Evidence map›Paper›PMID 38466778›Full record

ArticleACS chemical neuroscience2024

Rational Design of TDP-43 Derived α-Helical Peptide Inhibitors: An

Muthu Raj Salaikumaran, Pallavi P Gopal

Open access · greenAbstract read
In one paragraph

Article in ACS chemical neuroscience, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

2 citing papers in PubMed, 3 citations in OpenAlex.

  1. Article
  2. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Muthu Raj SalaikumaranDepartment of Pathology, Yale School of Medicine, New Haven, Connecticut 06520, United States.ORCID 0000-0003-2440-2832
Pallavi P GopalDepartment of Pathology, Yale School of Medicine, New Haven, Connecticut 06520, United States.
Yale University · US

Funding

Role of Ataxin-2 polyglutamine expansion on TDP-43 transport and post-transcriptional RNA regulation in neuronsR01NS122907 · NINDS · YALE UNIVERSITY · PI GOPAL, PALLAVI P. · 2021 to 2025
$2.1M
NINDS NIH HHS R01 NS122907
6 · The paper itself

Abstract

TDP-43, an essential RNA/DNA-binding protein, is central to the pathology of neurodegenerative diseases, such as amyotrophic lateral sclerosis and frontotemporal dementia. Pathological mislocalization and aggregation of TDP-43 disrupt RNA splicing, mRNA stability, and mRNA transport, thereby impairing neuronal function and survival. The formation of amyloid-like TDP-43 filaments is largely facilitated by the destabilization of an α-helical segment within the disordered C-terminal region. In this study, we hypothesized that preventing the destabilization of the α-helical domain could potentially halt the growth of these pathological filaments. To explore this, we utilized a range of

Indexed as

Amyotrophic Lateral SclerosisPeptidesDNA-Binding ProteinsHumansMolecular Docking SimulationProtein Conformation, alpha-HelicalDNA-Binding ProteinsPeptidesaggregationhelical propensity peptideneurodegenerative diseaseTDP-43

Identifiers

PMID38466778
PMCPMC10959110
OpenAlexW4392638794

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.