ArticlePloS one2013
Solution structure and peptide binding of the PTB domain from the AIDA1 postsynaptic signaling scaffolding protein.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
6 citing papers in PubMed, 11 citations in OpenAlex.
- Comparative analysis reveals distinctive epigenetic features of the human cerebellum.PLoS genetics · 2021Article
- ThePharmacogenomics · 2019Review
- High resolution chromosomal microarray analysis in paediatric obsessive-compulsive disorder.BMC medical genomics · 2017Article
- Novel functions of CCM1 delimit the relationship of PTB/PH domains.Biochimica et biophysica acta. Proteins and proteomics · 2017Article
- Initial characterization of behavior and ketamine response in a mouse knockout of the post-synaptic effector gene Anks1b.Neuroscience letters · 2017Article
- Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
AIDA1 links persistent chemical signaling events occurring at the neuronal synapse with global changes in gene expression. Consistent with its role as a scaffolding protein, AIDA1 is composed of several protein-protein interaction domains. Here we report the NMR structure of the carboxy terminally located phosphotyrosine binding domain (PTB) that is common to all AIDA1 splice variants. A comprehensive survey of peptides identified a consensus sequence around an NxxY motif that is shared by a number of related neuronal signaling proteins. Using peptide arrays and fluorescence based assays, we determined that the AIDA1 PTB domain binds amyloid protein precursor (APP) in a similar manner to the X11/Mint PTB domain, albeit at reduced affinity (∼10 µM) that may allow AIDA1 to effectively sample APP, as well as other protein partners in a variety of cellular contexts.
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Registered trials
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