Evidence map›Paper›PMID 29243911›Full record

ArticleACS chemical neuroscience2018

Neurodegenerative Disease Proteinopathies Are Connected to Distinct Histone Post-translational Modification Landscapes.

Karen Chen, Seth A Bennett, Navin Rana, Huda Yousuf, Mohamed Said, Sadiqa Taaseen, Natalie Mendo, Steven M Meltser, Mariana P Torrente

Open access · greenAbstract read
In one paragraph

Article in ACS chemical neuroscience, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed, 1 pooled it
1.9field-weighted citation impact, top 14% 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

36 citing papers in PubMed, 1 synthesis or guideline pooled it, 45 citations in OpenAlex.

  1. Exploring dysregulated miRNAs in ALS: implications for disease pathogenesis and early diagnosis.Neurological sciences : official journal of the Italian Neurological Society and of the Italian Society of Clinical Neurophysiology · 2025
    Pooled it
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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

9 authors at 2 institutions in 1 country.

Karen ChenChemistry Department of Brooklyn College , Brooklyn , New York 11210 , United States.
Seth A BennettChemistry Department of Brooklyn College , Brooklyn , New York 11210 , United States.
Navin RanaChemistry Department of Brooklyn College , Brooklyn , New York 11210 , United States.
Huda YousufChemistry Department of Brooklyn College , Brooklyn , New York 11210 , United States.
Mohamed SaidChemistry Department of Brooklyn College , Brooklyn , New York 11210 , United States.
Sadiqa TaaseenChemistry Department of Brooklyn College , Brooklyn , New York 11210 , United States.
Natalie MendoChemistry Department of Brooklyn College , Brooklyn , New York 11210 , United States.
Steven M MeltserChemistry Department of Brooklyn College , Brooklyn , New York 11210 , United States.
Mariana P TorrenteChemistry Department of Brooklyn College , Brooklyn , New York 11210 , United States.ORCID 0000-0001-8220-2228
Brooklyn College · USThe Graduate Center, CUNY · US

Funding

Epigenetics In Neurodegenerative Disease: Targeting Histone Modifications in ALSK22NS091314 · NINDS · UNIVERSITY OF PENNSYLVANIA · PI TORRENTE, MARIANA PLAZAS · 2015 to 2017
$536k
NINDS NIH HHS K22 NS091314
6 · The paper itself

Abstract

Amyotrophic lateral sclerosis (ALS) and Parkinson's disease (PD) are devastating neurodegenerative diseases involving the progressive degeneration of neurons. No cure is available for patients diagnosed with these diseases. A prominent feature of both ALS and PD is the accumulation of protein inclusions in the cytoplasm of degenerating neurons; however, the particular proteins constituting these inclusions vary: the RNA-binding proteins TDP-43 and FUS are most notable in ALS, while α-synuclein aggregates into Lewy bodies in PD. In both diseases, genetic causes fail to explain the occurrence of a large proportion of cases, and thus, both are considered mostly sporadic. Despite mounting evidence for a possible role of epigenetics in the occurrence and progression of ALS and PD, epigenetic mechanisms in the context of these diseases remain mostly unexplored. Here we comprehensively delineate histone post-translational modification (PTM) profiles in ALS and PD yeast proteinopathy models. Remarkably, we find distinct changes in histone modification profiles for each. We detect the most striking changes in the context of FUS aggregation: changes in several histone marks support a global decrease in gene transcription. We also detect more modest changes in histone modifications in cells overexpressing TDP-43 or α-synuclein. Our results highlight a great need for the inclusion of epigenetic mechanisms in the study of neurodegeneration. We hope our work will pave the way for the discovery of more effective therapies to treat patients suffering from ALS, PD, and other neurodegenerative diseases.

Indexed as

Amyotrophic Lateral SclerosisDNA-Binding ProteinsHistonesHumansLewy BodiesNeurodegenerative DiseasesNeuronsProtein Processing, Post-TranslationalYeastsDNA-Binding ProteinsHistonesTARDBP protein, humanALSepigeneticsFUShistone modificationsParkinson’s diseaseTDP-43α-synuclein

Identifiers

PMID29243911
PMCPMC5906139
OpenAlexW2774884271

What OpenQuestion holds

Textmetadata
LicenceTDM
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.