I wish to post a minor correction to the this article. In the fifth paragraph of the introduction, a description of prior literature should be amended; these corrections do not affect the utility or understanding of the research that follows. The current and corrected paragraphs appear below.

Current paragraph:

A role for apoE in the metabolism of APP, or the presenilin-dependant proteolytic product, Aβ, was revealed when apoE-null mice expressing human APP that carries the 'Swedish' mutation (APPswe; K595M/N596L) had a reduced development of fibrillar amyloid plaques when compared to wild-type mice [10,11]. Furthermore, APPswe mice expressing apoE4 produced higher levels of soluble Aβ and developed fibrillar amyloid plaques at an earlier time point than those expressing apoE3 [12,13]. ApoE may further have distinct roles depending on whether it is expressed in neurons or glia, as the cellular origin of apoE differentially modifies amyloid pathology in mice, as well as responses to excitotoxicity [14,15].

Corrected paragraph (corrections are in italics):

A role for apoE in the metabolism of APP, or the presenilin-dependant proteolytic product, Aβ, was revealed when apoE-null mice expressing human APP that carries the Indiana mutation (APPind; V717) had a reduced development of fibrillar amyloid plaques when compared to wild-type mice [10,11]. Furthermore, mice expressing APPind, or APP that has both the APPind and 'Swedish' (APPswe; K595M/N596L) mutations expressing apoE4 produced higher levels of soluble Aβ and developed fibrillar amyloid plaques at an earlier time point than those expressing apoE3 [12,13]. ApoE may further have distinct roles depending on whether it is expressed in neurons or glia, as the cellular origin of apoE differentially modifies amyloid pathology in mice, as well as responses to excitotoxicity [14,15].