ArticleJournal of molecular evolution2013
The dentin matrix acidic phosphoprotein 1 (DMP1) in the light of mammalian evolution.
Article in Journal of molecular evolution, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Expression of 20 SCPP genes during tooth and bone mineralization in Senegal bichir.Development genes and evolution · 2023Article
- The Role of Intrinsically Disordered Proteins in Liquid-Liquid Phase Separation during Calcium Carbonate Biomineralization.Biomolecules · 2022Review
- The Role of DMP1 in CKD-MBD.Current osteoporosis reports · 2021Review
- Whole exome sequencing identifies an AMBN missense mutation causing severe autosomal-dominant amelogenesis imperfecta and dentin disorders.International journal of oral science · 2018Article
- Evolutionary Analysis of the Mammalian Tuftelin Sequence Reveals Features of Functional Importance.Journal of molecular evolution · 2017Article
- Evolutionary Analysis Predicts Sensitive Positions of MMP20 and Validates Newly- and Previously-IdentifiedFrontiers in physiology · 2017Article
- Article
- Evolutionary analysis of selective constraints identifies ameloblastin (AMBN) as a potential candidate for amelogenesis imperfecta.BMC evolutionary biology · 2015Article
- Molecular evolution of the tissue-nonspecific alkaline phosphatase allows prediction and validation of missense mutations responsible for hypophosphatasia.The Journal of biological chemistry · 2014Article
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Authors and funding
3 authors.
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Abstract
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.
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