ArticleBiomolecular NMR assignments2012
Backbone and side chain NMR assignments for the intrinsically disordered cytoplasmic domain of human neuroligin-3.
Article in Biomolecular NMR assignments, 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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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
3 citing papers in PubMed, 7 citations in OpenAlex.
- There is Diversity in Disorder-"In all Chaos there is a Cosmos, in all Disorder a Secret Order".Frontiers in molecular biosciences · 2016Article
- VirtualSpectrum, a tool for simulating peak list for multi-dimensional NMR spectra.Journal of biomolecular NMR · 2014Article
- Conformational distributions of denatured and unstructured proteins are similar to those of 20 × 20 blocked dipeptides.Journal of biomolecular NMR · 2012Article
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Authors and funding
8 authors at 3 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Neuroligins act as heterophilic adhesion molecules at neuronal synapses. Their cytoplasmic domains interact with synaptic scaffolding proteins, and have been shown to be intrinsically disordered. Here we report the backbone and side chain (1)H, (13)C and (15)N resonance assignments for the cytoplasmic domain of human neuroligin 3.
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