Published in Genet Eng (N Y) on January 01, 1996
Translational termination in Escherichia coli: three bases following the stop codon crosslink to release factor 2 and affect the decoding efficiency of UGA-containing signals. Nucleic Acids Res (1998) 1.25
Mutations in RNAs of both ribosomal subunits cause defects in translation termination. EMBO J (1998) 1.16
Escherichia coli release factor 3: resolving the paradox of a typical G protein structure and atypical function with guanine nucleotides. RNA (1998) 1.10
Translational termination efficiency in mammals is influenced by the base following the stop codon. Proc Natl Acad Sci U S A (1995) 2.49
Translational termination: "stop" for protein synthesis or "pause" for regulation of gene expression. Biochemistry (1992) 2.49
The translational termination signal database. Nucleic Acids Res (1993) 1.90
Three, four or more: the translational stop signal at length. Mol Microbiol (1996) 1.61
Hidden infidelities of the translational stop signal. Prog Nucleic Acid Res Mol Biol (1996) 1.45
Translational termination efficiency in both bacteria and mammals is regulated by the base following the stop codon. Biochem Cell Biol (1996) 1.26
Translational termination in Escherichia coli: three bases following the stop codon crosslink to release factor 2 and affect the decoding efficiency of UGA-containing signals. Nucleic Acids Res (1998) 1.25
The translational stop signal: codon with a context, or extended factor recognition element? Biochimie (1996) 1.23
The translational termination signal database (TransTerm) now also includes initiation contexts. Nucleic Acids Res (1994) 1.21
Prokaryotic ribosomes recode the HIV-1 gag-pol-1 frameshift sequence by an E/P site post-translocation simultaneous slippage mechanism. Nucleic Acids Res (1995) 1.21
The nucleotide sequence of the first two genes of the CFA/I fimbrial operon of human enterotoxigenic Escherichia coli. Microb Pathog (1989) 1.14
UGA: a dual signal for 'stop' and for recoding in protein synthesis. Biochemistry (Mosc) (1999) 1.04
Structural analysis of a group II intron by chemical modifications and minimal energy calculations. J Biomol Struct Dyn (1990) 1.00
Mammalian polypeptide chain release factor and tryptophanyl-tRNA synthetase are distinct proteins. EMBO J (1993) 0.94
Structure-function relationships in a self-splicing group II intron: a large part of domain II of the mitochondrial intron aI5 is not essential for self-splicing. Nucleic Acids Res (1989) 0.93
Functional characterization of yeast mitochondrial release factor 1. J Biol Chem (2000) 0.93
Is the in-frame termination signal of the Escherichia coli release factor-2 frameshift site weakened by a particularly poor context? Nucleic Acids Res (1996) 0.91
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. Biol Chem (1998) 0.87
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. Eur J Biochem (1990) 0.83
Interaction of the release factor with the Escherichia coli ribosome: inhibition of the 30S subunit domain by specific antibodies. Biochem Int (1988) 0.82