2012
DOI: 10.1038/ijos.2012.59
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A post-classical theory of enamel biomineralization… and why we need one

Abstract: Enamel crystals are unique in shape, orientation and organization. They are hundreds of thousands times longer than they are wide, run parallel to each other, are oriented with respect to the ameloblast membrane at the mineralization front and are organized into rod or interrod enamel. The classical theory of amelogenesis postulates that extracellular matrix proteins shape crystallites by specifically inhibiting ion deposition on the crystal sides, orient them by binding multiple crystallites and establish hig… Show more

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Cited by 94 publications
(95 citation statements)
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References 88 publications
(102 reference statements)
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“…In addition, the diffusion of mineral ions from the oral environment to the enamel may decrease with an increase in the distance from the enamel surface (Park et al, 2008b;Simmer et al, 2012) because the changes in the mineral contents in the middle and the inner enamel layers are not significant between the two age groups (p40.05). As a result, there is no obvious difference in the fracture toughness of the interior enamel layers between the old and the young age groups.…”
Section: Discussionmentioning
confidence: 99%
“…In addition, the diffusion of mineral ions from the oral environment to the enamel may decrease with an increase in the distance from the enamel surface (Park et al, 2008b;Simmer et al, 2012) because the changes in the mineral contents in the middle and the inner enamel layers are not significant between the two age groups (p40.05). As a result, there is no obvious difference in the fracture toughness of the interior enamel layers between the old and the young age groups.…”
Section: Discussionmentioning
confidence: 99%
“…The nanoglobules are thought to do so by preferentially attaching to the lateral surfaces of the initial crystals, believed to be crystalline octacalcium phosphates (OCP) (Moradian-Oldak et al 2000;Rauth et al 2009). However, it was proposed recently that the initial long crystallite ribbons in the secretory stage consist not of crystalline but amorphous calcium phosphates (ACP) and that adsorption of amelogenins followed rather than induced the shapes of the crystals (Simmer et al 2012). A second possible function of amelogenins is that they act as a buffer to neutralize the protons that are generated during crystal formation (Smith, 1998;Smith et al 2005).…”
Section: Introductionmentioning
confidence: 99%
“…During the secretion stage, ameloblasts secrete enamel matrix proteins (EMPs). These include amelogenin (AMEL), ameloblastin (AMBN), enamelin (ENAM), and matrix metalloproteinase 20, a calcium-dependent peptidase that cleaves newly secreted EMPs into various derivative fragments (Bartlett et al 2004;Simmer et al 2012). AMEL represents 90% of the matrix deposited, while AMBN and ENAM form the majority of the remaining 10% of the organic matrix.…”
Section: Introductionmentioning
confidence: 99%