Evidence map›Paper›PMID 36499499›Full record

ArticleInternational journal of molecular sciences2022

Acetylation State of Lysine 14 of Histone H3.3 Affects Mutant Huntingtin Induced Pathogenesis.

Anikó Faragó, Nóra Zsindely, Anita Farkas, Alexandra Neller, Fruzsina Siági, Márton Richárd Szabó, Tamás Csont, László Bodai

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

Article in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.9field-weighted citation impact, top 30% 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

7 citing papers in PubMed, 9 citations in OpenAlex.

  1. Review
  2. Decoding Nucleotide Repeat Expansion Diseases: Novel Insights fromInternational journal of molecular sciences · 2024
    Review
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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

8 authors at 1 institution in 1 country.

Anikó FaragóDepartment of Biochemistry and Molecular Biology, Faculty of Science and Informatics, University of Szeged, Közép fasor 52, H-6726 Szeged, Hungary.
Nóra ZsindelyDepartment of Biochemistry and Molecular Biology, Faculty of Science and Informatics, University of Szeged, Közép fasor 52, H-6726 Szeged, Hungary.ORCID 0000-0002-6189-3100
Anita FarkasDepartment of Biochemistry and Molecular Biology, Faculty of Science and Informatics, University of Szeged, Közép fasor 52, H-6726 Szeged, Hungary.
Alexandra NellerDepartment of Biochemistry and Molecular Biology, Faculty of Science and Informatics, University of Szeged, Közép fasor 52, H-6726 Szeged, Hungary.
Fruzsina SiágiDepartment of Biochemistry and Molecular Biology, Faculty of Science and Informatics, University of Szeged, Közép fasor 52, H-6726 Szeged, Hungary.
Márton Richárd SzabóDepartment of Biochemistry, Albert Szent-Györgyi Medical School, University of Szeged, H-6720 Szeged, Hungary.ORCID 0000-0003-0415-5192
Tamás CsontDepartment of Biochemistry, Albert Szent-Györgyi Medical School, University of Szeged, H-6720 Szeged, Hungary.
László BodaiDepartment of Biochemistry and Molecular Biology, Faculty of Science and Informatics, University of Szeged, Közép fasor 52, H-6726 Szeged, Hungary.ORCID 0000-0001-8411-626X
University of Szeged · HU

Funding

Resource Component: Acquisition, maintenance and distribution of Drosophila stocksP40OD018537 · OD · TRUSTEES OF INDIANA UNIVERSITY · PI Annette L. Parks · 2014 to 2026
$13.5M
Hungarian Academy of Sciences BO/00522/19/8Hungarian National Research, Development and Innovation Office (NKFIH) K-143889Hungarian National Research, Development and Innovation Office (NKFIH) TKP2021-EGA-32Ministry for Innovation and Technology ÚNKP-19-3-SZTE-72Ministry for Innovation and Technology UNKP-21-5-SZTE-574National Research, Development and Innovation Office GINOP-2.3.2-15-2016-00032National Research, Development and Innovation Office GINOP-2.3.2-15-2016-00034National Research, Development and Innovation Office K-112294NIH HHS P40 OD018537
6 · The paper itself

Abstract

Huntington's Disease (HD) is a fatal neurodegenerative disorder caused by the expansion of a polyglutamine-coding CAG repeat in the

Indexed as

HistonesHuntington DiseaseAcetylationAnimalsDrosophilaHistone AcetyltransferasesHistone DeacetylasesLysineProtein Processing, Post-TranslationalHistone AcetyltransferasesHistone DeacetylasesHistonesLysineanimal modelDrosophilaepigeneticshistonehistone acetylationHuntington’s diseaseneurodegeneration

Identifiers

PMID36499499
PMCPMC9738228
OpenAlexW4311629963

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.