Evidence map›Paper›PMID 28280110›Full record

ArticleThe Biochemical journal2017

TatA complexes exhibit a marked change in organisation in response to expression of the TatBC complex.

Sarah M Smith, Andrew Yarwood, Roland A Fleck, Colin Robinson, Corinne J Smith

Open access · hybridAbstract read
In one paragraph

Article in The Biochemical journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.7field-weighted citation impact, top 28% 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

2 citing papers in PubMed, 3 citations in OpenAlex.

  1. Article
  2. Q&A: Array tomography.BMC biology · 2018
    Article
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

5 authors at 4 institutions in 1 country.

Sarah M SmithSchool of Life Sciences, University of Warwick, Coventry CV4 7AL, U.K.
Andrew YarwoodJEOL (UK) Ltd, Welwyn Garden City AL7 1LT, U.K.
Roland A FleckCentre For Ultrastructural Imaging, King's College London, New Hunts House, Guy's Campus, London SE1 1UL, U.K.
Colin RobinsonSchool of Biosciences, University of Kent, Canterbury CT2 7NJ, U.K.
Corinne J SmithSchool of Life Sciences, University of Warwick, Coventry CV4 7AL, U.K. corinne.smith@warwick.ac.uk.
University of Warwick · GBJEOL (United Kingdom) · GBKing's College London · GBUniversity of Kent · GB

Funding

Biotechnology and Biological Sciences Research CouncilWellcome Trust 055663/Z/98/Z
6 · The paper itself

Abstract

The twin-arginine translocation (Tat) system is an integral membrane protein complex that accomplishes the remarkable feat of transporting large, fully folded polypeptides across the inner membrane of bacteria, into the periplasm. In

Indexed as

Cell MembraneEscherichia coliEscherichia coli ProteinsImaging, Three-DimensionalMembrane Transport ProteinsMicroscopy, ImmunoelectronMultiprotein ComplexesOperonProtein BindingProtein TransportEscherichia coli ProteinsMembrane Transport ProteinsMultiprotein ComplexesTatA protein, E coliTatB protein, E coliTatC protein, E colielectron microscopytransmembrane proteinstransport

Identifiers

PMID28280110
PMCPMC5396077
OpenAlexW2593839778

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.