Evidence map›Paper›PMID 27863242›Full record

ArticleCell2016

Decoding Mammalian Ribosome-mRNA States by Translational GTPase Complexes.

Sichen Shao, Jason Murray, Alan Brown, Jack Taunton, V Ramakrishnan, Ramanujan S Hegde

Open access · hybridAbstract read
In one paragraph

Article in Cell, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 154 papers.

0numbers the graph read from it
0cells of the map it votes in
154citing papers in PubMed
10.8field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

154 citing papers in PubMed, 253 citations in OpenAlex.

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  17. Molecular architecture and diversity of StopGo/2A translational recoding.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  18. Targeting elongation factor 2 inFrontiers in insect science · 2026
    Review
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  20. Review

94 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

Sichen ShaoMRC-LMB, Francis Crick Avenue, Cambridge CB2 0QH, UK.
Jason MurrayMRC-LMB, Francis Crick Avenue, Cambridge CB2 0QH, UK.
Alan BrownMRC-LMB, Francis Crick Avenue, Cambridge CB2 0QH, UK.
Jack TauntonDepartment of Cellular and Molecular Pharmacology, University of California, San Francisco, San Francisco, CA 94158, USA.
V RamakrishnanMRC-LMB, Francis Crick Avenue, Cambridge CB2 0QH, UK. Electronic address: ramak@mrc-lmb.cam.ac.uk.
Ramanujan S HegdeMRC-LMB, Francis Crick Avenue, Cambridge CB2 0QH, UK. Electronic address: rhegde@mrc-lmb.cam.ac.uk.
University of California, San Francisco · US

Funding

Medical Research Council MC_U105184332Medical Research Council MC_UP_A022_1007Wellcome Trust
6 · The paper itself

Abstract

In eukaryotes, accurate protein synthesis relies on a family of translational GTPases that pair with specific decoding factors to decipher the mRNA code on ribosomes. We present structures of the mammalian ribosome engaged with decoding factor⋅GTPase complexes representing intermediates of translation elongation (aminoacyl-tRNA⋅eEF1A), termination (eRF1⋅eRF3), and ribosome rescue (Pelota⋅Hbs1l). Comparative analyses reveal that each decoding factor exploits the plasticity of the ribosomal decoding center to differentially remodel ribosomal proteins and rRNA. This leads to varying degrees of large-scale ribosome movements and implies distinct mechanisms for communicating information from the decoding center to each GTPase. Additional structural snapshots of the translation termination pathway reveal the conformational changes that choreograph the accommodation of decoding factors into the peptidyl transferase center. Our results provide a structural framework for how different states of the mammalian ribosome are selectively recognized by the appropriate decoding factor⋅GTPase complex to ensure translational fidelity.

Indexed as

Protein BiosynthesisAnimalsCryoelectron MicroscopyEndonucleasesHumansMicrofilament ProteinsModels, ChemicalModels, MolecularNuclear ProteinsPeptide Elongation FactorsRibosomesRNA, MessengerEndonucleasesMicrofilament ProteinsNuclear Proteinspelo protein, humanPeptide Elongation FactorsRNA, Messengercryo-EMmammalian ribosomemRNA decodingprotein translationtranslational GTPase

Identifiers

PMID27863242
PMCPMC5119991
OpenAlexW2549271860

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.