Ribonuclease U2: cloning, production in Pichia pastoris and affinity chromatography purification of the active recombinant protein.
FEMS microbiology letters, ISSN: 0378-1097, Vol: 189, Issue: 2, Page: 165-9
2000
- 3Citations
- 3Captures
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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
- Citations3
- Citation Indexes3
- Captures3
- Readers3
Article Description
RNase U2 is an endoribonuclease secreted by the fungus Ustilago sphaerogena. Its genomic DNA (rnu2), containing an intron of 116 bp, has been isolated and cloned. The corresponding cDNA has also been synthesized. The recombinant RNase U2 was successfully produced in Pichia pastoris, fused to the yeast alkaline phosphatase signal peptide. The recombinant RNase U2, purified by affinity chromatography, contains three extra amino acids at its amino-terminal end and retains the enzymatic and spectroscopic properties of the natural fungal protein.
Bibliographic Details
http://dx.doi.org/10.1111/j.1574-6968.2000.tb09224.x; http://www.ncbi.nlm.nih.gov/pubmed/10930732; https://academic.oup.com/femsle/article-lookup/doi/10.1111/j.1574-6968.2000.tb09224.x; https://dx.doi.org/10.1111/j.1574-6968.2000.tb09224.x; https://academic.oup.com/femsle/article-abstract/189/2/165/523342?redirectedFrom=fulltext
Oxford University Press (OUP)
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