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Owing to their extended morphology, with axons in humans exceeding a meter in length, in addition to which they are not renewed but persist for the entire lifespan, it is no surprise that neurons are highly vulnerable to any perturbation of their sophisticated transport machinery. There is emerging evidence that impaired transport is not only causative for a range of motor disorders, but possibly also for Alzheimer's disease (AD) and related neurodegenerative disorders. Support for this hypothesis comes from transgenic animal models. Overexpression of human tau and amyloid precursor protein (APP) in mice and flies models the key hallmark histopathological characteristics of AD, such as somatodendritic accumulation of phosphorylated forms of tau and \u03b2\u2010amyloid (A\u03b2) peptide\u2010containing amyloid plaques, as well as axonopathy. The latter has also been demonstrated in mutant mice with altered levels of Alzheimer\u2010associated genes, such as <jats:italic>presenilin<\/jats:italic> (<jats:italic>PS<\/jats:italic>). In A\u03b2\u2010producing APP transgenic mice, axonopathy was observed before the onset of plaque formation and tau hyperphosphorylation. In human AD brain, an axonopathy was revealed for early but not late Braak stages. The overall picture is that key players in AD, such as tau, APP and PS, perturb axonal transport early on in AD, causing impaired synaptic plasticity and reducing survival rates. It will be challenging to determine the molecular mechanisms of these different axonopathies, as this might assist in the development of new therapeutic strategies.<\/jats:p>","DOI":"10.1111\/j.1471-4159.2006.03955.x","type":"journal-article","created":{"date-parts":[[2006,6,19]],"date-time":"2006-06-19T10:26:53Z","timestamp":1150712813000},"page":"993-1006","source":"Crossref","is-referenced-by-count":105,"title":["Do axonal defects in tau and amyloid precursor protein transgenic animals model axonopathy in Alzheimer's disease?"],"prefix":"10.1111","volume":"98","author":[{"given":"J\u00fcrgen","family":"G\u00f6tz","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lars M.","family":"Ittner","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Stefan","family":"Kins","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2006,6,19]]},"reference":[{"key":"e_1_2_11_2_1","doi-asserted-by":"publisher","DOI":"10.1083\/jcb.100.5.1736"},{"key":"e_1_2_11_3_1","doi-asserted-by":"crossref","first-page":"17\u2003427","DOI":"10.1016\/S0021-9258(19)85352-8","article-title":"Inhibition of kinesin synthesis and rapid anterograde axonal transport in vivo by an antisense oligonucleotide","volume":"268","author":"Amaratunga A.","year":"1993","journal-title":"J. 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