{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,25]],"date-time":"2026-09-25T17:07:42Z","timestamp":1790356062998,"version":"4.1.0"},"reference-count":113,"publisher":"Wiley","issue":"4","license":[{"start":{"date-parts":[[2019,12,9]],"date-time":"2019-12-09T00:00:00Z","timestamp":1575849600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":["febs.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["The FEBS Journal"],"published-print":{"date-parts":[[2020,2]]},"abstract":"<jats:p>\n                    The accumulation of amyloid\u2010\u03b2 (A\u03b2) peptides is a key histopathological feature of the Alzheimer's brain. Defective clearance mechanisms result in toxic levels of soluble A\u03b2\n                    <jats:sub>40<\/jats:sub>\n                    and A\u03b2\n                    <jats:sub>42<\/jats:sub>\n                    oligomers, leading to impaired synaptic function, neurodegeneration and cognitive decline. Growing evidence points to the involvement of P\u2010glycoprotein (P\u2010gp or ABCB1), an ATP\u2010binding cassette transporter highly expressed on the luminal side of the blood\u2013brain barrier, in facilitating the clearance of A\u03b2 from the brain. In this review, we summarise evidence from human, animal and\n                    <jats:italic>in\u00a0vitro<\/jats:italic>\n                    studies examining the contribution of P\u2010gp to A\u03b2 clearance, and discuss the potential for P\u2010gp as a novel pharmacological target in Alzheimer's disease (AD). P\u2010gp expression and activity in the brain are inversely correlated with ageing, A\u03b2 deposition and AD. Moreover, A\u03b2 itself has been found to compromise the expression of P\u2010gp, thereby exacerbating A\u03b2 deposition and disease. Despite decades of research, the pathophysiology of AD remains elusive. Understanding the normal versus impaired processing and clearance mechanisms affecting A\u03b2 peptides will assist the development of more effective therapeutic agents to combat this progressive neurodegenerative condition that continues to devastate millions of patients globally.\n                  <\/jats:p>","DOI":"10.1111\/febs.15148","type":"journal-article","created":{"date-parts":[[2019,11,21]],"date-time":"2019-11-21T09:57:00Z","timestamp":1574330220000},"page":"612-625","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":92,"title":["P\u2010glycoprotein: a role in the export of amyloid\u2010\u03b2 in Alzheimer's disease?"],"prefix":"10.1111","volume":"287","author":[{"given":"Amanda B.","family":"Chai","sequence":"first","affiliation":[{"name":"School of Pharmacy Faculty of Medicine and Health University of Sydney Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gavin K. 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