Evidence map›Paper›PMID 20890290›Full record

ArticleNature structural & molecular biology2010

Structure of the Dom34-Hbs1 complex and implications for no-go decay.

Liming Chen, Denise Muhlrad, Vasili Hauryliuk, Zhihong Cheng, Meng Kiat Lim, Viktoriya Shyp, Roy Parker, Haiwei Song

Abstract readComparative Study
PubMed Publisher
In one paragraph

Article in Nature structural & molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.

0numbers the graph read from it
0cells of the map it votes in
64citing papers in PubMed
6.4field-weighted citation impact, top 3% 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

64 citing papers in PubMed, 114 citations in OpenAlex.

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  19. Roadblocks and resolutions in eukaryotic translation.Nature reviews. Molecular cell biology · 2018
    Review
  20. Article

4 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

8 authors at 3 institutions in 3 countries.

Liming ChenLaboratory of Macromolecular Structure, Institute of Molecular and Cell Biology, Proteos, Singapore.
Denise Muhlrad
Vasili Hauryliuk
Zhihong Cheng
Meng Kiat Lim
Viktoriya Shyp
Roy Parker
Haiwei Song
Institute of Molecular and Cell Biology · SGUniversity of Arizona · USUniversity of Tartu · EE

Funding

Howard Hughes Medical Institute
6 · The paper itself

Abstract

No-go decay (NGD) targets mRNAs with stalls in translation elongation for endonucleolytic cleavage in a process involving the Dom34 and Hbs1 proteins. The crystal structure of a Schizosaccharomyces pombe Dom34-Hbs1 complex reveals an overall shape similar to that of eRF1-eRF3-GTP and EF-Tu-tRNA-GDPNP. Similarly to eRF1 and GTP binding to eRF3, Dom34 and GTP bind to Hbs1 with strong cooperativity, and Dom34 acts as a GTP-dissociation inhibitor (GDI). A marked conformational change in Dom34 occurs upon binding to Hbs1, leading Dom34 to resemble a portion of a tRNA and to position a conserved basic region in a position expected to be near the peptidyl transferase center. These results support the idea that the Dom34-Hbs1 complex functions to terminate translation and thereby commit mRNAs to NGD. Consistent with this role, NGD at runs of arginine codons, which cause a strong block to elongation, is independent of the Dom34-Hbs1 complex.

Indexed as

CalorimetryCrystallography, X-RayEndoribonucleasesGuanosine TriphosphateModels, MolecularPeptide Elongation Factor TuProtein BindingProtein BiosynthesisProtein ConformationProtein Interaction MappingProtein Structure, TertiaryRecombinant Fusion ProteinsRNA, FungalRNA, MessengerRNA StabilityRNA, TransferEndoribonucleasesGuanosine TriphosphatePeptide Elongation Factor TuRecombinant Fusion ProteinsRNA, FungalRNA, MessengerRNA, TransferSchizosaccharomyces pombe ProteinsTranscription Factors

Identifiers

PMID20890290
OpenAlexW2002336825

What OpenQuestion holds

Textmetadata
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.