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Fluoride helps prevent dental decay by binding to the hydroxyapatite crystals in enamel.
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Hydroxyapatite precipitation in soft tissue is linked to cell death and membrane particle formation and binding to the extracellular matrix.
Due to their structural similarity to pyrophosphate, a normal component of bone matrix, they are integrated in the bone matrix by binding to hydroxyapatite crystals, resulting in inhibition of osteoclast-mediated bone resorption.
These drugs act at the site of active bone remodeling by binding to hydroxyapatite, inhibiting osteoclast development and migratory activity.
The increase in uptake of 99mTc-PyP is likely to come from its binding to hydroxyapatite crystals in damaged myocytes as well as its uptake in macrophages coordinating the clearance of damaged tissue.
Their binding to hydroxyapatite was measured in vitro.
Bisphosphonates localize to bone by mimicking pyrophosphate and binding to hydroxyapatite in mineralized bone.
Statherin has a particular affinity to the hydroxyapatite surfaces due to the presence of Ca2+ binding domains.
The hydroxyapatite DCFGP group was significantly (p < 0.05) superior to the hydroxyapatite and DCFGP groups.
The binding affinity to hydroxyapatite determines attachment to bone and duration of effect, and the inhibition of FPP synthase determines antiresorptive potential.
It has the highest binding affinity to hydroxyapatite and the highest skeletal uptake 68 and is the most potent osteoclast inhibitor.
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