Flavonoids inhibit the amidolytic activity of human thrombin
Biochimie, ISSN: 0300-9084, Vol: 88, Issue: 9, Page: 1297-1306
2006
- 49Citations
- 28Captures
Metric Options: CountsSelecting the 1-year or 3-year option will change the metrics count to percentiles, illustrating how an article or review compares to other articles or reviews within the selected time period in the same journal. Selecting the 1-year option compares the metrics against other articles/reviews that were also published in the same calendar year. Selecting the 3-year option compares the metrics against other articles/reviews that were also published in the same calendar year plus the two years prior.
Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
Citation Benchmarking is provided by Scopus and SciVal and is different from the metrics context provided by PlumX Metrics.
Metrics Details
- Citations49
- Citation Indexes49
- 49
- CrossRef34
- Captures28
- Readers28
- 28
Article Description
The effect of a group of natural flavonoids on human thrombin amidolytic activity was investigated using a spectrophotometric inhibition assay while information on the kinetics and thermodynamics was obtained using optical biosensor techniques. All the flavonoids tested acted as reversible inhibitors, and the quercetin–thrombin complex was found to be most stable at pH = 7.5. Docking analysis indicated that quercetin's inhibitory behavior could be related to its planar structure and low steric hindrance, and to its ability to form a critical H-bond with thrombin His57.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0300908406000575; http://dx.doi.org/10.1016/j.biochi.2006.04.007; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=33748768976&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/16690199; https://linkinghub.elsevier.com/retrieve/pii/S0300908406000575; https://dx.doi.org/10.1016/j.biochi.2006.04.007
Elsevier BV
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