Insights into the structural basis of rna recognition by star domain proteins
Advances in Experimental Medicine and Biology, ISSN: 0065-2598, Vol: 693, Page: 37-53
2010
- 66Citations
- 11Captures
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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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Metrics Details
- Citations66
- Citation Indexes66
- 12
- CrossRef11
- Captures11
- Readers11
- 11
Book Chapter Description
STAR proteins regulate diverse cellular processes and control numerous Developmentalevents. Theyfunctionatthe post-transcriptional levelbyregulating the stability, sub-cellular distribution, alternative splicing, ortranslational efficiency of specific rnRNA targets. Significant effort has been expended to define the determinants of RNA recognition by STAR proteins, in hopes of identifying new mRNA targets that contribute their role in cellular metabolism and development. This work has lead tothe extensive biochemical characterization of the nucleotide sequence specificity of a handful of STAR proteins. In contrast, little structural information is avaJLable to aialyze the molecular basis of sequence specific RNA recognition by this protein family. This chapter reviews the relevant literature on STAR domain protein structure and provides insights into how these proteins discriminate between different RNA sequences. © 2010 Landes Bioscience and Springer Science-f-Business Media.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=79952202277&origin=inward; http://dx.doi.org/10.1007/978-1-4419-7005-3_3; http://www.ncbi.nlm.nih.gov/pubmed/21189684; http://link.springer.com/10.1007/978-1-4419-7005-3_3; https://dx.doi.org/10.1007/978-1-4419-7005-3_3; https://link.springer.com/chapter/10.1007/978-1-4419-7005-3_3; http://www.springerlink.com/index/10.1007/978-1-4419-7005-3_3; http://www.springerlink.com/index/pdf/10.1007/978-1-4419-7005-3_3
Springer Science and Business Media LLC
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