Evidence shows the polymicrobial etiology of endodontic infections, in which bacteria and
their products are the main agents for the development, progression, and dissemination of …

Research on matrix metalloproteinases (MMPs) and in particular on gelatinase B, alias MMP-
9, has grown exponentially in the decade 2003–2012. Structural details about flexibility of …

Most abundant in the extracellular matrix are collagens, joined by elastin that confers elastic
recoil to the lung, aorta, and skin. These fibrils are highly resistant to proteolysis but can …

The proteolytic processing of collagen (collagenolysis) is critical in development and
homeostasis, but also contributes to numerous pathologies. Mammalian interstitial …

Matrix metalloproteinases (MMP) are enzymes that degrade the extracellular matrix and
regulate essential normal cell behaviors. Inhibition of these enzymes has been a strategy for …

We investigated the use of amphiphilic, protease-cleavable peptides as encapsulation
moieties for hydrophobic metallodrugs, in order to enhance their bioavailability and …

Interstitial collagen mechanical and biological properties are altered by proteases that
catalyze the hydrolysis of the collagen triple-helical structure. Collagenolysis is critical in …

While commonly known for degradation of the extracellular matrix, matrix metalloproteinases
(MMPs) exhibit broad potential for use in targeting of bioactive and imaging agents in cancer …

Cancer is a complex disease that starts with mutations of key genes in one cell or a small
group of cells at a primary site in the body. If these cancer cells continue to grow successfully …

Membrane type-1 matrix metalloproteinase (MT1-MMP) is a promising drug target in
malignancy. The structure of MT1-MMP includes the hemopexin domain (PEX) that is distinct …