A novel metal-Chelating inhibitor of protein farnesyltransferase
Bioorganic & Medicinal Chemistry Letters, ISSN: 0960-894X, Vol: 13, Issue: 9, Page: 1523-1526
2003
- 19Citations
- 9Captures
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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.
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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
- Citations19
- Citation Indexes19
- CrossRef19
- 19
- Captures9
- Readers9
Article Description
A novel metal chelator comprising a 4-(naphthalen-1-yl)pyridine and 2-aminoethanethiol was synthesized. This showed inhibitory activity against human protein farnesyltransferase with IC 50 1.9 μM, induced morphological change in K-ras-NRK cells at 0.5 μg/mL and showed growth inhibition of K-ras-NRK cells with IC 50 0.32 μg/mL.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0960894X03001835; http://dx.doi.org/10.1016/s0960-894x(03)00183-5; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=12444283656&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/12699746; http://linkinghub.elsevier.com/retrieve/pii/S0960894X03001835; http://api.elsevier.com/content/article/PII:S0960894X03001835?httpAccept=text/xml; http://api.elsevier.com/content/article/PII:S0960894X03001835?httpAccept=text/plain; https://linkinghub.elsevier.com/retrieve/pii/S0960894X03001835; http://dx.doi.org/10.1016/s0960-894x%2803%2900183-5; https://dx.doi.org/10.1016/s0960-894x%2803%2900183-5
Elsevier BV
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