Evidence map›Paper›PMID 28857741›Full record

ArticleeLife2017

In vivo experiments do not support the charge zipper model for Tat translocase assembly.

Felicity Alcock, Merel Pm Damen, Jesper Levring, Ben C Berks

Open access · goldAbstract read
In one paragraph

Article in eLife, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.6field-weighted citation impact, top 33% 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

8 citing papers in PubMed, 9 citations in OpenAlex.

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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

4 authors at 1 institution in 1 country.

Felicity Alcock *Department of Biochemistry, University of Oxford, Oxford, United Kingdom.ORCID https://orcid.org/0000-0002-3983-6097
Merel Pm Damen *Department of Biochemistry, University of Oxford, Oxford, United Kingdom.ORCID http://orcid.org/0000-0003-4233-2671
Jesper Levring *Department of Biochemistry, University of Oxford, Oxford, United Kingdom.
Ben C BerksDepartment of Biochemistry, University of Oxford, Oxford, United Kingdom.ORCID http://orcid.org/0000-0001-9685-4067
University of Oxford · GB

Funding

Biotechnology and Biological Sciences Research Council BB/L002531/1Wellcome TrustWellcome Trust 107929/Z/15/Z
6 · The paper itself

Abstract

The twin-arginine translocase (Tat) transports folded proteins across the bacterial cytoplasmic membrane and the plant thylakoid membrane. The Tat translocation site is formed by substrate-triggered oligomerization of the protein TatA. Walther and co-workers have proposed a structural model for the TatA oligomer in which TatA monomers self-assemble using electrostatic 'charge zippers' (

Indexed as

Protein MultimerizationAmino Acid SubstitutionDNA Mutational AnalysisEscherichia coliEscherichia coli ProteinsMembrane Transport ProteinsModels, BiologicalMutant ProteinsEscherichia coli ProteinsMembrane Transport ProteinsMutant ProteinsTatA protein, E colibiochemistryE. colimembrane proteinprotein transportTat system

Identifiers

PMID28857741
PMCPMC5601993
OpenAlexW2753825587

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.