ArticleJournal of biomolecular NMR2011
Kinetic analysis of protein aggregation monitored by real-time 2D solid-state NMR spectroscopy.
Article in Journal of biomolecular NMR, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 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
3 citing papers in PubMed.
- Article
- A Split Transcriptional Repressor That Links Protein Solubility to an Orthogonal Genetic Circuit.ACS synthetic biology · 2018Article
- Quantitative analysis of α-synuclein solubility in living cells using split GFP complementation.PloS one · 2012Article
Corrections and comments
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Authors and funding
3 authors.
Funding
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Abstract
It is shown that real-time 2D solid-state NMR can be used to obtain kinetic and structural information about the process of protein aggregation. In addition to the incorporation of kinetic information involving intermediate states, this approach can offer atom-specific resolution for all detectable species. The analysis was carried out using experimental data obtained during aggregation of the 10.4 kDa Crh protein, which has been shown to involve a partially unfolded intermediate state prior to aggregation. Based on a single real-time 2D (13)C-(13)C transition spectrum, kinetic information about the refolding and aggregation step could be extracted. In addition, structural rearrangements associated with refolding are estimated and several different aggregation scenarios were compared to the experimental data.
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Registered trials
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