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divides mutations that precipitate attacks of AIP into three broad groups according to their molecular basis.[41] Mutations that affect protein folding and stability, including mutations that occur in the hydrophobic core, in tight turns, and other conformationally restricted areas, typically resulting in aberrantly folded or unstable protein that is rapidly degraded in vivo .[41] Mutations that affect binding, reaction, and assembly of cofactor precursor preuroporphyrinogen (1-hydroxxymethyllbilane).[41] Mutations that affect the catalytic or substrate-binding residues resulting in a properly folded but inactive enzyme

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The compound binds to growth hormone receptors and triggers fibroblast proliferation, accelerating collagen production at injury sites