anti-Amelogenin, X-Linked (AMELX) Antibodies

Human Amelogenin, X-Linked (AMELX) interaction partners

1. High AMEL expression is associated with Aggressiveness in Odontogenic Tumors.

2. Single nucleotide polymorphisms in the AMELX and AMBN genes may be genetic variants that contribute to developmental defects of enamel in primary dentition of Polish children.

3. To the best of our knowledge, this is the first report of expression of human amelogenin in plants, offering the possibility to use this plant-made protein for nanotechnological applications.

4. The calcium level was associated with genetic variations in AMELX, AMNB and ESRRB. AMELX and AMNB are involved in enamel mineralization. Mutations in both these genes are responsible for the amelogenesis imperfecta phenotype (OMIN), which supports their link with enamel alterations as well as enamel mineralization.

5. a single-nucleotide polymorphism in the amelogenin gene using amplified product-length polymorphisms in combination with sex-determining region Y analysis, is reported.

6. Full-length amelogenin may have a negative mitogenic impact on human dental pulp stem cells.

7. suggestive overrepresentation of TT genotype of amelogenin marker in cases w/severe erosion when compared to no dentine erosion. Amelogenin also associated with severe erosion in recessive model; TT genotype significantly more frequent in affected group

8. Studies indicate that a single point mutation (41Pro-->Thr) in the amelogenin gene causes severe dental enamel malformation known as amelogenesis imperfect.

9. sequencing data showed presence of mutation. Samples showing mutation (43.3%) showed high correlation with caries (80.7%) experience which was statistically significant.

10. silent mutation in exon 4 of AMELX gene. generating and characterizing transgenic animal model, alteration of the ratio and quantity of the developmentally conserved alternative splicing repertoire of AMELX caused defects in enamel matrix mineralization.

11. Conversion to amelogenin expressing dental epithelial cells involved an up-regulation of the stem cell marker Sox2 and proliferation genes and decreased expression of mesenchymal markers

12. the interaction of amelogenin with Grp78/Bip contributed to cell proliferation, rather than correlate with the osteogenic differentiation

13. demonstrate the presence of copy number variations in regions containing 9 of the 13 CODIS(Combined DNA Index System) short tandem repeat(STR) and AMELX/Y loci

14. Associations between TFIP11 (p=0.02), ENAM (p=0.00001), and AMELX (p=0.01) could be seen with caries independent of having MIH or genomic DNA copies of Streptococcus mutans detected by real time PCR in the Brazilian sample.

15. The 21 non-CODIS STR loci of the Russian ethnic minority group were characterized by high genetic diversity and therefore may be useful for elucidating the population's genetic background, for individual identification.

16. Deletion of AMELX results in males with a characteristic snow-capped enamel phenotype.

17. Evolutionary and statistical analyses showed that none of the SNPs identified in this study were associated with caries susceptibility, suggesting that AMELX is not a gene candidate in our studied population.

18. These results suggest that SNPs of AMELX might be associated with dental caries susceptibility in Korean population.

19. A single Pro-70 to Thr (p.P70T) mutation of amelogenin affected the self-assembly and adsorption behaviour of amelogenin, resulting in increased binding to apatite and inhibited crystal growth.

20. These results suggest that hAm may be a key element in regulating hBMSCs osteogenic differentiation.

Xenopus laevis Amelogenin, X-Linked (AMELX) interaction partners

1. MMP20 in a common ancestor of tetrapods might have been recruited for the processing of AMEL and conserved over 350 million years of evolution.

Mouse (Murine) Amelogenin, X-Linked (AMELX) interaction partners

1. The maxillary incisors of Amelx-/- mutants indicated the increase of the frequency and number of labial grooves with aging.

2. Results provide evidence that all three regions of amelogenin (N-terminus, C-terminus, central core) are required for enamel formation and structure.

3. an involvement of LRAP in lipid-raft-dependent signaling pathways are mediated by flotillin-1.

4. transcriptional activation of Amelx was associated with enhanced osteogenic differentiation, especially in the early stage of biomineralization

5. LRAP is primarily monomeric in solution, suggesting that the monomeric species may be an important functional form of some amelogenins.

6. AMELX may function as a growth factor-like molecules solubilized in the aqueous microenvironment. In jaws, it might play some role in bone physiology through autocrine/paracrine pathways, particularly during development and stress-induced remodeling.

7. temporal/spatial localization of amelogenins with exon4 peptide and functional differences in HAP binding suggests unique properties of amelogenins containing exon4 cause specific enhancement of biomineralization of early-formed HAP at maturation stage

8. Conversion to amelogenin expressing dental epithelial cells involved an up-regulation of the stem cell marker Sox2 and proliferation genes and decreased expression of mesenchymal markers

9. Leucine rich amelogenin peptide alters ameloblast differentiation in vivo.

10. the interaction of amelogenin with Grp78/Bip contributed to cell proliferation, rather than correlate with the osteogenic differentiation

11. among amelogenins, M180 alone is sufficient for normal enamel mechanical properties and prism patterns, but that additional amelogenin splice products are required to restore enamel thickness.

12. ERP expression follows defined developmental profiles; affects osteoblast differentiation, mineralization, calvarial bone development. with role in developing enamel matrix, ERPs retain conserved function related to bone biomineralization.

13. The study investigates the structure, orientation, and dynamics of three regions in the N-terminus of the protein: L(15) to V(19), V(19) to L(23), and K(24) to S(28). Phosphorylation and ionic strength alter the LRAP-hydroxyapatite interface.

14. Analyses of these data suggest that MMP-9 may be involved in controlling amelogenin processing and enamel formation.

15. Amelogenin affected mandible morphology and incisor enamel formation, while enamelin only affected incisors, supporting the multifunctional role of amelogenin.

16. analysis of daily rhythms of clock genes and Amelx in murine ameloblast cells

17. Amelogenin molecules form complex 3D-structures with N-terminal alpha-helix-like segments and C-terminal PPII-helices.

18. Alterations in the assembly (i.e. premature aggregation) of mutant amelogenins may have a profound effect on intra- and extracellular processes.

19. Amelogenin assembly is a multistep hierarchical process and provides new insight into the control of enamel mineralization.

20. Amelogenin promotes odontoblast-like MDPC-23 cell differentiation