期刊
NEUROCHEMISTRY INTERNATIONAL
卷 52, 期 6, 页码 1030-1036出版社
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.neuint.2007.10.020
关键词
amyloid-beta peptide; phage displayed cDNA library; microtubule-associated protein 1B (MAP1B)
资金
- NIA NIH HHS [R21 AG023534-01, AG-20241, R01 AG020241, R21 AG023534, AG 023534, R21 AG023534-02] Funding Source: Medline
- NINDS NIH HHS [R01 NS050895, NS-050895] Funding Source: Medline
Extracellular and intraneuronal formation of amyloid-beta aggregates have been demonstrated to be involved in the pathogenesis of Alzheimer's disease. However, the precise mechanism of amyloid-beta neurotoxicity is not completely understood. Previous studies suggest that binding of amyloid-beta to a number of targets have deleterious effects on cellular functions. In the present study we have shown for the first time that amyloid-beta 1-42 bound to a peptide comprising The microtubule binding domain of the heavy chain of microtubule-associated protein 1B by the screening of a human brain cDNA library expressed on M13 phage. This interaction may explain, in part, the loss of neuronal cytoskeletal integrity, impairment of microtubule-dependent transport and synaptic dysfunction observed previously in Alzheimer's disease. (C) 2007 Elsevier Ltd. All rights reserved.
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