. The temporal localization of frame-shift ubiquitin-B and amyloid precursor protein, and complement proteins in the brain of non-demented control patients with increasing Alzheimer's disease pathology. Neurosci Lett. 2003 Sep 4;348(1):46-50. PubMed.

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  1. Currently there are around 20 different putative contributors related to the neuropathogenesis of Alzheimer’s disease (see ARF Current Hypotheses). In the paper by Konishi, et al., two of them are linked, i.e., frameshift and complement proteins. Several years ago, in discussions with Piet Eikelenboom (see Eikelenboom et al., 2002), we anticipated that frameshift proteins would show up earlier in postmortem material than complement proteins; aberrant proteins that can be the result of proteasome inhibition by UBB+1 (see Lindsten et al., 2002) may somehow give rise to an immune response. This idea has been worked out in the present paper, and has indeed been confirmed. It will be interesting to see if more attempts such as this (if possible, and not only in postmortem tissue!) will be made.

    References:

    . Neuroinflammation in Alzheimer's disease and prion disease. Glia. 2002 Nov;40(2):232-9. PubMed.

    . Mutant ubiquitin found in neurodegenerative disorders is a ubiquitin fusion degradation substrate that blocks proteasomal degradation. J Cell Biol. 2002 Apr 29;157(3):417-27. PubMed.