ArticleProceedings of the National Academy of Sciences of the United States of America2017
A close-up look at the spliceosome, at last.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
4 citing papers in PubMed.
- Spliceosome assembly and regulation: insights from analysis of highly reduced spliceosomes.RNA (New York, N.Y.) · 2023Review
- The Myc-associated zinc finger protein (MAZ) works together with CTCF to control cohesin positioning and genome organization.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Dynamic protein-RNA interactions in mediating splicing catalysis.Nucleic acids research · 2019Article
- Structural and functional analyses of the spliceosome requires a multi-disciplinary approach.Methods (San Diego, Calif.) · 2017Article
Corrections and comments
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Authors and funding
1 author.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Major developments in cryo-electron microscopy in the past three or four years have led to the solution of a number of spliceosome structures at high resolution, e.g., the fully assembled but not yet active spliceosome (Bact), the spliceosome just after the first step of splicing (C), and the spliceosome activated for the second step (C*). Therefore 30 years of genetics and biochemistry of the spliceosome can now be interpreted at the structural level. I have closely examined the RNase H domain of Prp8 in each of the structures. Interestingly, the RNase H domain has different and unexpected roles in each of the catalytic steps of splicing.
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