Structure based hypothesis of a mitochondrial ribosome rescue mechanism

Structural aspects of translation termination on the ribosome

(2011) A. A. Korostelev   RNA

Mutations in C12orf65 in Patients with Encephalomyopathy and a Mitochondrial Translation Defect

(2010) Hana Antonicka et al.   AMERICAN JOURNAL OF HUMAN GENETICS

Human mitochondrial mRNAs—like members of all families, similar but different

(2010) Richard J. Temperley et al.   BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS

Optimization of speed and accuracy of decoding in translation

(2010) Ingo Wohlgemuth et al.   EMBO JOURNAL

Recognition of the amber UAG stop codon by release factor RF1

(2010) Andrei Korostelev et al.   EMBO JOURNAL

A functional peptidyl-tRNA hydrolase, ICT1, has been recruited into the human mitochondrial ribosome

(2010) Ricarda Richter et al.   EMBO JOURNAL

Terminating human mitochondrial protein synthesis: A shift in our thinking

(2010) Robert N. Lightowlers et al.   RNA Biology

Bioinformatic, structural, and functional analyses support release factor-like MTRF1 as a protein able to decode nonstandard stop codons beginning with adenine in vertebrate mitochondria

(2010) D. J. Young et al.   RNA

Hungry Codons Promote Frameshifting in Human Mitochondrial Ribosomes

(2010) R. Temperley et al.   SCIENCE

Human mitochondrial RNA turnover caught in flagranti: involvement of hSuv3p helicase in RNA surveillance

(2009) Roman J. Szczesny et al.   NUCLEIC ACIDS RESEARCH

HMRF1L is a human mitochondrial translation release factor involved in the decoding of the termination codons UAA and UAG

(2008) Yusuke Nozaki et al.   GENES TO CELLS

Structural basis for translation termination on the 70S ribosome

(2008) Martin Laurberg et al.   NATURE

Crystal structure of a translation termination complex formed with release factor RF2

(2008) A. Korostelev et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Insights into Translational Termination from the Structure of RF2 Bound to the Ribosome

(2008) A. Weixlbaumer et al.   SCIENCE