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Plays a role in the biomineralization of teeth.
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MMP20 (Montrer MMP20 Kits ELISA) in a common ancestor of tetrapods might have been recruited for the processing of AMEL and conserved over 350 million years of evolution.
Molecular dynamics simulations of the intrinsically disordered protein amelogenin have been reported.
Differences in the viscoelastic properties of phosphorylated amelogenin (P173) and recombinant non-phosphorylated amelogenin (rP172) in the adsorbed state were observed, consistent with noted differences in hydroxyapatite (HAP) binding.
The present study provides novel insights into the possible cooperation between enamelin (Montrer ENAM Kits ELISA) and amelogenin in macromolecular coassembly and in controlling enamel mineral formation.
The N-terminal domain of amelogenin may play a direct role in early stages of enamel formation.
Results confirm that the N- and C-termini of amelogenin are conformationally responsive and represent potential interactive sites for amelogenin-target interactions during enamel matrix mineralization.
PPII conformation plays an important role in amelogenin self-assembly and rP172 assembly is more favorable than rP148
Plays a role in the biomineralization of teeth. Seems to regulate the formation of crystallites during the secretory stage of tooth enamel development. Thought to play a major role in the structural organization and mineralization of developing enamel.
, amelogenin 173A
, amelogenin 173A/173B
, leucine-rich amelogenin peptide
, amelogenin (X chromosome)
, amelogenin, X-linked
, X-chromosomal amelogenin
, amelogenin (amelogenesis imperfecta 1, X-linked)
, amelogenin, X isoform
, class I amelogenin