Randomized codon mutagenesis reveals that the HIV Rev arginine-rich motif is robust to substitutions and that double substitution of two critical residues alters specificity

The Control of HIV Transcription: Keeping RNA Polymerase II on Track

(2011) Melanie Ott et al.   Cell Host & Microbe

Structural basis for cooperative RNA binding and export complex assembly by HIV Rev

(2010) Matthew D Daugherty et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Protein Dynamism and Evolvability

(2009) N. Tokuriki et al.   SCIENCE

Bacteriophage P22 Antitermination boxB Sequence Requirements Are Complex and Overlap with Those of  

(2008) A. I. Cocozaki et al.   JOURNAL OF BACTERIOLOGY

The RNA-Binding Domain of Bacteriophage P22 N Protein Is Highly Mutable, and a Single Mutation Relaxes Specificity toward  

(2008) A. I. Cocozaki et al.   JOURNAL OF BACTERIOLOGY

Amino acid requirement for the high affinity binding of a selected arginine-rich peptide with the HIV Rev-response element RNA

(2008) Maki Sugaya et al.   JOURNAL OF PEPTIDE SCIENCE

A Solution to Limited Genomic Capacity: Using Adaptable Binding Surfaces to Assemble the Functional HIV Rev Oligomer on RNA

(2008) Matthew D. Daugherty et al.   MOLECULAR CELL

Tailoring the Peptide-Binding Specificity Of An RNA by Combinations of Specificity-Altering Mutations

(2008) Maki Sugaya et al.   NUCLEOSIDES NUCLEOTIDES & NUCLEIC ACIDS