A novel bivalent single-chain variable fragment (scFV) inhibits the action of tumour necrosis factor α
Biotechnology and Applied Biochemistry, ISSN: 0885-4513, Vol: 50, Issue: 4, Page: 173-179
2008
- 14Citations
- 8Captures
Metric Options: Counts1 Year3 YearSelecting 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
- Citations14
- Citation Indexes13
- 13
- CrossRef9
- Patent Family Citations1
- Patent Families1
- Captures8
- Readers8
Article Description
Suppression of TNFα (tumour necrosis factor α) activity is widely considered to be among the most efficient treatments available for chronic inflammatory diseases. Here, a bivalent scFv (single-chain variable fragment) fragment, named TNF-BAb, was engineered by fusing two anti-TNFα scFV fragments in tandem via a long and flexible linking peptide derived from human serum albumin and produced in functional form from Escherichia coli inclusion bodies. The bioactivity assays demonstrated that TNF-BAb gained enormously in avidity and showed a much stronger ability to inhibit the biological action of TNFα, indicating that TNF-BAb may become a good candidate for anti-TNFα therapy. © 2008 Portland Press Ltd.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=49249090889&origin=inward; http://dx.doi.org/10.1042/ba20070229; http://www.ncbi.nlm.nih.gov/pubmed/18047471; https://iubmb.onlinelibrary.wiley.com/doi/10.1042/BA20070229; http://doi.wiley.com/10.1042/BA20070229; https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1042%2FBA20070229; https://dx.doi.org/10.1042/ba20070229; https://iubmb.onlinelibrary.wiley.com/doi/abs/10.1042/BA20070229
Wiley
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