ArticleBiophysical journal2011
Study of receptor-chaperone interactions using the optical technique of spectroscopic ellipsometry.
Article in Biophysical journal, 2011. 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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
6 citing papers in PubMed.
- Review
- Review
- Ellipsometric-based novel DNA biosensor for label-free, real-time detection of Bordetella parapertussis.Journal of biological physics · 2019Article
- Analysis of Toxic Amyloid Fibril Interactions at Natively Derived Membranes by Ellipsometry.PloS one · 2015Article
- Quantification of interaction strengths between chaperones and tetratricopeptide repeat domain-containing membrane proteins.The Journal of biological chemistry · 2013Article
- Article
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
This work describes a detailed quantitative interaction study between the novel plastidial chaperone receptor OEP61 and isoforms of the chaperone types Hsp70 and Hsp90 using the optical method of total internal reflection ellipsometry (TIRE). The receptor OEP61 was electrostatically immobilized on a gold surface via an intermediate layer of polycations. The TIRE measurements allowed the evaluation of thickness changes in the adsorbed molecular layers as a result of chaperone binding to receptor proteins. Hsp70 chaperone isoforms but not Hsp90 were shown to be capable of binding OEP61. Dynamic TIRE measurements were carried out to evaluate the affinity constants of the above reactions and resulted in clear discrimination between specific and nonspecific binding of chaperones as well as differences in binding properties between the highly similar Hsp70 isoforms.
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Registered trials
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