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Nevertheless, the genetic and other evidence remains strong, if not overwhelming, that A\u03b2 is central to the disease process. Most attention has focused on the biosynthesis of A\u03b2 from its precursor protein through the successive actions of the \u03b2\u2010 and \u03b3\u2010secretases leading to the development of inhibitors of these membrane proteases. However, the levels of A\u03b2 are maintained through a balance of its biosynthesis and clearance, which occurs both through further proteolysis by a family of amyloid\u2010degrading enzymes (ADEs) and by a variety of transport processes. The development of late\u2010onset AD appears to arise from a failure of these clearance mechanisms rather than by overproduction of the peptide. This review focuses on the nature of these clearance mechanisms, particularly the various proteases known to be involved, and their regulation and potential as therapeutic targets in AD drug development. The majority of the ADEs are zinc metalloproteases [e.g., the neprilysin (NEP) family, insulin\u2010degrading enzyme, and angiotensin converting enzymes (ACE)]. Strategies for up\u2010regulating the expression and activity of these enzymes, such as genetic, epigenetic, stem cell technology, and other pharmacological approaches, will be highlighted. Modifiable physiological mechanisms affecting the efficiency of A\u03b2 clearance, including brain perfusion, obesity, diabetes, and sleep, will also be outlined. These new insights provide optimism for future therapeutic developments in AD research.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Linked Articles<\/jats:title>\n                    <jats:p>\n                      This article is part of a themed section on Therapeutics for Dementia and Alzheimer's Disease: New Directions for Precision Medicine. To view the other articles in this section visit\n                      <jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" xlink:href=\"http:\/\/onlinelibrary.wiley.com\/doi\/10.1111\/bph.v176.18\/issuetoc\">http:\/\/onlinelibrary.wiley.com\/doi\/10.1111\/bph.v176.18\/issuetoc<\/jats:ext-link>\n                    <\/jats:p>\n                  <\/jats:sec>","DOI":"10.1111\/bph.14593","type":"journal-article","created":{"date-parts":[[2019,2,2]],"date-time":"2019-02-02T04:23:50Z","timestamp":1549081430000},"page":"3447-3463","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":155,"title":["Targeting amyloid clearance in Alzheimer's disease as a therapeutic strategy"],"prefix":"10.1111","volume":"176","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-7134-3540","authenticated-orcid":false,"given":"Natalia N.","family":"Nalivaeva","sequence":"first","affiliation":[{"name":"School of Biomedical Sciences University of Leeds  Leeds UK"},{"name":"Laboratory of Physiology and Pathology of CNS I.M. 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