Evidence map›Paper›PMID 24735854›Full record

ArticleCurrent biology : CB2014

Protein translocation: the Sec61/SecYEG translocon caught in the act.

Martin Spiess

Abstract readComment
PubMed Publisher
In one paragraph

Article in Current biology : CB, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

1 author.

Martin SpiessBiozentrum of the University of Basel, Klingelbergstrasse 50/70, CH-4056 Basel, Switzerland. Electronic address: martin.spiess@unibas.ch.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Sec61/SecYEG complex mediates both the translocation of newly synthesized proteins across the membrane and the integration of transmembrane segments into the lipid bilayer. New cryo-electron microscopy studies show ribosome-channel complexes in action and reveal their repertoire of conformational states.

Indexed as

Protein BiosynthesisAnimalsCell MembraneEscherichia coliEscherichia coli ProteinsMembrane ProteinsMethanocaldococcusMultiprotein ComplexesPeptidesProtein SubunitsRibosomesUltrasonographyEscherichia coli ProteinsMembrane ProteinsMultiprotein ComplexesPeptidesProtein Subunits

Identifiers

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.