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 PMID:17183681  

Physiological mouse brain Abeta levels are not related to the phosphorylation state of threonine-668 of Alzheimer's APP.

Yoshitake Sano | Tadashi Nakaya | Steve Pedrini | Shizu Takeda | Kanae Iijima-Ando | Koichi Iijima | Paul M Mathews | Shigeyoshi Itohara | Sam Gandy | Toshiharu Suzuki
PloS one | 2006

Amyloid-beta peptide species ending at positions 40 and 42 (Abeta40, Abeta42) are generated by the proteolytic processing of the Alzheimer's amyloid precursor protein (APP). Abeta peptides accumulate in the brain early in the course of Alzheimer's disease (AD), especially Abeta42. The cytoplasmic domain of APP regulates intracellular trafficking and metabolism of APP and its carboxyl-terminal fragments (CTFalpha, CTFbeta). The role of protein phosphorylation in general, and that of the phosphorylation state of APP at threonine-668 (Thr668) in particular, has been investigated in detail by several laboratories (including our own). Some investigators have recently proposed that the phosphorylation state of Thr668 plays a pivotal role in governing brain Abeta levels, prompting the current study.

Pubmed ID: 17183681

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Associated grants

  • Agency: NINDS NIH HHS, United States
    Id: R01 NS041017
  • Agency: NINDS NIH HHS, United States
    Id: NS45357
  • Agency: NINDS NIH HHS, United States
    Id: NS41017
  • Agency: NIA NIH HHS, United States
    Id: AG010491
  • Agency: NIA NIH HHS, United States
    Id: R01 AG023611
  • Agency: NINDS NIH HHS, United States
    Id: R21 NS045357
  • Agency: NIA NIH HHS, United States
    Id: P01 AG010491-14
  • Agency: NIA NIH HHS, United States
    Id: P01 AG010491
  • Agency: NIA NIH HHS, United States
    Id: AG023611

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Progen (tool)

RRID:SCR_006726

Antibody and density gradient media supplier.

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C57BL/6J (tool)

RRID:IMSR_JAX:000664

Mus musculus with name C57BL/6J from IMSR.

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