Structure of Xenopus laevis ribosomal protein L32 and its expression during development
Nucleic Acids Research, ISSN: 0305-1048, Vol: 18, Issue: 15, Page: 4423-4426
1990
- 16Citations
- 4Captures
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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
- Citations16
- Citation Indexes16
- 16
- CrossRef6
- Captures4
- Readers4
Article Description
cDNA clones for Xenopus laevis ribosomal protein L32 have been isolated and sequenced. The deduced amino acid sequence indicates that L32 is a basic protein of 110 amino acids, has a molecular weight of 12,603 and is homologous to the rat ribosomal protein L35. Using the cDNA clone as a probe to follow the expression of this gene during Xenopus development, it has been shown that the pattern of accumulation of this mRNA follows the one previously described for other ribosomal protein mRNAs during oogenesis and embryogenesis. The analysis of the utilization of L32 mRNA during embryogenesis shows that this is controlled by the translational regulation typical of other ribosomal protein mRNAs. © 1990 Oxford University Press.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0025039808&origin=inward; http://dx.doi.org/10.1093/nar/18.15.4423; http://www.ncbi.nlm.nih.gov/pubmed/2388827; https://academic.oup.com/nar/article-lookup/doi/10.1093/nar/18.15.4423; https://dx.doi.org/10.1093/nar/18.15.4423; https://academic.oup.com/nar/article/18/15/4423/1048872
Oxford University Press (OUP)
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