Evidence map›Paper›PMID 24096398›Full record

ArticleNature structural & molecular biology2013

Zooming in on eukaryotic translation initiation.

Anders Liljas

Abstract readNewsComment
PubMed Publisher
In one paragraph

Article in Nature structural & molecular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

1 author.

Anders LiljasDepartment of Biochemistry and Structural Biology, Lund University, Lund, Sweden.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Translation initiation in eukaryotes is a complex and highly regulated process during which several initiation factors cooperate to recruit an initiator tRNA to the small ribosomal subunit, where the mRNA is scanned for an AUG start codon. Two recent reports provide new structural insights into this process and reveal key functions of initiation factors 1 (eIF1) and 1A (eIF1A) in start-codon selection in atomic detail.

Indexed as

Models, MolecularProtein BiosynthesisProtein ConformationAnimalsEukaryotic Initiation FactorsHumansMultiprotein ComplexesRibosome Subunits, Small, EukaryoticRNA, MessengerTetrahymena thermophilaEukaryotic Initiation FactorsMultiprotein ComplexesRNA, Messenger

Identifiers

PMID24096398

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.