K. K. McCaughan

Two regions of the Escherichia coli 16S ribosomal RNA are important for decoding stop signals in polypeptide chain termination.

Chris M. Brown, W. Tate, K. McCaughan, 1993, Nucleic acids research.

Translational termination efficiency in mammals is influenced by the base following the stop codon.

W P Tate, M E Dalphin, C. Brown, 1995, Proceedings of the National Academy of Sciences of the United States of America.

Translational termination efficiency in both bacteria and mammals is regulated by the base following the stop codon.

Daniel N. Wilson, C. Brown, W. Tate, 1995, Biochemistry and cell biology = Biochimie et biologie cellulaire.

Efficient In Vitro Translational Termination in Escherichia coli Is Constrained by the Orientations of the Release Factor, Stop Signal and Peptidyl-tRNA within the Termination Complex

W. Tate, H. Pel, E. Poole, 1998, Biological chemistry.

The ribosomal domain of the bacterial release factors. The carboxyl-terminal domain of the dimer of Escherichia coli ribosomal protein L7/L12 located in the body of the ribosome is important for release factor interaction.

W. Tate, K. McCaughan, B. Kastner, 1990, European journal of biochemistry.

The concentration of polypeptide chain release factors 1 and 2 at different growth rates of Escherichia coli.

C. Kurland, W. Tate, K. McCaughan, 1994, Journal of molecular biology.

Mammalian polypeptide chain release factor and tryptophanyl‐tRNA synthetase are distinct proteins.

W. Tate, M. Dalphin, K. McCaughan, 1993, The EMBO journal.

Identification of the prfC gene, which encodes peptide-chain-release factor 3 of Escherichia coli.

Y. Nakamura, W. Tate, J. Moffat, 1994, Proceedings of the National Academy of Sciences of the United States of America.

Molecular mimicry in the decoding of translational stop signals.

Daniel N. Wilson, W. Tate, E. Poole, 2003, Progress in nucleic acid research and molecular biology.