The eye lens crystallins: Ambiguity as evolutionary strategy
Journal of Molecular Evolution, ISSN: 0022-2844, Vol: 24, Issue: 1-2, Page: 121-129
1986
- 50Citations
- 7Captures
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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
- Citations50
- Citation Indexes50
- 50
- CrossRef45
- Captures7
- Readers7
Article Description
Comparative studies of the different families of lens-specific proteins of the vertebrates, the crystallins, and their genes reveal several interesting evolutionary features. The origin of α-crystallin can be traced back to the small heat shock proteins, while the superfamily of βγ-crystallins shows structural similarities with a bacterial spore coat protein. The crystallins display a great diversity within and between species, as well as during development. Ambiguous transcription, mRNA-processing, and translation contribute to this diversity of the crystallins and their expression. These mechanisms include the occurrence of atypical poly-A addition signals, alternative splicing, and the use of two initiation codons on a single mRNA. © 1986 Springer-Verlag New York Inc.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0022824191&origin=inward; http://dx.doi.org/10.1007/bf02099960; http://www.ncbi.nlm.nih.gov/pubmed/3104612; http://link.springer.com/10.1007/BF02099960; http://link.springer.com/content/pdf/10.1007/BF02099960; https://dx.doi.org/10.1007/bf02099960; https://link.springer.com/article/10.1007/BF02099960
Springer Nature
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