Proteases - invasion and more
Article Abstract:
Considerable progress is being made towards answering some questions about the importance of proteases and protease inhibitors in cancer biology. It is already known that interactions between tumour and stromal cells control the two protease systems that are behind most of the proteolysis outside the cell. It is believed that some proteases mainly affect tumour growth rather than invasion. The next generations of selective antagonists will be developed through identifying the most significant weapons at specific tumour sites.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1998
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Structure of the metal-ion-activated diphtheria toxin repressor/tox operator complex
Article Abstract:
The dimers of the repressor DtxR are arranged so that they are situated on almost opposite sites of the nucleic acid and have no interaction with each other. This is the only prokaryotic repressor identified so far for which two dimers that are structurally independent of each other bind to a target DNA. It is possible that a metal-ion-induced helix-to-coil structural transition in the amino-terminal region of the protein is partly the reason for the unique method of repressor activation by transition metal ions.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1998
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Proteases: to each his own
Article Abstract:
A protease or proteolytic enzyme has been discovered that processes the propeptide responsible for producing the cytokine interleukin-1 beta. This particular proteolytic activation helps to keep undesirable side reactions in check which might otherwise harm the cell by stimulating hazardous molecules. The enzyme was identified by two teams, N.A. Thornberry and colleagues and D.P. Cerretti and colleagues, who were hoping to find which enzymes were unique to which propeptide.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1992
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