Evidence map›Paper›PMID 29259129›Full record

ArticleThe Journal of biological chemistry2018

Transmembrane region of bacterial chemoreceptor is capable of promoting protein clustering.

Abiola M Pollard, Victor Sourjik

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
1.0field-weighted citation impact, top 24% 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

3 citing papers in PubMed, 11 citations in OpenAlex.

  1. Article
  2. Article
  3. 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

2 authors at 1 institution in 1 country.

Abiola M PollardFrom the Max Planck Institute for Terrestrial Microbiology and LOEWE Center for Synthetic Microbiology (SYNMIKRO), D-35043 Marburg, Germany abiola.pollard@synmikro.mpi-marburg.mpg.de.
Victor SourjikFrom the Max Planck Institute for Terrestrial Microbiology and LOEWE Center for Synthetic Microbiology (SYNMIKRO), D-35043 Marburg, Germany victor.sourjik@synmikro.mpi-marburg.mpg.de.
Loewe Center for Synthetic Microbiology · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Many membrane proteins are known to form higher-order oligomers, but the degree to which membrane regions could facilitate protein complex assembly remains largely unclear. Clusters of chemotaxis receptors are among the most prominent structures in the bacterial cell membrane, and they play important functions in processing of chemotactic signals. Although much work has been done to elucidate mechanisms of cluster formation, it almost exclusively focused on cytoplasmic interactions among receptors and other chemotaxis proteins, whereas involvement of membrane-mediated interactions was only hypothesized. Here we used imaging of constructs composed of only a fluorescent protein and the TM helices of Tar to demonstrate that interactions between the lipid bilayer and transmembrane (TM) helices of

Indexed as

ChemotaxisCluster AnalysisEscherichia coli ProteinsIntracellular Signaling Peptides and ProteinsLipid BilayersMembrane ProteinsMethyl-Accepting Chemotaxis ProteinsProtein MultimerizationProtein Structure, SecondaryEscherichia coli ProteinsIntracellular Signaling Peptides and ProteinsLipid BilayersMembrane ProteinsMethyl-Accepting Chemotaxis Proteinsbacterial signal transductionchemotaxisprotein–protein interactionprotein self-assemblytransmembrane domain

Identifiers

PMID29259129
PMCPMC5808774
OpenAlexW2779319562

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.