Evidence map›Paper›PMID 25485085›Full record

ArticleInterface focus2014

Effects of molecular noise on bistable protein distributions in rod-shaped bacteria.

L Wettmann, M Bonny, K Kruse

Open access · bronzeAbstract read
In one paragraph

Article in Interface focus, 2014. 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
0.9field-weighted citation impact, top 19% 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, 10 citations in OpenAlex.

  1. Article
  2. The Min-protein oscillations inPhilosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018
    Review
  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

3 authors at 1 institution in 1 country.

L WettmannTheoretische Physik , Universität des Saarlandes , Postfach 151150, 66041 Saarbrücken , Germany.
M BonnyTheoretische Physik , Universität des Saarlandes , Postfach 151150, 66041 Saarbrücken , Germany.
K KruseTheoretische Physik , Universität des Saarlandes , Postfach 151150, 66041 Saarbrücken , Germany.ORCID 0000-0001-8665-2349
Universitätsklinikum des Saarlandes · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The distributions of many proteins in rod-shaped bacteria are far from homogeneous. Often they accumulate at the cell poles or in the cell centre. At the same time, the copy number of proteins in a single cell is relatively small making the patterns noisy. To explore limits to protein patterns due to molecular noise, we studied a generic mechanism for spontaneous polar protein assemblies in rod-shaped bacteria, which are based on cooperative binding of proteins to the cytoplasmic membrane. For mono-polar assemblies, we find that the switching time between the two poles increases exponentially with the cell length and with the protein number. This feature could be beneficial to organelle maintenance in ageing bacteria.

Indexed as

cooperative bindingmolecular noiserod-shaped bacteriaspatial protein distributionsstochastic processes

Identifiers

PMID25485085
PMCPMC4213450
OpenAlexW1991937302

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.