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<OAI-PMH schemaLocation=http://www.openarchives.org/OAI/2.0/ http://www.openarchives.org/OAI/2.0/OAI-PMH.xsd> <responseDate>2018-01-17T12:07:23Z</responseDate> <request identifier=oai:HAL:hal-01545482v1 verb=GetRecord metadataPrefix=oai_dc>http://api.archives-ouvertes.fr/oai/hal/</request> <GetRecord> <record> <header> <identifier>oai:HAL:hal-01545482v1</identifier> <datestamp>2018-01-11</datestamp> <setSpec>type:ART</setSpec> <setSpec>subject:sdv</setSpec> <setSpec>collection:EVOL_PARIS_SEINE-EDS</setSpec> <setSpec>collection:EVOLUTION_PARIS_SEINE</setSpec> <setSpec>collection:UPMC</setSpec> <setSpec>collection:CNRS</setSpec> <setSpec>collection:UNIV-AG</setSpec> <setSpec>collection:UNICE</setSpec> <setSpec>collection:SAE</setSpec> <setSpec>collection:GIP-BE</setSpec> <setSpec>collection:UPMC_POLE_4</setSpec> <setSpec>collection:IBPS</setSpec> <setSpec>collection:UCA-TEST</setSpec> <setSpec>collection:UNIV-COTEDAZUR</setSpec> </header> <metadata><dc> <publisher>HAL CCSD</publisher> <title lang=en>The Dentin Matrix Acidic Phosphoprotein 1 (DMP1) in the Light of Mammalian Evolution</title> <creator>Silvent, Jeremie</creator> <creator>Sire, Jean-Yves</creator> <creator>Delgado, Sidney</creator> <contributor>Evolution et développement du squelette (EDS) ; Evolution Paris Seine ; Université Nice Sophia Antipolis (UNS) ; Université Côte d'Azur (UCA) - Université Côte d'Azur (UCA) - Centre National de la Recherche Scientifique (CNRS) - Université des Antilles et de la Guyane (UAG) - Université Pierre et Marie Curie - Paris 6 (UPMC) - Université Nice Sophia Antipolis (UNS) ; Université Côte d'Azur (UCA) - Université Côte d'Azur (UCA) - Centre National de la Recherche Scientifique (CNRS) - Université des Antilles et de la Guyane (UAG) - Université Pierre et Marie Curie - Paris 6 (UPMC) - Systématique, adaptation, évolution (SAE) ; Université Pierre et Marie Curie - Paris 6 (UPMC) - Centre National de la Recherche Scientifique (CNRS)</contributor> <contributor>Centre National de la Recherche Scientifique (CNRS)</contributor> <contributor> Universite Pierre et Marie Curie (UMR7138)</contributor> <description>International audience</description> <source>ISSN: 0022-2844</source> <source>EISSN: 1432-1432</source> <source>Journal of Molecular Evolution</source> <publisher>Springer Verlag</publisher> <identifier>hal-01545482</identifier> <identifier>https://hal.archives-ouvertes.fr/hal-01545482</identifier> <source>https://hal.archives-ouvertes.fr/hal-01545482</source> <source>Journal of Molecular Evolution, Springer Verlag, 2013, 76 (1-2), pp.59-70. 〈10.1007/s00239-013-9539-2〉</source> <identifier>DOI : 10.1007/s00239-013-9539-2</identifier> <relation>info:eu-repo/semantics/altIdentifier/doi/10.1007/s00239-013-9539-2</relation> <language>en</language> <subject lang=en>Dentin matrix acidic phosphoprotein 1</subject> <subject lang=en> Evolutionary analysis</subject> <subject lang=en> Dentin</subject> <subject lang=en> Bone</subject> <subject lang=en> Mineralization</subject> <subject lang=en> Mammals</subject> <subject>[SDV.BID.EVO] Life Sciences [q-bio]/Biodiversity/Populations and Evolution [q-bio.PE]</subject> <type>info:eu-repo/semantics/article</type> <type>Journal articles</type> <description lang=en>Dentin matrix acidic phosphoprotein 1 (DMP1) is an acidic, highly phosphorylated, noncollagenous protein secreted during dentin and bone formation. Previous functional studies of DMP1 have revealed various motifs playing a role in either mineralization or cell differentiation. We performed an evolutionary analysis of DMP1 to identify residues and motifs that were conserved during 220 millions years (Ma) of mammalian evolution, and hence have an important function. In silico search provided us with 41 sequences that were aligned and analyzed using the Hyphy program. We showed that DMP1 contains 55 positions that were kept unchanged for 220 Ma. We also defined in a more precise manner some motifs that were already known (i.e., cleavage sites, RGD motif, ASARM peptide, glycosaminoglycan chain attachment site, nuclear localization signal sites, and dentin sialophosphoprotein-binding site), and we found five, highly conserved, new functional motifs. In the near future, functional studies could be performed to understand the role played by them.</description> <date>2013-02</date> </dc> </metadata> </record> </GetRecord> </OAI-PMH>