Structure of the large ribosomal subunit from human mitochondria
Structure of the large ribosomal subunit from human mitochondria
Making mitochondrial hydrophobic proteins Mitochondria produce chemical energy for the cell. Human mitochondria have their own specific ribosomes—mitoribosomes, which are distinct from cytoplasmic ribosomes. Mitoribosomes synthesize the mitochondrial membrane proteins that generate the chemical energy. Brown et al. used cryo–electron microscopy to determine the high-resolution structure of the large subunit of the human mitoribosome. The mitoribosome has a number of unique features, including an exit tunnel lined with hydrophobic amino acid residues. Science , this issue p. 718
- Medical Research Council United Kingdom
- MRC Laboratory of Molecular Biology United Kingdom
Mitochondrial Proteins, Binding Sites, Protein Conformation, Cryoelectron Microscopy, Mutation, Ribosome Subunits, Humans, Nucleic Acid Conformation, RNA, Transfer, Val, Mitochondria
Mitochondrial Proteins, Binding Sites, Protein Conformation, Cryoelectron Microscopy, Mutation, Ribosome Subunits, Humans, Nucleic Acid Conformation, RNA, Transfer, Val, Mitochondria
53 Research products, page 1 of 6
- 2017IsRelatedTo
- 2017IsRelatedTo
- 2017IsRelatedTo
- 2017IsRelatedTo
- 2017IsRelatedTo
- 2017IsRelatedTo
- 2017IsRelatedTo
- 2017IsRelatedTo
- 2017IsRelatedTo
- 2017IsRelatedTo
chevron_left - 1
- 2
- 3
- 4
- 5
chevron_right
citations This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).284 popularity This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.Top 1% influence This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).Top 10% impulse This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.Top 1%
