Evidence map›Paper›PMID 37239918›Full record

ArticleInternational journal of molecular sciences2023

Identification of New FG-Repeat Nucleoporins with Amyloid Properties.

Lavrentii G Danilov, Xenia V Sukhanova, Tatiana M Rogoza, Ekaterina Y Antonova, Nina P Trubitsina, Galina A Zhouravleva, Stanislav A Bondarev

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in International journal of molecular sciences, 2023. 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
0.9field-weighted citation impact, top 25% 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, 6 citations in OpenAlex.

  1. Article
  2. Review
  3. Advances in the understanding of nuclear pore complexes in human diseases.Journal of cancer research and clinical oncology · 2024
    Review
  4. Review
  5. The Aβ42 Peptide and IAPP Physically Interact in a Yeast-Based Assay.International journal of molecular sciences · 2023
    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

7 authors at 1 institution in 1 country.

Lavrentii G DanilovDepartment of Genetics and Biotechnology, St. Petersburg State University, 199034 St. Petersburg, Russia.ORCID 0000-0002-4479-3095
Xenia V SukhanovaDepartment of Genetics and Biotechnology, St. Petersburg State University, 199034 St. Petersburg, Russia.ORCID 0000-0001-7022-0832
Tatiana M RogozaDepartment of Genetics and Biotechnology, St. Petersburg State University, 199034 St. Petersburg, Russia.ORCID 0000-0003-2981-0421
Ekaterina Y AntonovaDepartment of Genetics and Biotechnology, St. Petersburg State University, 199034 St. Petersburg, Russia.
Nina P TrubitsinaDepartment of Genetics and Biotechnology, St. Petersburg State University, 199034 St. Petersburg, Russia.ORCID 0000-0002-8892-8043
Galina A ZhouravlevaDepartment of Genetics and Biotechnology, St. Petersburg State University, 199034 St. Petersburg, Russia.ORCID 0000-0002-3013-4662
Stanislav A BondarevDepartment of Genetics and Biotechnology, St. Petersburg State University, 199034 St. Petersburg, Russia.ORCID 0000-0003-3137-944X
St Petersburg University · RU

Funding

Russian Science Foundation 23-24-00186
6 · The paper itself

Abstract

Amyloids are fibrillar protein aggregates with a cross-β structure. More than two hundred different proteins with amyloid or amyloid-like properties are already known. Functional amyloids with conservative amyloidogenic regions were found in different organisms. Protein aggregation appears to be beneficial for the organism in these cases. Therefore, this property might be conservative for orthologous proteins. The amyloid aggregates of the CPEB protein were suggested to play an important role in the long-term memory formation in

Indexed as

Nuclear Pore Complex ProteinsSaccharomyces cerevisiae ProteinsAmyloidAmyloidogenic ProteinsAnimalsDrosophila melanogasterHumansMiceNuclear ProteinsRNA-Binding ProteinsSaccharomyces cerevisiaeAmyloidAmyloidogenic ProteinsFXR1 protein, humanNSP1 protein, S cerevisiaeNuclear Pore Complex ProteinsNuclear ProteinsNUP116 protein, S cerevisiaeNUP153 protein, humanNup153 protein, mouseRNA-Binding ProteinsSaccharomyces cerevisiae ProteinsamyloidsArchCandyC-DAGevolutionFG-repeatsnucleoporins

Identifiers

PMID37239918
PMCPMC10218210
OpenAlexW4376138604

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.