The October report in Science by Vassar and colleagues idetifying β-secretase, (see below) has now been followed up by three more reports this month identifying the BACE enzyme (or ASP2, as it has been termed by two of the groups)-one in the online journal Molecular and Cellular Neuroscience and two in Nature. Writing a News and Views article in Nature, Bart De Strooper and Gerhard Koenig welcome the new reports because the researchers took varied paths to get to the same point, helping to confirm the earlier reported results. For example, Yan and colleagues scanned the C elegans genome for aspartyl-protease-like gene products and then looked in the vertebrate genome for homologues of the proteases they had found. Sinha and colleagues took a classical protein fractionation approach to arrive at the same molecule, designing a transition state analogue that could "hook" or "freeze" the BACE molecule in the act of cleaving its substrate.—Hakon Heimer


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Primary Papers

  1. . Identification of a novel aspartic protease (Asp 2) as beta-secretase. Mol Cell Neurosci. 1999 Dec;14(6):419-27. PubMed.
  2. . Membrane-anchored aspartyl protease with Alzheimer's disease beta-secretase activity. Nature. 1999 Dec 2;402(6761):533-7. PubMed.
  3. . Purification and cloning of amyloid precursor protein beta-secretase from human brain. Nature. 1999 Dec 2;402(6761):537-40. PubMed.
  4. . Alzheimer's disease. A firm base for drug development. Nature. 1999 Dec 2;402(6761):471-2. PubMed.