Evidence map›Paper›PMID 28137911›Full record

ArticleMolecular and cellular biology2017

Effects of Mutations on the Aggregation Propensity of the Human Prion-Like Protein hnRNPA2B1.

Kacy R Paul, Amandine Molliex, Sean Cascarina, Amy E Boncella, J Paul Taylor, Eric D Ross

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

29 citing papers in PubMed, 35 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Structural Bases of Prion Variation in Yeast.International journal of molecular sciences · 2022
    Review
  7. Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Review
  14. 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
  15. Article
  16. Review
  17. Review
  18. 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

6 authors at 2 institutions in 1 country.

Kacy R PaulDepartment of Biochemistry & Molecular Biology, Colorado State University, Fort Collins, Colorado, USA.
Amandine MolliexDepartment of Cell and Molecular Biology, St. Jude Children's Research Hospital, Memphis, Tennessee, USA.
Sean CascarinaDepartment of Biochemistry & Molecular Biology, Colorado State University, Fort Collins, Colorado, USA.
Amy E BoncellaDepartment of Chemistry, Colorado State University, Fort Collins, Colorado, USA.
J Paul TaylorDepartment of Cell and Molecular Biology, St. Jude Children's Research Hospital, Memphis, Tennessee, USA.
Eric D RossDepartment of Biochemistry & Molecular Biology, Colorado State University, Fort Collins, Colorado, USA Eric.Ross@ColoState.Edu.ORCID http://orcid.org/0000-0002-6473-9977
Colorado State University · USSt. Jude Children's Research Hospital · US

Funding

Dynamic RNA-protein assemblies and neurological diseaseR35NS097974 · NINDS · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI TAYLOR, JOSEPH PAUL · 2017 to 2024
$7.2M
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 GM105991NINDS NIH HHS R35 NS097974
6 · The paper itself

Abstract

Hundreds of human proteins contain prion-like domains, which are a subset of low-complexity domains with high amino acid compositional similarity to yeast prion domains. A recently characterized mutation in the prion-like domain of the human heterogeneous nuclear ribonucleoprotein hnRNPA2B1 increases the aggregation propensity of the protein and causes multisystem proteinopathy. The mutant protein forms cytoplasmic inclusions when expressed in

Indexed as

Protein AggregatesAlgorithmsAmino AcidsAmyloidAnimalsDrosophila melanogasterHeterogeneous-Nuclear Ribonucleoprotein Group A-BHumansHydrophobic and Hydrophilic InteractionsMutationPrionsProtein DomainsAmino AcidsAmyloidHeterogeneous-Nuclear Ribonucleoprotein Group A-BhnRNP A2PrionsProtein Aggregatesaggregationlow-complexity domainprion-likeprions

Identifiers

PMID28137911
PMCPMC5376634
OpenAlexW2580158211

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.