Mary J. Bossard

TL;DR: Cathepsin K may represent the elusive protease implicated in degradation of protein matrix during bone resorption and represents a novel molecular target in treatment of disease states associated with excessive bone loss such as osteoporosis.

TL;DR: In this article, the design and synthesis of high affinity FKBP12 ligands is described, which can inhibit the cis-trans-peptidylprolyl isomerase (rotamase) activity with an inhibition constant as low as 1 nM, yet they possess remarkable structural simplicity relative to FK506 and rapamycin.

TL;DR: Inhibitors of cathepsin K are effective at reducing osteoclast‐mediated bone resorption and may have therapeutic potential in diseases of excessive bone Resorption such as rheumatoid arthritis or osteoporosis.

TL;DR: Initial kinetic studies suggest the possibility of irreversible and reversible active-site modification in cathepsin K, a cysteine protease unique to osteoclasts, and promising leads for therapeutic agents for the treatment of osteoporosis.