Evidence map›Paper›PMID 33835818›Full record

ArticleThe journal of physical chemistry. B2021

Tryptophan Probes of TDP-43 C-Terminal Domain Amyloid Formation.

Sydney O Shuster, Jennifer C Lee

Open access · greenAbstract read
In one paragraph

Article in The journal of physical chemistry. B, 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
0.8field-weighted citation impact, top 26% 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, 10 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
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

2 authors at 1 institution in 1 country.

Sydney O ShusterLaboratory of Protein Conformation and Dynamics, Biochemistry and Biophysics Center, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland 20892, United States.
Jennifer C LeeLaboratory of Protein Conformation and Dynamics, Biochemistry and Biophysics Center, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland 20892, United States.ORCID 0000-0003-0506-8349
National Institutes of Health · US

Funding

Protein Misfolding and AggregationZIAHL001055 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI LEE, JENNIFER · 2009 to 2025
$16.9M
Intramural NIH HHS ZIA HL001055
6 · The paper itself

Abstract

Aggregated TAR DNA-binding protein 43 (TDP-43) forms the cytoplasmic hallmarks associated with patients suffering from amyotrophic lateral sclerosis and frontotemporal lobar degeneration with ubiquitin. Under normal conditions, TDP-43 is a 414-amino acid protein; however, aggregates are enriched with N-terminal truncations which contain residues 267-414, known as the C-terminal domain of TDP-43 (TDP-43

Indexed as

AmyloidDNA-Binding ProteinsTryptophanAmyloidogenic ProteinsAmyotrophic Lateral SclerosisHumansAmyloidAmyloidogenic ProteinsDNA-Binding ProteinsTARDBP protein, humanTryptophan

Identifiers

PMID33835818
PMCPMC8080960
OpenAlexW3145657363

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.