Evidence map›Paper›PMID 28960135›Full record

ReviewPrion2017

Amyloids and prions in plants: Facts and perspectives.

K S Antonets, A A Nizhnikov

Open access · goldAbstract readReview
In one paragraph

Review in Prion, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

14 citing papers in PubMed, 31 citations in OpenAlex.

  1. Review
  2. Biochemistry · 2023
    Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Review
  14. Predicting Amyloidogenic Proteins in the Proteomes of Plants.International journal of molecular sciences · 2017
    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.

K S Antonetsa All-Russia Research Institute for Agricultural Microbiology , St. Petersburg , Russian Federation.
A A Nizhnikova All-Russia Research Institute for Agricultural Microbiology , St. Petersburg , Russian Federation.ORCID http://orcid.org/0000-0002-8338-3494
St Petersburg University · RU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Amyloids represent protein fibrils that have highly ordered structure with unique physical and chemical properties. Amyloids have long been considered lethal pathogens that cause dozens of incurable diseases in humans and animals. Recent data show that amyloids may not only possess pathogenic properties but are also implicated in the essential biological processes in a variety of prokaryotes and eukaryotes. Functional amyloids have been identified in archaea, bacteria, fungi, and animals, including humans. Plants are one of the most poorly studied groups of organisms in the field of amyloid biology. Although amyloid properties have not been shown under native conditions for any plant protein, studies demonstrating amyloid properties for a set of plant proteins in vitro or in heterologous systems in vivo have been published in recent years. In this review, we systematize the data on the amyloidogenic proteins of plants and their functions and discuss the perspectives of identifying novel amyloids using bioinformatic and proteomic approaches.

Indexed as

AmyloidAnimalsArabidopsisChlorophytaHumansPlant ProteinsPrion ProteinsProteomicsAmyloidPlant ProteinsPrion ProteinsAFPAmyloidA. thalianaLDplantprionPSIASARPS. cerevisiaeWALTZyeast

Identifiers

PMID28960135
PMCPMC5639834
OpenAlexW2760234660

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.