
Unwinding RNA for protein synthesis During the first steps of protein synthesis, the small subunit of the ribosome scans the 5′ end of the mRNA, looking for the protein start codon. This process involves one of the translation initiation factors, eIF4A, which helps to remove any RNA structures that might impede the ribosome's search. García-García et al. used single-molecule optical trap assays to show that eIF4A, in combination with two other translation initiation factors, is able to continuously and directionally unwind a double-stranded RNA hairpin. The factors unwound RNA in steps roughly equal to a turn of the RNA double helix. Science , this issue p. 1486
570, General Science & Technology, DNA, Biological Sciences, Adenosine Triphosphate, Protein Biosynthesis, 616, Eukaryotic Initiation Factor-4A, Genetics, Humans, Nucleic Acid Conformation, RNA, Biochemistry and Cell Biology, Generic health relevance, Eukaryotic Initiation Factors, Eukaryotic Initiation Factor-4G
570, General Science & Technology, DNA, Biological Sciences, Adenosine Triphosphate, Protein Biosynthesis, 616, Eukaryotic Initiation Factor-4A, Genetics, Humans, Nucleic Acid Conformation, RNA, Biochemistry and Cell Biology, Generic health relevance, Eukaryotic Initiation Factors, Eukaryotic Initiation Factor-4G
| selected citations These citations are derived from selected sources. This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically). | 82 | |
| popularity This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network. | Top 10% | |
| influence This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically). | Top 10% | |
| impulse This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network. | Top 1% |
