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Abstract The enzymes that hydrolyse peptide bonds, called peptidases or proteases, are very important to mankind and are also very numerous. The many scientists working on these enzymes are rapidly acquiring new data, and they need good methods to store it and retrieve it. The storage and...
Abstract The matrix metalloproteinases (MMPs) constitute a family of multidomain zinc endopeptidases with a metzincin-like catalytic domain, which are involved in extracellular matrix degradation but also in a number of other important biological processes. Under healthy conditions, their...
Abstract The abundance of mRNAs transcribed from human genes of the calpain superfamily was studied in 72 human tissues and cell types by the Human Multiple Tissue Expression (MTE™) Array technique. The analysis included the large subunits of u- and m-calpains, the small subunits, calpastatin...
Abstract Using UV laser cross-linking and immunoprecipitation we measured the in vivo binding of Arabidopsis heat shock transcription factor HSF1 to the promoters of target genes, Hsp18.2 and Hsp70. The amplification of promoter sequences, co-precipitated with HSF1-specific antibodies, indicated...
Abstract Identification of relevant substrates is essential for elucidation of in vivo functions of peptidases. The recent availability of the complete genome sequences of many eukaryotic organisms holds the promise of identifying specific peptidase substrates by systematic proteome analyses in...
Abstract Cathepsin K is a potent extracellular matrix-degrading protease that requires interactions with soluble glycosaminolycans for its collagenolytic activity in bone and cartilage. The major sources of glycosaminoglycans in cartilage are aggrecan aggregates. Therefore, we investigated...
Abstract Components of kinin-forming systems operating at inflammatory sites are likely to interact with elastase that is released by recruited neutrophils and may, at least temporarily, constitute the major proteolytic activity present at these sites. The aim of this work was to determine the...
Abstract Cathepsin B is a papain-family cysteine protease that is normally located in lysosomes, where it is involved in the turnover of proteins and plays various roles in maintaining the normal metabolism of cells. This protease has been implicated in pathological conditions, e.g., tumor...
Abstract We have previously reported that type V collagen is a poorly adhesive, anti-proliferative and motility-inhibitory substrate for the 8701-BC breast cancer cell line, which also triggers DNA fragmentation and impairs survival of the same cell line. In the present work we have extended to...
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