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 …

The extracellular matrix (ECM) is a macromolecules network, in which the most abundant
molecule is collagen. This protein in triple helical conformation is highly resistant to …

Matrix metalloproteinases (MMPs), also called matrixins, function in the extracellular
environment of cells and degrade both matrix and non-matrix proteins. They play central …

Matrix metalloproteinases (MMPs), also designated matnxms, are a family of related zinc
metalloendopeptidases that function in the turnover of components of the extracellular …

The field of bioinorganic chemistry is at a propitious stage of development. Ever more
complex metallobiomolecules are isolated and purified, physical methodologies and …

Zinc is required for the activity of> 300 enzymes, covering all six classes of enzymes. Zinc
binding sites in proteins are often distorted tetrahedral or trigonal bipyramidal geometry …

Matrix metalloproteinases (MMPs) are a large family of calcium-dependent zinc-containing
endopeptidases, which are responsible for the tissue remodeling and degradation of the …

It is 40 years since the first member of what came to be known as the matrix
metalloproteinase (MMP) family was described. Structural, molecular and biochemical …

Posters and lectures presented at the Seventh International Conference on Bioinorganic
Chemistry (ICBIC) in Lubeck, Germany, last year was divided into 16 sections, including …

Zinc is known to be indispensable to growth and development and transmission of the
genetic message. It does this through a remarkable mosaic of zinc binding motifs that …