Results 181 to 190 of about 5,635 (209)
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On the formation of amelogenin microribbons
European Journal of Oral Sciences, 2006We recently reported the remarkable spontaneous self‐assembly and hierarchical organization of amelogenin ‘microribbons’ and their ability to facilitate oriented growth of apatite crystals in vitro. In a letter of correction we communicated the finding that the X‐ray diffraction pattern reported in our original report was that of cellulose contaminant ...
C. Du+2 more
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The International journal of developmental biology, 1995
Amelogenin is a major protein constituent of the developing enamel matrix. This protein is now well characterized from the data of amino acid sequences which have been shown to be at a high degree of homology between all species investigated to date.
Hitoyata Shimokawa, S Sasaki
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Amelogenin is a major protein constituent of the developing enamel matrix. This protein is now well characterized from the data of amino acid sequences which have been shown to be at a high degree of homology between all species investigated to date.
Hitoyata Shimokawa, S Sasaki
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Journal of Biochemistry, 2008
We previously demonstrated that the uptake of M180 amelogenin protein in dental epithelial cells (HAT-7) results in increased levels of amelogenin mRNA through enhanced mRNA stabilization. To determine the processes involved in the uptake of extracellular M180 amelogenin by cells and in amelogenin intracellular trafficking in the amelogenin protein ...
Hidemitsu Harada+2 more
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We previously demonstrated that the uptake of M180 amelogenin protein in dental epithelial cells (HAT-7) results in increased levels of amelogenin mRNA through enhanced mRNA stabilization. To determine the processes involved in the uptake of extracellular M180 amelogenin by cells and in amelogenin intracellular trafficking in the amelogenin protein ...
Hidemitsu Harada+2 more
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The Small Bovine Amelogenin LRAP Fails to Rescue the Amelogenin Null Phenotype
Calcified Tissue International, 2003Amelogenins are the most abundant secreted proteins in developing dental enamel. These evolutionarily-conserved proteins have important roles in enamel mineral formation, as mutations within the amelogenin gene coding region lead to defects in enamel thickness or mineral structure. Because of extensive alternative splicing of the primary RNA transcript
Marina D'Angelo+12 more
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Quantitative Analysis of Amelogenin Solubility
Journal of Dental Research, 1998Amelogenins are a group of extracellular enamel matrix proteins which are believed to be involved in the regulation of the size and habits of forming enamel crystals. The aim of this study was to compare the solubility properties of several amelogenins at various pH (from 4.0 to 9.0) at constant ionic strength (IS), and to examine the influence of ...
Janet Moradian-Oldak+4 more
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Molecular Evolution of Amelogenin in Mammals
Journal of Molecular Evolution, 2005An evolutionary analysis of mammalian amelogenin, the major protein of forming enamel, was conducted by comparison of 26 sequences (including 14 new ones) representative of the main mammalian lineages. Amelogenin shows highly conserved residues in the hydrophilic N- and C-terminal regions.
Jean-Yves Sire+2 more
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The amelogenin story: origin and evolution
European Journal of Oral Sciences, 2006Genome sequencing and gene mapping have permitted the identification of HEVIN (SPARC‐Like1) as the probable ancestor of the enamel matrix proteins (EMPs), amelogenin (AMEL), ameloblastin (AMBN) and enamelin (ENAM). We have undertaken a phylogenetic analysis to elucidate their relationships.
Sidney Delgado+2 more
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Amelogenin is a Cell Adhesion Protein
Journal of Dental Research, 2002Amelogenin, the major protein component of tooth enamel, is shown to be a cell adhesion protein. Since it had been shown that an amelogenin-containing preparation, Emdogain®, possessed cell-adhesive activity, we tested the hypothesis that amelogenin was responsible for cell-adhesive activity.
Robert J. Klebe+5 more
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Alternative Splicing of Amelogenins
Connective Tissue Research, 1995Amelogenins comprise as much as 90% of the protein in the developing enamel matrix. Separating amelogenins by gel electrophoresis reveals a complex of polypeptides with apparent mobilities ranging from low molecular weight species on up to 28,000 Daltons.
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Microstructures of an Amelogenin Gel Matrix
Journal of Structural Biology, 1999The thermo-reversible transition (clear opaque) of the amelogenin gel matrix, which has been known for some three decades, has now been clarified by microstructural investigations. A mixed amelogenin preparation extracted from porcine developing enamel matrix (containing "25K," 7.4%; "23K," 10.7%; "20K," 49.5%; and smaller peptides, 32.4%) was ...
Janet Moradian-Oldak+4 more
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