The first matrix metalloproteinase (MMP) was discovered in 1962 from the tail of a tadpole by
its ability to degrade collagen. As their name suggests, matrix metalloproteinases are …

Simple Summary MMP9, due to its proteolytic activity, plays a key role in tumorigenesis by
regulating migration, epithelial-to-mesenchymal transition and survival of cancer cells …

Since the identification of matrix metalloproteinases (MMPs), a family of zinc-dependent
endopeptidases, as being a driving factor for cancer progression and patient prognosis …

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 …

Matrix metalloproteinases (MMPs), also designated matrixins, hydrolyze components of the
extracellular matrix. These proteinases play a central role in many biological processes …

Matrix metalloproteinases (MMPs) are a large family of enzymes that degrade the
extracellular matrix (ECM). Under pathologic conditions, overexpression of MMPs or …

Abstract Matrix metalloproteinase-2 (MMP-2) and matrix metalloproteinase-9 (MMP-9) are
collectively known as gelatinases whereas MMP-2 is gelatinase-A and MMP-9 is termed as …

The activity of matrix metalloproteinases (MMPs) is regulated at several levels, including
enzyme activation, inhibition, complex formation and compartmentalization. Regulation at …

The matrix metalloproteinases (MMP)-2 and-9, also known as the gelatinases have been
long recognized as major contributors to the proteolytic degradation of extracellular matrix …

Matrix metalloproteinases (MMPs) have been shown to be key players in both extracellular
matrix remodeling and cell migration during cancer metastasis. MMP-14, a membrane …