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首页> 外文期刊>European journal of oral sciences >Using the yeast two-hybrid assay to discover protein partners for the leucine-rich amelogenin peptide and for tuftelin-interacting protein 11.
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Using the yeast two-hybrid assay to discover protein partners for the leucine-rich amelogenin peptide and for tuftelin-interacting protein 11.

机译:使用酵母双杂交测定法发现富含亮氨酸的釉原蛋白肽和与图菲特林相互作用的蛋白11的蛋白伴侣。

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摘要

The established structural proteins of the enamel matrix are amelogenin, ameloblastin, and enamelin. Historically, tuftelin and tuftelin-interacting protein 11 (TFIP11) have also been discussed as possible enamel proteins. Protein complexes are achieved by protein-protein interactions, and it is protein complexes that control biomineralization. The purpose of our recent studies was to catalog protein partners for these proteins that are, or have been, implicated in tooth formation. We used the sensitive yeast two-hybrid assay to identify proteins that interact directly with amelogenin, ameloblastin, enamelin, the leucine-rich amelogenin peptide (LRAP) and TFIP11. In this manuscript we refer to, or document, potential protein partners for the proteins listed above. The yeast two-hybrid assay may ultimately prove to be a valuable proteomics methodology for using to decipher molecular events that ultimately result in enamel biomineralization.
机译:牙釉质基质的建立的结构蛋白是牙釉蛋白,成釉细胞蛋白和釉蛋白。历史上,也已经讨论了Tuftelin和Tuftelin相互作用蛋白11(TFIP11)作为可能的牙釉质蛋白。蛋白质复合物是通过蛋白质与蛋白质的相互作用而实现的,正是蛋白质复合物控制着生物矿化作用。我们最近的研究的目的是为已经或已经参与牙齿形成的这些蛋白质的蛋白质伴侣分类。我们使用了敏感的酵母双杂交测定法来鉴定与釉原蛋白,成釉细胞蛋白,enamelin,富含亮氨酸的釉原蛋白肽(LRAP)和TFIP11直接相互作用的蛋白质。在本手稿中,我们指的是或列出了上面列出的蛋白质的潜在蛋白质伴侣。酵母双杂交测定法可能最终被证明是一种有价值的蛋白质组学方法,可用于破译最终导致牙釉质生物矿化的分子事件。

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