The DOI matches its Crossref record; 27 of the 27 references it cites were found in a registry or an index.
Determination of half-maximal inhibitory concentration using biosensor-based protein interaction analysis
Open accessAbstract
The half-maximal inhibitory concentration (IC50) is the most widely used and informative measure of a drug’s efficacy. It indicates how much drug is needed to inhibit a biological process by half, thus providing a measure of potency of an antagonist drug in pharmacological research. Most approaches to determine IC50 of a pharmacological compound are based on assays that utilize whole cell systems. While they generally provide outstanding potency information, results can depend on the experimental cell line used and may not differentiate a compound’s ability to inhibit specific interactions. Here we show using the secreted Transforming Growth Factor-β (TGF-β) family ligand BMP-4 and its receptors as example that surface plasmon resonance can be used to accurately determine IC50 values of individual ligand-receptor pairings. The molecular resolution achievable with this approach can help distinguish inhibitors that specifically target individual complexes, or that can inhibit multiple functional interactions at the same time.
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Therapeutic antibodies: successes, limitations and hopes for the future
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Survey of the year 2003 commercial optical biosensor literature
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Metadata
- Authors
- Aykul, S., & Martinez-Hackert, E.
- Venue
- Analytical Biochemistry
- Publisher
- Elsevier BV
- Published
- 2016-09
- Volume
- 508
- Pages
- 97-103
- ISSN
- 0003-2697 (ISSN-L)
- OpenAlex
- W2471711949
- Cited by
- 284
- References
- 27
- FWCI
- 2.86
- Type
- journal article
- Language
- en
- Open access
- green
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
