Evidence map›Paper›PMID 29720870›Full record

ArticleEvolutionary bioinformatics online2018

Exploring Proteins Containing Amyloidogenic Regions in the Proteomes of Bacteria of the Order

Kirill S Antonets, Sergey F Kliver, Anton A Nizhnikov

Open access · goldAbstract read
In one paragraph

Article in Evolutionary bioinformatics online, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
1.4field-weighted citation impact, top 15% 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

5 citing papers in PubMed, 7 citations in OpenAlex.

  1. OmpC and OmpF Outer Membrane Proteins ofInternational journal of molecular sciences · 2023
    Article
  2. Review
  3. Article
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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

3 authors at 1 institution in 1 country.

Kirill S AntonetsLaboratory for Proteomics of Supra-Organismal Systems, All-Russia Research Institute for Agricultural Microbiology, St. Petersburg, Russian Federation.
Sergey F KliverLaboratory for Proteomics of Supra-Organismal Systems, All-Russia Research Institute for Agricultural Microbiology, St. Petersburg, Russian Federation.
Anton A NizhnikovLaboratory for Proteomics of Supra-Organismal Systems, All-Russia Research Institute for Agricultural Microbiology, St. Petersburg, Russian Federation.
All-Russian Research Institute of Agricultural Microbiology · RU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Amyloids are protein fibrils with a highly ordered spatial structure called cross-β. To date, amyloids were shown to be implicated in a wide range of biological processes, both pathogenic and functional. In bacteria, functional amyloids are involved in forming biofilms, storing toxins, overcoming the surface tension, and other functions.

Indexed as

Amyloidamyloidogenic regioncompositionally biased regionproteobacteriaproteomicsRhizobialesroot nodule bacteriaSARPWaltz

Identifiers

PMID29720870
PMCPMC5922492
OpenAlexW2797939803

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.