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N and ameloblastin co-localized near the secretory face of ameloblasts at the earliest stages of their formation; with maturation, ameloblastin was lost from the enamel surface. Additionally, they found using circular dichroism, that amelogenin and ameloblastin could form stable complexes. C-terminal polypeptides of ameloblastin were cleaved into smaller peptides and lost from the extracellular ma
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Omplex process in which large mineral (HA) crystals are formed as the organic matrix is removed, is similarly dependent on IDPs. Janet Moradian-Oldak and her collaborators John Evans and Wendy Shaw investigated the secondary structure of amelogenin and ameloblastin, two major enamel proteins. Both were shown to be IDPs [43,44], their binding partners were other IDPs (enamelin and tuftelin) and HA.
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N and ameloblastin co-localized near the secretory face of ameloblasts at the earliest stages of their formation; with maturation, ameloblastin was lost from the enamel surface. Additionally, they found using circular dichroism, that amelogenin and ameloblastin could form stable complexes. C-terminal polypeptides of ameloblastin were cleaved into smaller peptides and lost from the extracellular ma
1
N and ameloblastin co-localized near the secretory face of ameloblasts at the earliest stages of their formation; with maturation, ameloblastin was lost from the enamel surface. Additionally, they found using circular dichroism, that amelogenin and ameloblastin could form stable complexes. C-terminal polypeptides of ameloblastin were cleaved into smaller peptides and lost from the extracellular ma
1
N and ameloblastin co-localized near the secretory face of ameloblasts at the earliest stages of their formation; with maturation, ameloblastin was lost from the enamel surface. Additionally, they found using circular dichroism, that amelogenin and ameloblastin could form stable complexes. C-terminal polypeptides of ameloblastin were cleaved into smaller peptides and lost from the extracellular ma
1
N and ameloblastin co-localized near the secretory face of ameloblasts at the earliest stages of their formation; with maturation, ameloblastin was lost from the enamel surface. Additionally, they found using circular dichroism, that amelogenin and ameloblastin could form stable complexes. C-terminal polypeptides of ameloblastin were cleaved into smaller peptides and lost from the extracellular ma
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S by enzymes, e.g., enamelysin (matrix metalloproteinase 20, Mmp-20) and kallikrein 4 [49]. The ways in which these proteins guide the formation of HA in enamel is unknown. There are, however, some important clues from recent studies. In the teeth of mice that produce a truncated form of ameloblastin, enamel fails to appear [50,51]. These mice also have reduced expression of amelogenin with no app
1
S by enzymes, e.g., enamelysin (matrix metalloproteinase 20, Mmp-20) and kallikrein 4 [49]. The ways in which these proteins guide the formation of HA in enamel is unknown. There are, however, some important clues from recent studies. In the teeth of mice that produce a truncated form of ameloblastin, enamel fails to appear [50,51]. These mice also have reduced expression of amelogenin with no app