ArticleGenomics, proteomics & bioinformatics2012
Novel adaptors of amyloid precursor protein intracellular domain and their functional implications.
Article in Genomics, proteomics & bioinformatics, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- Cellular levels of Grb2 and cytoskeleton stability are correlated in a neurodegenerative scenario.Disease models & mechanisms · 2017Article
- Clinical proteomics of enervated neurons.Clinical proteomics · 2016Review
- CSF proteomics of secondary phase spinal cord injury in human subjects: perturbed molecular pathways post injury.PloS one · 2014Article
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Authors and funding
2 authors.
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Abstract
Amyloid precursor protein intracellular domain (AICD) is one of the potential candidates in deciphering the complexity of Alzheimer's disease. It plays important roles in determining cell fate and neurodegeneration through its interactions with several adaptors. The presence or absence of phosphorylation at specific sites determines the choice of partners. In this study, we identified 20 novel AICD-interacting proteins by in vitro pull down experiments followed by 2D gel electrophoresis and MALDI-MS analysis. The identified proteins can be grouped into different functional classes including molecular chaperones, structural proteins, signaling and transport molecules, adaptors, motor proteins and apoptosis determinants. Interactions of nine proteins were further validated either by colocalization using confocal imaging or by co-immunoprecipitation followed by immunoblotting. The cellular functions of most of the proteins can be correlated with AD. Hence, illustration of their interactions with AICD may shed some light on the disease pathophysiology.
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