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AlF<jats:sub>x<\/jats:sub> mimics a \u03b3-phosphate at its transition state in a G \u03b1 protein and is therefore able to inhibit its GTPase activity. AlF<jats:sub>x<\/jats:sub> also forms complexes with small GTP-binding proteins in the presence of their GTPase-activating proteins (GAP). As phosphate analogs, AlF<jats:sub>x<\/jats:sub> or BeF<jats:sub>x<\/jats:sub> affect the activity of a variety of phosphoryl transfer enzymes. Most of these enzymes are fundamentally important in cell signal transduction or energy metabolism. Al<jats:sup>3+<\/jats:sup> and F<jats:sup>-<\/jats:sup> tend to form stable complexes in aqueous solution. The exact structure and concentration of AlF<jats:sub>x<\/jats:sub> depend on the pH and the amount of F<jats:sup>-<\/jats:sup> and Al<jats:sup>3+<\/jats:sup> in the solution. Humans are exposed to both F and Al. It is possible that Al-F complexes may be formed in vivo, or formed in vitro prior to their intake by humans. Al-F complexes may play physiological or pathological roles in bone biology, fluorosis, neurotoxicity, and oral diseases such as dental caries and periodontal disease. 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