Evidence map›Paper›PMID 34424055›Full record

ArticleMolecular and cellular biology2021

Huntingtin Polyglutamine Fragments Are a Substrate for Hsp104 in Saccharomyces cerevisiae.

Nicole J Wayne, Katherine E Dembny, Tyler Pease, Farrin Saba, Xiaohong Zhao, Daniel C Masison, Lois E Greene

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

Article in Molecular and cellular biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.4field-weighted citation impact, top 46% 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

4 citing papers in PubMed, 4 citations in OpenAlex.

  1. Article
  2. The value of exosome-derived noncoding RNAs in colorectal cancer proliferation, metastasis, and clinical applications.Clinical & translational oncology : official publication of the Federation of Spanish Oncology Societies and of the National Cancer Institute of Mexico · 2022
    Review
  3. Article
  4. Review
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.

Nicole J WayneLaboratory of Cell Biology, National Heart, Lung, and Blood Institute, National Institutes of Healthgrid.94365.3d, Bethesda, Maryland, USA.
Katherine E DembnyLaboratory of Cell Biology, National Heart, Lung, and Blood Institute, National Institutes of Healthgrid.94365.3d, Bethesda, Maryland, USA.
Tyler PeaseLaboratory of Cell Biology, National Heart, Lung, and Blood Institute, National Institutes of Healthgrid.94365.3d, Bethesda, Maryland, USA.
Farrin SabaLaboratory of Cell Biology, National Heart, Lung, and Blood Institute, National Institutes of Healthgrid.94365.3d, Bethesda, Maryland, USA.
Xiaohong ZhaoLaboratory of Cell Biology, National Heart, Lung, and Blood Institute, National Institutes of Healthgrid.94365.3d, Bethesda, Maryland, USA.
Daniel C MasisonLaboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Healthgrid.94365.3d, Bethesda, Maryland, USA.
Lois E GreeneLaboratory of Cell Biology, National Heart, Lung, and Blood Institute, National Institutes of Healthgrid.94365.3d, Bethesda, Maryland, USA.ORCID 0000-0003-3786-8594
National Institutes of Health · US

Funding

Role of molecular chaperones in protein folding diseasesZIAHL000516 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI GREENE, LOIS · 2009 to 2022
$19.6M
Chaperone-amyloid interactionsZIADK024954 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI MASISON, DANIEL · 2009 to 2025
$3.8M
Intramural NIH HHS ZIA HL000516
6 · The paper itself

Abstract

The aggregation of huntingtin fragments with expanded polyglutamine repeat regions (HttpolyQ) that cause Huntington's disease depends on the presence of a prion with an amyloid conformation in yeast. As a result of this relationship, HttpolyQ aggregation indirectly depends on Hsp104 due to its essential role in prion propagation. We find that HttQ103 aggregation is directly affected by Hsp104 with and without the presence of [

Indexed as

CopperGalactokinaseHeat-Shock ProteinsHumansHuntingtin ProteinHuntington DiseasePeptidesPlaque, AmyloidPrionsPromoter Regions, GeneticProtein Aggregation, PathologicalSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsCopperGAL1 protein, S cerevisiaeGalactokinaseHeat-Shock ProteinsHsP104 protein, S cerevisiaeHuntingtin ProteinPeptidespolyglutaminePrionsSaccharomyces cerevisiae ProteinsamyloidHsp104Huntington’s diseaseprionsyeast

Identifiers

PMID34424055
PMCPMC8547424
OpenAlexW3195962418

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.