The carboxyl-terminal domain of phosphophoryn contains unique extended triplet amino acid repeat sequences forming ordered carboxyl-phosphate interaction ridges that may be essential in the biomineralization process.

The carboxyl-terminal domain of phosphophoryn contains unique extended triplet amino acid repeat sequences forming ordered carboxyl-phosphate interaction ridges that may be essential in the biomineralization process.

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http://www.wikidata.org/entity/Q36836757

Q36836757

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Dentin Matrix Proteins in Bone Tissue Engineering The expression of dentin sialophosphoprotein gene in bone Proteolytic processing of dentin sialophosphoprotein (DSPP) is essential to dentinogenesis Biomineralization mechanisms: a new paradigm for crystal nucleation in organic matrices.Identification and characterization of the carboxyl-terminal region of rat dentin sialoprotein.N-terminal sequence analysis of bovine dentin phosphophoryn after conversion of phosphoseryl to S-propylcysteinyl residues.Genomic organization, chromosomal mapping, and promoter analysis of the mouse dentin sialophosphoprotein (Dspp) gene, which codes for both dentin sialoprotein and dentin phosphoprotein.Characterization of porcine dentin sialoprotein (DSP) and dentin sialophosphoprotein (DSPP) cDNA clones.Echinoderm phosphorylated matrix proteins UTMP16 and UTMP19 have different functions in sea urchin tooth mineralization.Engineering gene expression and protein synthesis by modulation of nuclear shape.Bone regeneration mediated by biomimetic mineralization of a nanofiber matrix.Self-assembly of peptide amphiphiles: from molecules to nanostructures to biomaterials Dentin sialophosphoprotein in biomineralization Phosphorylation of the proteins of the extracellular matrix of mineralized tissues by casein kinase-like activity.Cement proteins of the tube-building polychaete Phragmatopoma californica.A comparative study of zwitterionic ligands-mediated mineralization and the potential of mineralized zwitterionic matrices for bone tissue engineering.Enzyme Directed Templating of Artificial Bone Mineral.Biomimetic systems for hydroxyapatite mineralization inspired by bone and enamel.Differentiation of embryonic mesenchymal cells to odontoblast-like cells by overexpression of dentin matrix protein 1.Ca(2+)-induced self-assembly of Bombyx mori silk sericin into a nanofibrous network-like protein matrix for directing controlled nucleation of hydroxylapatite nano-needles.Expression of dentin sialophosphoprotein in non-mineralized tissues.Dentin phosphoprotein (DPP) activates integrin-mediated anchorage-dependent signals in undifferentiated mesenchymal cells.Disorders of human dentin Preferential sites for intramolecular glucosepane cross-link formation in type I collagen: A thermodynamic study.Dspp mutations disrupt mineralization homeostasis during odontoblast differentiation.Changes in matrix phosphorylation during bovine dentin development Sulfobetaine as a zwitterionic mediator for 3D hydroxyapatite mineralization Gene evolution and functions of extracellular matrix proteins in teeth Acidic domain in dentin phosphophoryn facilitates cellular uptake: implications in targeted protein delivery.Emerging peptide nanomedicine to regenerate tissues and organs.Biomimetic self-assembling peptides as injectable scaffolds for hard tissue engineering.Porcine dentin sialophosphoprotein: length polymorphisms, glycosylation, phosphorylation, and stability.Phosphorylated proteins and control over apatite nucleation, crystal growth, and inhibition.Hereditary dentine disorders: dentinogenesis imperfecta and dentine dysplasia.Supramolecular Nanofibers of Peptide Amphiphiles for Medicine.Association of calcium and phosphate ions with collagen in the mineralization of vertebrate tissues.Multifunctional ECM proteins in bone and teeth.Induction of reparative dentin formation on exposed dental pulp by dentin phosphophoryn/collagen composite.Odontoblast cells immortalized by telomerase produce mineralized dentin-like tissue both in vitro and in vivo.Effects on Hardness and Elastic Modulus for DSS-8 Peptide Treatment on Remineralization of Human Dental Tissues.

P2860

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P2860

The carboxyl-terminal domain of phosphophoryn contains unique extended triplet amino acid repeat sequences forming ordered carboxyl-phosphate interaction ridges that may be essential in the biomineralization process.

Item

http://www.wikidata.org/entity/Q36836757

description

1996 nî lūn-bûn

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1996年の論文

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1996年論文

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1996年論文

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1996年論文

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1996年論文

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1996年論文

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1996年论文

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1996年论文

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1996年论文

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name

The carboxyl-terminal domain o ...... the biomineralization process.

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The carboxyl-terminal domain o ...... the biomineralization process.

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prefLabel

The carboxyl-terminal domain o ...... the biomineralization process.

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P1476

The carboxyl-terminal domain o ...... the biomineralization process.

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P2093

Bannon L

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Copeland NG

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Dillon JW

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George A

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Gilbert DJ

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Jenkins NA

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Malone J

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Sabsay B

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Veis A

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P2860

Mapping of the human dentin matrix acidic phosphoprotein gene (DMP1) to the dentinogenesis imperfecta type II critical region at chromosome 4q21

Genomic organization of the human osteopontin gene: exclusion of the locus from a causative role in the pathogenesis of dentinogenesis imperfecta type II

An immunocytochemical study of the routes of secretion of collagen and phosphophoryn from odontoblasts into dentin

Innovative materials processing strategies: a biomimetic approach.

Domain structure and sequence distribution in dentin phosphophoryn.

Development and applications of a molecular genetic linkage map of the mouse genome.

The development of sequence-tagged sites for human chromosome 4.

Hierarchical control of lymphocyte survival.

Type I collagen shows a specific binding affinity for bovine dentin phosphophoryn.

Characteristics of phosphorylated and non-phosphorylated dentine phosphoprotein

P304

32869-32873

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scholarly article

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10.1074/JBC.271.51.32869

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English

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271

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1996-12-01T00:00:00Z

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14252653

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8955126

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P921

biomineralization

The carboxyl-terminal domain of phosphophoryn contains unique extended triplet amino acid repeat sequences forming ordered carboxyl-phosphate interaction ridges that may be essential in the biomineralization process.

about

P2860

P2860

The carboxyl-terminal domain of phosphophoryn contains unique extended triplet amino acid repeat sequences forming ordered carboxyl-phosphate interaction ridges that may be essential in the biomineralization process.

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P2860

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P921