ArticleBiomacromolecules2011
Primary structure and phosphorylation of dentin matrix protein 1 (DMP1) and dentin phosphophoryn (DPP) uniquely determine their role in biomineralization.
Article in Biomacromolecules, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
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Who cites it
49 citing papers in PubMed, 126 citations in OpenAlex.
- Amelogenin Phosphorylation Affects Key Regulatory Genes in the Enamel Organ.Calcified tissue international · 2026Review
- Dentin matrix protein-1 promoted osteogenic differentiation of valvular interstitial cells via MAPK signal pathway during aortic valve calcification.In vitro cellular & developmental biology. Animal · 2025Article
- Amyloid-induced mineralization: From biological systems to biomimetic materials.Bioactive materials · 2025Review
- The effects and mechanisms underlying collagen-binding peptides MDPs on dentin remineralization: an in vitro study.BMC oral health · 2025Article
- DSP and DPP are dispensable for initiation of dentin and enamel mineralization but critical for circumpulpal dentin mineralization.Scientific reports · 2025Article
- Phosphate in Physiological and Pathological Mineralization: Important yet Often Unheeded.MedComm · 2025Review
- Article
- Deciphering 3D periodontal fibroblast-macrophage crosstalk in bioactive nanoparticle-guided immunomodulation for treating traumatic dental avulsion.Bioactive materials · 2024Article
- Role of amelogenin phosphorylation in regulating dental enamel formation.Matrix biology : journal of the International Society for Matrix Biology · 2024Article
- Structure of biomimetic casein micelles: Critical tests of the hydrophobic colloid and multivalent-binding models using recombinant deuterated and phosphorylated β-casein.Journal of structural biology: X · 2024Article
- LPS-induced inflammation potentiates dental pulp stem cell odontogenic differentiation through C5aR and p38.Connective tissue research · 2023Article
- Fam20C overexpression in odontoblasts regulates dentin formation and odontoblast differentiation.Journal of molecular histology · 2023Article
- Effects of Red LED Irradiation in Enhancing the Mineralization of Human Dental Pulp Cells In Vitro.International journal of molecular sciences · 2023Article
- Expression of immunomodulatory and tissue regenerative biomarkers in human dental pulp derived-mesenchymal stem cells treated with curcumin: an in vitro study.Molecular biology reports · 2022Article
- Self-assembly peptide PJournal of dentistry · 2022Article
- Promoting mineralization at biological interfacesMaterials today. Bio · 2022Article
- Leptin in Dental Pulp and Periapical Tissues: A Narrative Review.International journal of molecular sciences · 2022Review
- Mechanisms of Enamel Mineralization Guided by Amelogenin Nanoribbons.Journal of dental research · 2021Review
- Agarose-based spheroid culture enhanced stemness and promoted odontogenic differentiation potential of human dental follicle cells in vitro.In vitro cellular & developmental biology. Animal · 2021Article
- Redox Control of IL-6-Mediated Dental Pulp Stem-Cell Differentiation on Alginate/Hydroxyapatite Biocomposites for Bone Ingrowth.Nanomaterials (Basel, Switzerland) · 2019Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
The SIBLING (small integrin-binding ligand N-linked glycoproteins) family is the major group of noncollagenous proteins in bone and dentin. These extremely acidic and highly phosphorylated extracellular proteins play critical roles in the formation of collagenous mineralized tissues. Whereas the lack of individual SIBLINGs causes significant mineralization defects in vivo, none of them led to a complete cessation of mineralization suggesting that these proteins have overlapping functions. To assess whether different SIBLINGs regulate biomineralization in a similar manner and how phosphorylation impacts their activity, we studied the effects of two SIBLINGs, dentin matrix protein 1 (DMP1) and dentin phosphophoryn (DPP), on mineral morphology and organization in vitro. Our results demonstrate distinct differences in the effects of these proteins on mineralization. We show that phosphorylation has a profound effect on the regulation of mineralization by both proteins. Specifically, both phosphorylated proteins facilitated organized mineralization of collagen fibrils and phosphorylated DMP1-induced formation of organized mineral bundles in the absence of collagen. In summary, these results indicate that the primary structure and phosphorylation uniquely determine functions of individual SIBLINGs in regulation of mineral morphology and organization.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.