse tibiae. J. Bone Miner. Metab. 1997, 15:184-192.
    • (1997) J. Bone Miner. Metab. , vol.15 , pp. 184-192
    • Nakamura, H.1    Yamada, M.2    Fukae, M.3    Ozawa, H.4
  • 91
    • 0017875774 scopus 로고
    • Interaction of vitamin K dependent proteins with membranes
    • Nelsestuen G.L., Kisiel W., Di Scipio R.G. Interaction of vitamin K dependent proteins with membranes. Biochemistry 1978, 17:2134-2138.
    • (1978) Biochemistry , vol.17 , pp. 2134-2138
    • Nelsestuen, G.L.1    Kisiel, W.2    Di Scipio, R.G.3
  • 92
    • 0034731197 scopus 로고    scopus 로고
    • A preliminary investigation of the application of differential scanning calorimetry to the study of collagen degradation in archaeological bone
    • Nielsen-Marsh C.M., Hedges R.E.M., Mann T., Collins M.J. A preliminary investigation of the application of differential scanning calorimetry to the study of collagen degradation in archaeological bone. Thermochim. Acta 2000, 365:129-139.
    • (2000) Thermochim. Acta , vol.365 , pp. 129-139
    • Nielsen-Marsh, C.M.1    Hedges, R.E.M.2    Mann, T.3    Collins, M.J.4
  • 96
    • 0023193605 scopus 로고
    • Levels of Creatine Kinase activity in cartilage of tubular and nontubular bone in relation to pathogenesis of achondroplasia
    • Nogami H.M.D., Oohira A., Ogasawara N.M.D. Levels of Creatine Kinase activity in cartilage of tubular and nontubular bone in relation to pathogenesis of achondroplasia. Clin. Orthop. Relat. Res 1987, 219:308-312.
    • (1987) Clin. Orthop. Relat. Res , vol.219 , pp. 308-312
    • Nogami, H.M.D.1    Oohira, A.2    Ogasawara, N.M.D.3
  • 97
    • 0024970684 scopus 로고
    • Ancient DNA and the polymerase chain reaction. The emerging field of molecular archaeology
    • Paabo S., Higuchi R.G., Wilson A.C. Ancient DNA and the polymerase chain reaction. The emerging field of molecular archaeology. J. Biol. Chem. 1989, 264:9709-9712.
    • (1989) J. Biol. Chem. , vol.264 , pp. 9709-9712
    • Paabo, S.1    Higuchi, R.G.2    Wilson, A.C.3
  • 98
    • 0001513835 scopus 로고
    • Fetuin, a new globulin isolated from serum
    • Pedersen K.O. Fetuin, a new globulin isolated from serum. Nature 1944, 154:575.
    • (1944) Nature , vol.154 , pp. 575
    • Pedersen, K.O.1
  • 99
    • 0004732607 scopus 로고    scopus 로고
    • The albumin molecule: its structure and chemical properties
    • Academic Press, San Diego, All about albumin
    • Peters T.J. The albumin molecule: its structure and chemical properties. Biochemistry, Genetics, and Medical Applications 1996, 9-75. Academic Press, San Diego.
    • (1996) Biochemistry, Genetics, and Medical Applications , pp. 9-75
    • Peters, T.J.1
  • 100
    • 0014594078 scopus 로고
    • Crystal chemistry of bone mineral
    • Posner A.S. Crystal chemistry of bone mineral. Physiol. Rev. 1969, 49(4):760-792.
    • (1969) Physiol. Rev. , vol.49 , Issue.4 , pp. 760-792
    • Posner, A.S.1
  • 101
    • 84910593249 scopus 로고    scopus 로고
    • Animal management strategies during the Chalcolithic in the Lower Galilee: new data from Marj Rabba (Israel)
    • Price M.D., Buckley M., Kersel M., Rowan Y.M. Animal management strategies during the Chalcolithic in the Lower Galilee: new data from Marj Rabba (Israel). Paléorient 2013, 39(2):183-200.
    • (2013) Paléorient , vol.39 , Issue.2 , pp. 183-200
    • Price, M.D.1    Buckley, M.2    Kersel, M.3    Rowan, Y.M.4
  • 102
    • 0031572274 scopus 로고    scopus 로고
    • Characterization of the complex between bovine osteocalcin and type 1 collagen
    • Prigodich R.V., Vesely M.R. Characterization of the complex between bovine osteocalcin and type 1 collagen. Arch. Biochem. Biophys. 1997, 345(2):339-341.
    • (1997) Arch. Biochem. Biophys. , vol.345 , Issue.2 , pp. 339-341
    • Prigodich, R.V.1    Vesely, M.R.2
  • 103
    • 3042701269 scopus 로고    scopus 로고
    • Post-translational modifications of sibling proteins and their roles in osteogenesis and dentinogenesis
    • Qin C., Baba O., Butler W.T. Post-translational modifications of sibling proteins and their roles in osteogenesis and dentinogenesis. Crit. Rev. Oral Biol. Med. 2004, 15:126.
    • (2004) Crit. Rev. Oral Biol. Med. , vol.15 , pp. 126
    • Qin, C.1    Baba, O.2    Butler, W.T.3
  • 106
    • 0012831712 scopus 로고
    • Macromolecules form living and fossil biominerals; implications for the establishment of molecuar phyolgenies
    • Plenum, New York. M.H. Engle, S.A. Macko (Eds.)
    • Robbins L.L., Muyzer G., Brew K. Macromolecules form living and fossil biominerals; implications for the establishment of molecuar phyolgenies. Org Geochem 1993, 799-816. Plenum, New York. M.H. Engle, S.A. Macko (Eds.).
    • (1993) Org Geochem , pp. 799-816
    • Robbins, L.L.1    Muyzer, G.2    Brew, K.3
  • 107
    • 0022580184 scopus 로고
    • Inhibition of hydroxyapatite-crystal growth by bone-specific and other calcium-binding proteins
    • Romberg R.W., Werness P.G., Riggs B.L., Mann K.G. Inhibition of hydroxyapatite-crystal growth by bone-specific and other calcium-binding proteins. Biochemistry 1986, 25:1176-1180.
    • (1986) Biochemistry , vol.25 , pp. 1176-1180
    • Romberg, R.W.1    Werness, P.G.2    Riggs, B.L.3    Mann, K.G.4
  • 109
    • 0025823515 scopus 로고
    • Extracellular proteins that moderate cell-matrix interactions. SPARC, tenascin and thrombospondin
    • Sage E.H., Bornstein P. Extracellular proteins that moderate cell-matrix interactions. SPARC, tenascin and thrombospondin. J. Biol. Chem. 1991, 266(23):14831-14834.
    • (1991) J. Biol. Chem. , vol.266 , Issue.23 , pp. 14831-14834
    • Sage, E.H.1    Bornstein, P.2
  • 110
    • 0026802046 scopus 로고
    • A gene family consisting of ezrin, radixin and moesin. Its specific localization at actin filament/plasma membrane association sites
    • Sato N., Funayama N., Nagafuchi A., Yonemura S., Tsukita S., Tsukita S. A gene family consisting of ezrin, radixin and moesin. Its specific localization at actin filament/plasma membrane association sites. J. Cell Sci. 1992, 103(Pt 1):131-143.
    • (1992) J. Cell Sci. , vol.103 , pp. 131-143
    • Sato, N.1    Funayama, N.2    Nagafuchi, A.3    Yonemura, S.4    Tsukita, S.5    Tsukita, S.6
  • 111
    • 33847352500 scopus 로고    scopus 로고
    • Well preserved non-collagenous extracellular matrix proteins in ancient human bone and teeth
    • Schmidt-Schultz T.H., Schultz M. Well preserved non-collagenous extracellular matrix proteins in ancient human bone and teeth. Int. J. Osteoarchaeol. 2007, 17(1):91-99.
    • (2007) Int. J. Osteoarchaeol. , vol.17 , Issue.1 , pp. 91-99
    • Schmidt-Schultz, T.H.1    Schultz, M.2
  • 112
    • 0035013395 scopus 로고    scopus 로고
    • Mammalian evidence from Middle Pleistocene fluvial sequences for complex environmental change at the oxygen isotope substage level
    • Schreve D.C. Mammalian evidence from Middle Pleistocene fluvial sequences for complex environmental change at the oxygen isotope substage level. Quat. Int. 2001, 79:65-74.
    • (2001) Quat. Int. , vol.79 , pp. 65-74
    • Schreve, D.C.1
  • 113
    • 2942525306 scopus 로고    scopus 로고
    • Molecular paleontology: some current advances and problems
    • Schweitzer M.H. Molecular paleontology: some current advances and problems. Ann. Paléontol. 2004, 90:81-102.
    • (2004) Ann. Paléontol. , vol.90 , pp. 81-102
    • Schweitzer, M.H.1
  • 115
    • 0019366659 scopus 로고
    • Plough and pastoralism: aspects of the Secondary Products Revolution
    • Cambridge University Press, Cambridge, I. Hodder, G. Isaac, N. Hammond (Eds.)
    • Sherratt A. Plough and pastoralism: aspects of the Secondary Products Revolution. Patterns of the Past 1981, 261-305. Cambridge University Press, Cambridge. I. Hodder, G. Isaac, N. Hammond (Eds.).
    • (1981) Patterns of the Past , pp. 261-305
    • Sherratt, A.1
  • 118
    • 84984160550 scopus 로고
    • The vertebrate fauna of the type Cromerian
    • Stuart A.J. The vertebrate fauna of the type Cromerian. Boreas 1975, 4:63-76.
    • (1975) Boreas , vol.4 , pp. 63-76
    • Stuart, A.J.1
  • 120
    • 0034764832 scopus 로고    scopus 로고
    • The mammalian faunas of Pakefield/Kessingland and Corton, Suffolk, UK: evidence for a new temperate episode in the British early Middle Pleistocene
    • Stuart A.J., Lister A.M. The mammalian faunas of Pakefield/Kessingland and Corton, Suffolk, UK: evidence for a new temperate episode in the British early Middle Pleistocene. Quat. Sci. Rev. 2001, 20:1677-1692.
    • (2001) Quat. Sci. Rev. , vol.20 , pp. 1677-1692
    • Stuart, A.J.1    Lister, A.M.2
  • 121
    • 84910622821 scopus 로고
    • Some Notes on the New Excavations at Asine
    • Styrenius C.-G. Some Notes on the New Excavations at Asine. Opuscula Atheniensia 1975, 177-183.
    • (1975) Opuscula Atheniensia , pp. 177-183
    • Styrenius, C.-G.1
  • 123
    • 17044366009 scopus 로고
    • An analysis of faunal remains from archaeological sites in southern South West Africa (Namibia)
    • Thackeray J.F. An analysis of faunal remains from archaeological sites in southern South West Africa (Namibia). S. Afr. Archaeol. Bull. 1979, 18-33.
    • (1979) S. Afr. Archaeol. Bull.
    • Thackeray, J.F.1
  • 124
    • 84866709537 scopus 로고    scopus 로고
    • Human serine protease HTRA1 positively regulates osteogenesis of human bone marrow-derived mesenchymal stem cells and mineralization of differentiating bone-forming cells through the modulation of extracellular matrix protein
    • Tiaden A.N., Breiden M., Mirsaidi A., Weber F.A., Bahrenberg G., Glanz S., Cinelli P., Ehrmann M., Richards P.J. Human serine protease HTRA1 positively regulates osteogenesis of human bone marrow-derived mesenchymal stem cells and mineralization of differentiating bone-forming cells through the modulation of extracellular matrix protein. Stem cells (Dayton, Ohio) 2012, 30:2271-2282.
    • (2012) Stem cells (Dayton, Ohio) , vol.30 , pp. 2271-2282
    • Tiaden, A.N.1    Breiden, M.2    Mirsaidi, A.3    Weber, F.A.4    Bahrenberg, G.5    Glanz, S.6    Cinelli, P.7    Ehrmann, M.8    Richards, P.J.9
  • 127
    • 0018263654 scopus 로고
    • Plasma disappearance of rabbit α2 HS-glycoprotein and its uptake by bone tissue
    • Triffitt J., Owen M., Ashton B., Wilson J. Plasma disappearance of rabbit α2 HS-glycoprotein and its uptake by bone tissue. Calcif. Tissue Res. 1978, 26:155-161.
    • (1978) Calcif. Tissue Res. , vol.26 , pp. 155-161
    • Triffitt, J.1    Owen, M.2    Ashton, B.3    Wilson, J.4
  • 128
    • 1942456460 scopus 로고    scopus 로고
    • Mineralogical and compositional changes in bones exposed on soil surfaces in Amboseli National Park, Kenya: diagenetic mechanisms and the role of sediment pore fluids
    • Trueman C.N.G., Behrensmeyer A.K., Tuross N., Weiner S. Mineralogical and compositional changes in bones exposed on soil surfaces in Amboseli National Park, Kenya: diagenetic mechanisms and the role of sediment pore fluids. J. Archaeol. Sci. 2004, 31:721-739.
    • (2004) J. Archaeol. Sci. , vol.31 , pp. 721-739
    • Trueman, C.N.G.1    Behrensmeyer, A.K.2    Tuross, N.3    Weiner, S.4
  • 129
    • 0023582399 scopus 로고
    • Albumin preservation in the Taima-taima mastodon skeleton
    • Tuross N. Albumin preservation in the Taima-taima mastodon skeleton. Appl. Geochem. 1989, 4:255-259.
    • (1989) Appl. Geochem. , vol.4 , pp. 255-259
    • Tuross, N.1
  • 130
    • 0025126721 scopus 로고
    • Effects of vitamin D-binding protein on bone resorption stimulated by 1, 25 dihydroxyvitamin D3
    • Vargas S., Bouillon R., Van Baelen H., Raisz L.G. Effects of vitamin D-binding protein on bone resorption stimulated by 1, 25 dihydroxyvitamin D3. Calcif. Tissue Int. 1990, 47:164-168.
    • (1990) Calcif. Tissue Int. , vol.47 , pp. 164-168
    • Vargas, S.1    Bouillon, R.2    Van Baelen, H.3    Raisz, L.G.4
  • 131
    • 3042718717 scopus 로고    scopus 로고
    • Differential roles for small leucine-rich proteoglycans in bone formation
    • (discussion 21)
    • Waddington R.J., Roberts H.C., Sugars R.V., Schonherr E. Differential roles for small leucine-rich proteoglycans in bone formation. Eur. Cells Mater. 2003, 6:12-21. (discussion 21).
    • (2003) Eur. Cells Mater. , vol.6 , pp. 12-21
    • Waddington, R.J.1    Roberts, H.C.2    Sugars, R.V.3    Schonherr, E.4
  • 132
    • 84893826865 scopus 로고    scopus 로고
    • Proteome degradation in fossils: investigating the longevity of protein survival in ancient bone
    • Wadsworth C., Buckley M. Proteome degradation in fossils: investigating the longevity of protein survival in ancient bone. Rapid Commun. Mass Spectrom. 2014, 28(6):605-615.
    • (2014) Rapid Commun. Mass Spectrom. , vol.28 , Issue.6 , pp. 605-615
    • Wadsworth, C.1    Buckley, M.2
  • 134
    • 0025206192 scopus 로고
    • States of preservation of bones from prehistoric sites in the Near East: a survey
    • Weiner S., Bar-Yosef O. States of preservation of bones from prehistoric sites in the Near East: a survey. J. Archaeol. Sci. 1990, 17:187-196.
    • (1990) J. Archaeol. Sci. , vol.17 , pp. 187-196
    • Weiner, S.1    Bar-Yosef, O.2
  • 135
    • 0023027892 scopus 로고
    • Disaggregation of bone into crystals
    • Weiner S., Price P.A. Disaggregation of bone into crystals. Calcif. Tissue Int. 1986, 39:365-375.
    • (1986) Calcif. Tissue Int. , vol.39 , pp. 365-375
    • Weiner, S.1    Price, P.A.2
  • 136
    • 0023043475 scopus 로고
    • Organization of hydroxyapatite crystals within collagen fibrils
    • Weiner S., Traub W. Organization of hydroxyapatite crystals within collagen fibrils. FEBS Lett. 1986, 206:262-266.
    • (1986) FEBS Lett. , vol.206 , pp. 262-266
    • Weiner, S.1    Traub, W.2
  • 138
    • 0032559637 scopus 로고    scopus 로고
    • Ezrin/radixin/moesin (ERM) proteins bind to a positively charged amino acid cluster in the juxta-membrane cytoplasmic domain of CD44, CD43, and ICAM-2
    • Yonemura S., Hirao M., Doi Y., Takahashi N., Kondo T., Tsukita S., Tsukita S. Ezrin/radixin/moesin (ERM) proteins bind to a positively charged amino acid cluster in the juxta-membrane cytoplasmic domain of CD44, CD43, and ICAM-2. J. Cell Biol. 1998, 140:885-895.
    • (1998) J. Cell Biol. , vol.140 , pp. 885-895
    • Yonemura, S.1    Hirao, M.2    Doi, Y.3    Takahashi, N.4    Kondo, T.5    Tsukita, S.6    Tsukita, S.7
  • 139
    • 0141429078 scopus 로고    scopus 로고
    • Biglycan knockout mice: new models for musculoskeletal diseases
    • Young M.F., Bi Y., Ameye L., Chen X.D. Biglycan knockout mice: new models for musculoskeletal diseases. Glycoconj. J. 2002, 19:257-262.
    • (2002) Glycoconj. J. , vol.19 , pp. 257-262
    • Young, M.F.1    Bi, Y.2    Ameye, L.3    Chen, X.D.4
  • 140
    • 0034233269 scopus 로고    scopus 로고
    • Encapsulation of protein in humic acid from a histosol as an explanation for the occurrence of organic nitrogen in soil and sediment
    • Zang X., van Heemst J.D.H., Dria K.J., Hatcher P.G. Encapsulation of protein in humic acid from a histosol as an explanation for the occurrence of organic nitrogen in soil and sediment. Org. Geochem. 2000, 31:679-695.
    • (2000) Org. Geochem. , vol.31 , pp. 679-695
    • Zang, X.1    van Heemst, J.D.H.2    Dria, K.J.3    Hatcher, P.G.4
  • 141
    • 84884098298 scopus 로고    scopus 로고
    • The regulatory role of matrix proteins in mineralisation of bone
    • Elsevier, New York, D. Feldman, D. Nelson, C.J. Rosen (Eds.)
    • Zhu W., Robey P.G., Boskey A.L. The regulatory role of matrix proteins in mineralisation of bone. Osteoporosis 2007, 191-240. Elsevier, New York. Third ed. D. Feldman, D. Nelson, C.J. Rosen (Eds.).
    • (2007) Osteoporosis , pp. 191-240
    • Zhu, W.1    Robey, P.G.2    Boskey, A.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.