Structural comparison between the trout and mammalian hydrophilic domain of nadphcytochrome P-450 reductase
Journal of Chromatography A, ISSN: 0021-9673, Vol: 397, Issue: C, Page: 123-136
1987
- 19Citations
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.
Citation Benchmarking is provided by Scopus and SciVal and is different from the metrics context provided by PlumX Metrics.
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
- 19
- CrossRef18
Article Description
The isolation of the protease-solubilized NADPHcytochrome P-450 reductase from trout liver and its properties are described. The sequence of the “hydrophilic domain” [protease-solubilized NADPHcytochrome P-450 reductase from trout (residues Lys 56 —Ser 678 )] is reported. The CNBr fragments of the trout “hydrophilic domain” and their proteolytic subpeptides were sequenced. The CNBr fragments were aligned by homology to the reported sequence of the porcine NADPHcytochrome P-450 reductase. The structures of the mammalian and the trout NADPHcytochrome P-450 reductases were compared. Stretches with high exchange rates between the pig and trout reductase were found at the NH 2 and the COOH terminal regions of the hydrophilic domain.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0021967301849955; http://dx.doi.org/10.1016/s0021-9673(01)84995-5; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0023665680&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/3116019; http://linkinghub.elsevier.com/retrieve/pii/S0021967301849955; http://api.elsevier.com/content/article/PII:S0021967301849955?httpAccept=text/xml; http://api.elsevier.com/content/article/PII:S0021967301849955?httpAccept=text/plain; https://linkinghub.elsevier.com/retrieve/pii/S0021967301849955; http://dx.doi.org/10.1016/s0021-9673%2801%2984995-5; https://dx.doi.org/10.1016/s0021-9673%2801%2984995-5
Elsevier BV
Provide Feedback
Have ideas for a new metric? Would you like to see something else here?Let us know