{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2024,9,5]],"date-time":"2024-09-05T19:46:40Z","timestamp":1725565600272},"reference-count":65,"publisher":"Elsevier BV","issue":"9","license":[{"start":{"date-parts":[[2005,9,1]],"date-time":"2005-09-01T00:00:00Z","timestamp":1125532800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Archives of Oral Biology"],"published-print":{"date-parts":[[2005,9]]},"DOI":"10.1016\/j.archoralbio.2005.02.002","type":"journal-article","created":{"date-parts":[[2005,3,11]],"date-time":"2005-03-11T16:52:35Z","timestamp":1110559955000},"page":"807-819","source":"Crossref","is-referenced-by-count":13,"title":["Association of bovine dentine phosphophoryn with collagen fragments"],"prefix":"10.1016","volume":"50","author":[{"given":"N. Laila","family":"Huq","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ashwini","family":"Loganathan","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Keith J.","family":"Cross","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Yu-Yen","family":"Chen","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Neil I.","family":"Johnson","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Matthew","family":"Willetts","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Paul D.","family":"Veith","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Eric C.","family":"Reynolds","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.archoralbio.2005.02.002_bib1","doi-asserted-by":"crossref","first-page":"4326","DOI":"10.1021\/bi00287a025","article-title":"Bovine dentin phosphophoryn: composition and molecular weight","volume":"22","author":"Stetler-Stevenson","year":"1983","journal-title":"Biochemistry"},{"key":"10.1016\/j.archoralbio.2005.02.002_bib2","doi-asserted-by":"crossref","first-page":"838","DOI":"10.1083\/jcb.56.3.838","article-title":"Radioautography visualization of the deposition of a phosphoprotein at the mineralization front in the dentin of the rat incisor","volume":"56","author":"Weinstock","year":"1973","journal-title":"J Cell Biol"},{"key":"10.1016\/j.archoralbio.2005.02.002_bib3","doi-asserted-by":"crossref","first-page":"493","DOI":"10.1042\/bj2320493","article-title":"Production and characterization of antibodies against murine dentine phosphoprotein","volume":"232","author":"MacDougall","year":"1985","journal-title":"Biochem J"},{"key":"10.1016\/j.archoralbio.2005.02.002_bib4","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1016\/S0021-9673(00)92338-0","article-title":"Isoelectric focusing of the phosphoprotein of rat-incisor dentin in Ampholine and Acid pH gradients. Evidence for carrier Ampholyte-protein complexes","volume":"157","author":"Jonsson","year":"1978","journal-title":"J Chromat"},{"key":"10.1016\/j.archoralbio.2005.02.002_bib5","doi-asserted-by":"crossref","first-page":"154","DOI":"10.1002\/ar.1092240206","article-title":"Dentin matrix proteins: composition and possible functions in calcification","volume":"224","author":"Linde","year":"1989","journal-title":"Anat Rec"},{"key":"10.1016\/j.archoralbio.2005.02.002_bib6","doi-asserted-by":"crossref","first-page":"56","DOI":"10.1016\/0304-4165(91)90074-Q","article-title":"Preferential adsorption of dentin and bone acidic proteins on the (100) face of hydroxyapatite crystals","volume":"1075","author":"Fujisawa","year":"1991","journal-title":"Biochim Biophys Acta"},{"key":"10.1016\/j.archoralbio.2005.02.002_bib7","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3109\/03008209409005630","article-title":"In vitro and in vivo association of dentin phosphophoryn with alpha- 1CB6 peptide of type I collagen","volume":"31","author":"Fujisawa","year":"1994","journal-title":"Conn Tiss Res"},{"key":"10.1016\/j.archoralbio.2005.02.002_bib8","doi-asserted-by":"crossref","first-page":"162","DOI":"10.1006\/jsbi.1998.4025","article-title":"Type I collagen-phosphophoryn interactions: specificity of the monomer-monomer binding","volume":"123","author":"Dahl","year":"1998","journal-title":"J Struct Biol"},{"key":"10.1016\/j.archoralbio.2005.02.002_bib9","series-title":"International Association for Dental Research, 79th General Session and Exhibition","first-page":"782","article-title":"Effect of dentin phosphophoryn of odontoblast-like cells in vitro","author":"Fujisawa","year":"2001"},{"key":"10.1016\/j.archoralbio.2005.02.002_bib10","doi-asserted-by":"crossref","first-page":"9457","DOI":"10.1074\/jbc.273.16.9457","article-title":"Genomic organization, chromosomal mapping, and promoter cnalysis of the mouse dentin sialophosphoprotein (Dspp) gene, which codes for both dentin sialoprotein and dentin phosphoprotein","volume":"273","author":"Feng","year":"1998","journal-title":"J Biol Chem"},{"key":"10.1016\/j.archoralbio.2005.02.002_bib11","doi-asserted-by":"crossref","first-page":"21695","DOI":"10.1074\/jbc.271.36.21695","article-title":"Sequence determination of an extremely acidic rat dentin phosphoprotein","volume":"271","author":"Ritchie","year":"1996","journal-title":"J Biol Chem"},{"key":"10.1016\/j.archoralbio.2005.02.002_bib12","doi-asserted-by":"crossref","first-page":"1914","DOI":"10.1177\/00220345000790111701","article-title":"N-terminal sequence analysis of bovine dentine phosphophoryn after conversion of phosphoseryl to S-propylcysteinyl residues","volume":"79","author":"Huq","year":"2000","journal-title":"J Dent Res"},{"key":"10.1016\/j.archoralbio.2005.02.002_bib13","doi-asserted-by":"crossref","first-page":"49","DOI":"10.3109\/03008209909005277","article-title":"Rat dentin matrix protein 3 is a compound protein of rat dentin sialoprotein and phosphophoryn","volume":"40","author":"George","year":"1999","journal-title":"Connect Tissue Res"},{"key":"10.1016\/j.archoralbio.2005.02.002_bib14","doi-asserted-by":"crossref","first-page":"680","DOI":"10.1038\/227680a0","article-title":"Cleavage of structural proteins during the assembly of the head bacteriophage T4","volume":"227","author":"Laemmli","year":"1970","journal-title":"Nature"},{"key":"10.1016\/j.archoralbio.2005.02.002_bib15","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1016\/0003-2697(73)90167-X","article-title":"Differential staining of phosphoproteins on polyacrylamide gels with a cationic carbocyanine dye","volume":"56","author":"Green","year":"1973","journal-title":"Anal Biochem"},{"key":"10.1016\/j.archoralbio.2005.02.002_bib16","doi-asserted-by":"crossref","first-page":"110","DOI":"10.1016\/0003-2697(83)90229-4","article-title":"Staining of alkali-labile phosphoproteins and alkaline phosphatases on polyacrylamide gels","volume":"133","author":"Debruyne","year":"1983","journal-title":"Anal Biochem"},{"key":"10.1016\/j.archoralbio.2005.02.002_bib17","series-title":"The Practical Approach","first-page":"53","article-title":"Gel Electrophoresis of Proteins","author":"Hames","year":"1990"},{"key":"10.1016\/j.archoralbio.2005.02.002_bib18","doi-asserted-by":"crossref","first-page":"2653","DOI":"10.3168\/jds.S0022-0302(95)76895-3","article-title":"Characterization of multiply phosphorylated peptides selectively precipitated from a pancreatic casein digest","volume":"78","author":"Adamson","year":"1995","journal-title":"J Dairy Sci"},{"key":"10.1016\/j.archoralbio.2005.02.002_bib19","doi-asserted-by":"crossref","first-page":"1625","DOI":"10.1177\/00220345790580061201","article-title":"The nature of covalent complexes of phosphoproteins with collagen in the bovine dentin matrix","volume":"58","author":"Curley-Joseph","year":"1979","journal-title":"J Dent Res"},{"key":"10.1016\/j.archoralbio.2005.02.002_bib20","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1007\/BF02407173","article-title":"Studies on the structure and chemistry of dentin collagen- phosphophoryn covalent complexes","volume":"31","author":"Lee","year":"1980","journal-title":"Calcif Tissue Int"},{"key":"10.1016\/j.archoralbio.2005.02.002_bib21","doi-asserted-by":"crossref","first-page":"239","DOI":"10.1007\/BF02405323","article-title":"Systematic purification of free and matrix- bound phosphophoryns of bovine dentin: presence of matrix-bound phosphophoryn as a distinct molecular entity","volume":"36","author":"Fujisawa","year":"1984","journal-title":"Calcif Tissue Int"},{"key":"10.1016\/j.archoralbio.2005.02.002_bib22","series-title":"5th Biennial Conference of ANZMAG","article-title":"NMR spectroscopy studies of bovine phosphophoryn","author":"Cross","year":"2004"},{"key":"10.1016\/j.archoralbio.2005.02.002_bib23","doi-asserted-by":"crossref","first-page":"5931","DOI":"10.1016\/S0021-9258(19)70720-0","article-title":"Noncollagenous proteins of dentin. A re-examination of proteins from rat incisor dentin utilizing techniques to avoid artifacts","volume":"255","author":"Linde","year":"1980","journal-title":"J Biol Chem"},{"key":"10.1016\/j.archoralbio.2005.02.002_bib24","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1016\/S0174-173X(81)80019-2","article-title":"Nonocollagenous proteins of dentin. Isolation and partial characterization of rat dentin proteins and proteoglycans using a three-step preparative method","volume":"1","author":"Butler","year":"1981","journal-title":"Coll Relat Res"},{"key":"10.1016\/j.archoralbio.2005.02.002_bib25","doi-asserted-by":"crossref","first-page":"527","DOI":"10.1016\/S0968-0004(02)02169-2","article-title":"Intrinsically unstructured proteins","volume":"27","author":"Tompa","year":"2002","journal-title":"Trends Biochem Sci"},{"key":"10.1016\/j.archoralbio.2005.02.002_bib26","doi-asserted-by":"crossref","first-page":"315","DOI":"10.1016\/0167-4838(82)90253-9","article-title":"Disagreement in molecular weight determinations of dentin phosphoprotein","volume":"705","author":"Jontell","year":"1982","journal-title":"Biochim Biophys Acta"},{"key":"10.1016\/j.archoralbio.2005.02.002_bib27","doi-asserted-by":"crossref","first-page":"1359","DOI":"10.1002\/bip.360341008","article-title":"Phosphophoryn, an \u201cAcidic\u201d Biomineralization Regulatory Protein: Conformational folding in the presence of Cd(II)","volume":"34","author":"Evans","year":"1994","journal-title":"Biopolymers"},{"key":"10.1016\/j.archoralbio.2005.02.002_bib28","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1034\/j.1600-0722.2000.00765.x","article-title":"Molecular cloning of a human dentin sialophosphoprotein gene","volume":"108","author":"Gu","year":"2000","journal-title":"Eur J Oral Sci"},{"key":"10.1016\/j.archoralbio.2005.02.002_bib29","doi-asserted-by":"crossref","first-page":"425","DOI":"10.1006\/bbrc.1997.6126","article-title":"A mammalian bicistronic transcript encoding two dentin-specific proteins","volume":"231","author":"Ritchie","year":"1997","journal-title":"Biochem Biophys Res Comm"},{"key":"10.1016\/j.archoralbio.2005.02.002_bib30","doi-asserted-by":"crossref","first-page":"241","DOI":"10.1006\/jsbi.1999.4107","article-title":"Lamellar bone: structure-function relations","volume":"126","author":"Weiner","year":"1999","journal-title":"J Struct Biol"},{"issue":"Suppl 1","key":"10.1016\/j.archoralbio.2005.02.002_bib31","doi-asserted-by":"crossref","first-page":"206","DOI":"10.1080\/03008200390181672","article-title":"Electrostatic interactions lead to the formation of asymmetric collagen-phosphophoryn aggregates","volume":"44","author":"Dahl","year":"2003","journal-title":"Connect Tissue Res"},{"key":"10.1016\/j.archoralbio.2005.02.002_bib32","doi-asserted-by":"crossref","first-page":"212","DOI":"10.1006\/jsbi.2000.4320","article-title":"A transmission electron microscope study using vitrified ice sections of predentin: structural changes in the dentin collagenous matrix prior to mineralization","volume":"132","author":"Beniash","year":"2000","journal-title":"J Struct Biol"},{"key":"10.1016\/j.archoralbio.2005.02.002_bib33","doi-asserted-by":"crossref","first-page":"197","DOI":"10.1016\/S0934-8832(11)80062-4","article-title":"Dentin phosphophoryn binding to collagen fibrils","volume":"12","author":"Traub","year":"1992","journal-title":"Matrix"},{"key":"10.1016\/j.archoralbio.2005.02.002_bib34","doi-asserted-by":"crossref","first-page":"4223","DOI":"10.1074\/jbc.M110709200","article-title":"Mapping the ligand-binding sites and disease-associated mutations on the most abundant protein in the human, type I collagen","volume":"277","author":"Di Lullo","year":"2002","journal-title":"J Biol Chem"},{"key":"10.1016\/j.archoralbio.2005.02.002_bib35","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1074\/jbc.275.1.35","article-title":"The collagen-binding A-domains of integrins alpha(1) beta(1) and alpha(2) beta(1) recognize the same specific amino acid sequence, GFOGER, in native (triple-helical) collagens","volume":"275","author":"Knight","year":"2000","journal-title":"J Biol Chem"},{"key":"10.1016\/j.archoralbio.2005.02.002_bib36","doi-asserted-by":"crossref","first-page":"454","DOI":"10.1038\/8259","article-title":"Sequence dependent conformational variations of collagen triple-helical structure","volume":"6","author":"Kramer","year":"1999","journal-title":"Nat Struct Biol"},{"key":"10.1016\/j.archoralbio.2005.02.002_bib37","doi-asserted-by":"crossref","first-page":"11649","DOI":"10.1074\/jbc.M309296200","article-title":"Dentin matrix protein 1 immobilized on type I collagen fibrils facilitates apatite deposition in vitro","volume":"279","author":"He","year":"2004","journal-title":"J Biol Chem"},{"key":"10.1016\/j.archoralbio.2005.02.002_bib38","doi-asserted-by":"crossref","first-page":"293","DOI":"10.1016\/0168-9525(90)90235-X","article-title":"Brittle bones\u2013fragile molecules: disorders of collagen gene structure and expression","volume":"6","author":"Byers","year":"1990","journal-title":"Trends Genet"},{"key":"10.1016\/j.archoralbio.2005.02.002_bib39","doi-asserted-by":"crossref","first-page":"2175","DOI":"10.1093\/hmg\/2.12.2175","article-title":"A novel glycine to glutamic acid substitution at position 343 in the alpha 2 chain of type I collagen in an individual with lethal osteogenesis imperfecta","volume":"2","author":"Rose","year":"1993","journal-title":"Hum Mol Genet"},{"key":"10.1016\/j.archoralbio.2005.02.002_bib40","first-page":"393","article-title":"Osteogenesis imperfecta at the beginning of bone and joint decade","volume":"42","author":"Primorac","year":"2001","journal-title":"Croat Med J"},{"key":"10.1016\/j.archoralbio.2005.02.002_bib41","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1136\/jmg.16.2.101","article-title":"Genetic heterogeneity in osteogenesis imperfecta","volume":"16","author":"Sillence","year":"1979","journal-title":"J Med Genet"},{"key":"10.1016\/j.archoralbio.2005.02.002_bib42","doi-asserted-by":"crossref","first-page":"1650","DOI":"10.1359\/jbmr.2000.15.9.1650","article-title":"Type V osteogenesis imperfecta: a new form of brittle bone disease","volume":"15","author":"Glorieux","year":"2000","journal-title":"J Bone Min Res"},{"key":"10.1016\/j.archoralbio.2005.02.002_bib43","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1093\/nar\/25.1.181","article-title":"The human type I collagen mutation database","volume":"25","author":"Dalgleish","year":"1997","journal-title":"Nucleic Acids Res"},{"key":"10.1016\/j.archoralbio.2005.02.002_bib44","doi-asserted-by":"crossref","first-page":"253","DOI":"10.1093\/nar\/26.1.253","article-title":"The Human Collagen Mutation Database","volume":"26","author":"Dalgleish","year":"1998","journal-title":"Nucleic Acids Res"},{"key":"10.1016\/j.archoralbio.2005.02.002_bib45","doi-asserted-by":"crossref","first-page":"347","DOI":"10.1002\/1097-0282(200103)58:3<347::AID-BIP1011>3.0.CO;2-M","article-title":"Computed free energy differences between point mutations in a collagen-like peptide","volume":"58","author":"Mooney","year":"2001","journal-title":"Biopolymers"},{"key":"10.1016\/j.archoralbio.2005.02.002_bib46","doi-asserted-by":"crossref","first-page":"4273","DOI":"10.1073\/pnas.070050097","article-title":"Destabilization of osteogenesis imperfecta collagen-like model peptides correlates with the identity of the residue replacing glycine","volume":"97","author":"Beck","year":"2000","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/j.archoralbio.2005.02.002_bib47","doi-asserted-by":"crossref","first-page":"15608","DOI":"10.1016\/S0021-9258(18)98449-8","article-title":"Substitutions for glycine alpha 1\u2013637 and glycine alpha 2\u2013694 of type I procollagen in lethal osteogenesis imperfecta. The conformational strain on the triple helix introduced by a glycine substitution can be transmitted along the helix","volume":"266","author":"Tsuneyoshi","year":"1991","journal-title":"J Biol Chem"},{"key":"10.1016\/j.archoralbio.2005.02.002_bib48","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1002\/(SICI)1098-1004(1998)12:1<71::AID-HUMU16>3.0.CO;2-4","article-title":"Four new cases of lethal osteogenesis imperfecta due to glycine substitutions in COL1A1 and genes. Mutations in brief no. 152 Online","volume":"12","author":"Mottes","year":"1998","journal-title":"Hum Mutat"},{"key":"10.1016\/j.archoralbio.2005.02.002_bib49","doi-asserted-by":"crossref","first-page":"14751","DOI":"10.1016\/S0021-9258(17)36689-9","article-title":"Substitution of an aspartic acid for glycine 700 in the alpha 2(I) chain of type I collagen in a recurrent lethal type II osteogenesis imperfecta dramatically affects the mineralization of bone","volume":"269","author":"Cohen-Solal","year":"1994","journal-title":"J Biol Chem"},{"key":"10.1016\/j.archoralbio.2005.02.002_bib50","doi-asserted-by":"crossref","first-page":"25162","DOI":"10.1016\/S0021-9258(19)74583-9","article-title":"Two additional cases of osteogenesis imperfecta with substitutions for glycine in the alpha 2(I) collagen chain. A regional model relating mutation location with phenotype","volume":"268","author":"Wang","year":"1993","journal-title":"J Biol Chem"},{"key":"10.1016\/j.archoralbio.2005.02.002_bib51","doi-asserted-by":"crossref","first-page":"347","DOI":"10.1006\/geno.1995.9867","article-title":"Mapping of the human dentin matrix acidic phosphoprotein gene (DMP1) to the dentinogenesis imperfecta type II critical region at chromosome 4q21","volume":"30","author":"Aplin","year":"1995","journal-title":"Genomics"},{"key":"10.1016\/j.archoralbio.2005.02.002_bib52","doi-asserted-by":"crossref","first-page":"227","DOI":"10.1111\/j.1600-0722.1998.tb02180.x","article-title":"Refined mapping of the human dentin sialophosphoprotein (DSPP) gene within the critical dentinogenesis imperfecta type II and dentin dysplasia type II loci","volume":"106","author":"MacDougall","year":"1998","journal-title":"Eur J Oral Sci"},{"key":"10.1016\/j.archoralbio.2005.02.002_bib53","doi-asserted-by":"crossref","first-page":"201","DOI":"10.1038\/84848","article-title":"Dentinogenesis imperfecta 1 with or without progressive hearing loss is associated with distinct mutations in DSPP","volume":"27","author":"Xiao","year":"2001","journal-title":"Nat Genet"},{"key":"10.1016\/j.archoralbio.2005.02.002_bib54","doi-asserted-by":"crossref","first-page":"151","DOI":"10.1038\/84765","article-title":"DSPP mutation in dentinogenesis imperfecta Shields type II","volume":"27","author":"Zhang","year":"2001","journal-title":"Nat Genet"},{"key":"10.1016\/j.archoralbio.2005.02.002_bib55","doi-asserted-by":"crossref","first-page":"24874","DOI":"10.1074\/jbc.M303908200","article-title":"Dentin sialophosphoprotein knockout mouse teeth display widened predentin zone and develop defective dentin mineralization similar to human dentinogenesis imperfecta type III","volume":"278","author":"Sreenath","year":"2003","journal-title":"J Biol Chem"},{"key":"10.1016\/j.archoralbio.2005.02.002_bib56","doi-asserted-by":"crossref","first-page":"401","DOI":"10.1080\/03008200290001005","article-title":"Odontoblast dysfunction in osteogenesis imperfecta: an LM, SEM, and ultrastructural study","volume":"43","author":"Hall","year":"2002","journal-title":"Connect Tissue Res"},{"key":"10.1016\/j.archoralbio.2005.02.002_bib57","doi-asserted-by":"crossref","first-page":"85","DOI":"10.1016\/S0945-053X(98)90127-5","article-title":"The complete cDNA coding sequence for the bovine proalpha2(I) chain of type I procollagen","volume":"17","author":"Shirai","year":"1998","journal-title":"Matrix Biol"},{"key":"10.1016\/j.archoralbio.2005.02.002_bib58","doi-asserted-by":"crossref","first-page":"2596","DOI":"10.1021\/bi00280a001","article-title":"Phosphoproteins of bovine dentin: evidence for polydispersity during tooth maturation","volume":"22","author":"Lee","year":"1983","journal-title":"Biochemistry"},{"key":"10.1016\/j.archoralbio.2005.02.002_bib59","doi-asserted-by":"crossref","first-page":"1057","DOI":"10.1016\/0003-9969(92)90038-A","article-title":"Comparison of phosphoprotein isolated from mature and immature human tooth roots","volume":"37","author":"McCurdy","year":"1992","journal-title":"Arch Oral Biol"},{"key":"10.1016\/j.archoralbio.2005.02.002_bib60","doi-asserted-by":"crossref","first-page":"149","DOI":"10.1007\/s002239900101","article-title":"Characterization and identification of a human dentin phosphophoryn","volume":"59","author":"Chang","year":"1996","journal-title":"Calcif Tissue Int"},{"key":"10.1016\/j.archoralbio.2005.02.002_bib61","doi-asserted-by":"crossref","first-page":"651","DOI":"10.1042\/bj2870651","article-title":"Characteristics of phosphorylated and non-phosphorylated dentine phosphoprotein","volume":"287","author":"MacDougall","year":"1992","journal-title":"Biochem J"},{"key":"10.1016\/j.archoralbio.2005.02.002_bib62","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1016\/S0167-4781(00)00150-0","article-title":"The presence of multiple rat DSP-PP transcripts","volume":"1493","author":"Ritchie","year":"2000","journal-title":"Biochim Biophys Acta"},{"key":"10.1016\/j.archoralbio.2005.02.002_bib63","doi-asserted-by":"crossref","first-page":"212","DOI":"10.1016\/S0167-4781(01)00274-3","article-title":"A novel rat 523 amino acid phosphophoryn: nucleotide sequence and genomic organization","volume":"1520","author":"Ritchie","year":"2001","journal-title":"Biochim Biophys Acta"},{"key":"10.1016\/j.archoralbio.2005.02.002_bib64","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1007\/BF02010765","article-title":"Phosphophoryns-major noncollagenous proteins of rat incisor dentin","volume":"25","author":"Dimuzio","year":"1978","journal-title":"Calcif Tissue Res"},{"key":"10.1016\/j.archoralbio.2005.02.002_bib65","doi-asserted-by":"crossref","first-page":"321","DOI":"10.1007\/BF02064089","article-title":"Phosphoprotein of rat incisor dentine","volume":"22","author":"Jontell","year":"1977","journal-title":"Calcif Tissue Res"}],"container-title":["Archives of Oral Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0003996905000683?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0003996905000683?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2021,7,6]],"date-time":"2021-07-06T21:11:20Z","timestamp":1625605880000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0003996905000683"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2005,9]]},"references-count":65,"journal-issue":{"issue":"9","published-print":{"date-parts":[[2005,9]]}},"alternative-id":["S0003996905000683"],"URL":"https:\/\/doi.org\/10.1016\/j.archoralbio.2005.02.002","relation":{},"ISSN":["0003-9969"],"issn-type":[{"value":"0003-9969","type":"print"}],"subject":[],"published":{"date-parts":[[2005,9]]}}}