ArticleActa crystallographica. Section F, Structural biology and crystallization communications2006
Crystallization and preliminary X-ray analysis of a U2AF65 variant in complex with a polypyrimidine-tract analogue by use of protein engineering.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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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
10 citing papers in PubMed, 11 citations in OpenAlex.
- An Unusual U2AF2 Inhibits Splicing and Attenuates the Virulence of the Human Protozoan ParasiteFrontiers in cellular and infection microbiology · 2022Article
- A splice site-sensing conformational switch in U2AF2 is modulated by U2AF1 and its recurrent myelodysplasia-associated mutation.Nucleic acids research · 2020Article
- An extended U2AF(65)-RNA-binding domain recognizes the 3' splice site signal.Nature communications · 2016Article
- Structure-guided U2AF65 variant improves recognition and splicing of a defective pre-mRNA.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- U2AF65 adapts to diverse pre-mRNA splice sites through conformational selection of specific and promiscuous RNA recognition motifs.Nucleic acids research · 2013Article
- Roles of polypyrimidine tract binding proteins in major immediate-early gene expression and viral replication of human cytomegalovirus.Journal of virology · 2009Article
- Solution conformation and thermodynamic characteristics of RNA binding by the splicing factor U2AF65.The Journal of biological chemistry · 2008Article
- Structure of the central RNA recognition motif of human TIA-1 at 1.95A resolution.Biochemical and biophysical research communications · 2008Article
- A serendipitous discovery that in situ proteolysis is essential for the crystallization of yeast CPSF-100 (Ydh1p).Acta crystallographica. Section F, Structural biology and crystallization communications · 2006Article
- Structural basis for polypyrimidine tract recognition by the essential pre-mRNA splicing factor U2AF65.Molecular cell · 2006Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The large subunit of the essential pre-mRNA splicing factor U2 auxiliary factor (U2AF65) binds the polypyrimidine tract near the 3' splice site of pre-mRNA introns and directs the association of the U2 small nuclear ribonucleoprotein particle (U2 snRNP) of the spliceosome with the pre-mRNA. Protein engineering, in which the flexible linker region connecting tandem RNA-recognition motifs (RRMs) within the U2AF65 RNA-binding domain was partially deleted, allowed successful crystallization of the protein-nucleic acid complex. Cocrystals of a U2AF65 variant with a deoxyuridine dodecamer diffract X-rays to 2.9 angstroms resolution and contain one complex per asymmetric unit.
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