Morphing molecular specificities between Arm-peptide and NUT-RNA in the antitermination complexes of bacteriophages λ and P22
Author:
Publisher
Wiley
Subject
Molecular Biology,Microbiology
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1365-2958.2004.04018.x/fullpdf
Reference42 articles.
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2. Large libraries reveal diverse solutions to an RNA recognition problem;Barrick;Proc Natl Acad Sci USA,2001
3. Solution structure of P22 transcriptional antitermination N peptide-boxB RNA complex;Cai;Nature Struct Biol,1998
4. Sensitive mutants of bacteriophage λ;Campbell;Virology,1961
5. Bipartite function of a small RNA hairpin in transcription antitermination in bacteriophage lambda;Chattopadhyay;Proc Natl Acad Sci USA,1995
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1. HK022 Nun Requires Arginine-Rich Motif Residues Distinct from λ N;Journal of Bacteriology;2015-11-15
2. Replacement of the λ boxB RNA-N peptide with heterologous RNA-peptide interactions relaxes the strict spatial requirements for the formation of a transcription anti-termination complex;Molecular Microbiology;2009-10
3. Genomic analysis of bacteriophage ε34 of Salmonella entericaserovar Anatum (15+);BMC Microbiology;2008-12
4. The RNA-Binding Domain of Bacteriophage P22 N Protein Is Highly Mutable, and a Single Mutation Relaxes Specificity toward λ;Journal of Bacteriology;2008-12
5. Bacteriophage P22 Antitermination boxB Sequence Requirements Are Complex and Overlap with Those of λ;Journal of Bacteriology;2008-06-15
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