Evidence map›Paper›PMID 28394888›Full record

ArticlePLoS computational biology2017

Amino acid composition predicts prion activity.

Fayyaz Ul Amir Afsar Minhas, Eric D Ross, Asa Ben-Hur

Open access · goldAbstract read
In one paragraph

Article in PLoS computational biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.1field-weighted citation impact, top 12% 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

21 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. Article
  3. Detecting anomalous proteins using deep representations.NAR genomics and bioinformatics · 2024
    Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Review
  11. Composition-based prediction and rational manipulation of prion-like domain recruitment to stress granules.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  12. Using protein engineering to understand and modulate aggregation.Current opinion in structural biology · 2020
    Review
  13. Article
  14. Article
  15. The molecular language of membraneless organelles.The Journal of biological chemistry · 2019
    Review
  16. Article
  17. Frontiers in physiology · 2019
    Article
  18. Article
  19. Article
  20. 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 2 institutions in 2 countries.

Fayyaz Ul Amir Afsar MinhasDepartment of Computer and Information Sciences, Pakistan Institute of Engineering and Applied Sciences, Islamabad, Pakistan.ORCID 0000-0001-9129-1189
Eric D RossDepartment of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, Colorado, United States of America.
Asa Ben-HurDepartment of Computer Science, Colorado State University, Fort Collins, Colorado, United States of America.ORCID 0000-0001-8269-6942
Colorado State University · USPakistan Institute of Engineering and Applied Sciences · PK

Funding

The determinants of aggregation and toxicity of prion-like domainsR01GM105991 · NIGMS · COLORADO STATE UNIVERSITY · PI ROSS, ERIC D · 2013 to 2017
$1.5M
NIGMS NIH HHS R01 GM105991
6 · The paper itself

Abstract

Many prion-forming proteins contain glutamine/asparagine (Q/N) rich domains, and there are conflicting opinions as to the role of primary sequence in their conversion to the prion form: is this phenomenon driven primarily by amino acid composition, or, as a recent computational analysis suggested, dependent on the presence of short sequence elements with high amyloid-forming potential. The argument for the importance of short sequence elements hinged on the relatively-high accuracy obtained using a method that utilizes a collection of length-six sequence elements with known amyloid-forming potential. We weigh in on this question and demonstrate that when those sequence elements are permuted, even higher accuracy is obtained; we also propose a novel multiple-instance machine learning method that uses sequence composition alone, and achieves better accuracy than all existing prion prediction approaches. While we expect there to be elements of primary sequence that affect the process, our experiments suggest that sequence composition alone is sufficient for predicting protein sequences that are likely to form prions. A web-server for the proposed method is available at http://faculty.pieas.edu.pk/fayyaz/prank.html, and the code for reproducing our experiments is available at http://doi.org/10.5281/zenodo.167136.

Indexed as

Amino Acid SequenceMachine LearningAmyloidAsparagineComputational BiologyGlutamineHumansPrionsYeastsAmyloidAsparagineGlutaminePrions

Identifiers

PMID28394888
PMCPMC5402983
OpenAlexW2605586296

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.