Evidence map›Paper›PMID 34009955›Full record

ArticleBiochemistry2021

Fungally Derived Isoquinoline Demonstrates Inducer-Specific Tau Aggregation Inhibition.

David J Ingham, Bryce R Blankenfeld, Shibin Chacko, Chamani Perera, Berl R Oakley, Truman Christopher Gamblin

Open access · hybridAbstract read
In one paragraph

Article in Biochemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.8field-weighted citation impact, top 29% 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

3 citing papers in PubMed, 7 citations in OpenAlex.

  1. Disrupting pathologic phase transitions in neurodegeneration.The Journal of clinical investigation · 2023
    Review
  2. Article
  3. Biochemistry · 2022
    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

6 authors at 1 institution in 1 country.

David J InghamDepartment of Molecular Biosciences, University of Kansas, Lawrence, Kansas 66045, United States.
Bryce R BlankenfeldDepartment of Molecular Biosciences, University of Kansas, Lawrence, Kansas 66045, United States.
Shibin ChackoSynthetic Chemical Biology Core Facility, University of Kansas, Lawrence, Kansas 66047, United States.
Chamani PereraSynthetic Chemical Biology Core Facility, University of Kansas, Lawrence, Kansas 66047, United States.
Berl R OakleyDepartment of Molecular Biosciences, University of Kansas, Lawrence, Kansas 66045, United States.ORCID 0000-0002-3046-8240
Truman Christopher GamblinDepartment of Molecular Biosciences, University of Kansas, Lawrence, Kansas 66045, United States.ORCID 0000-0001-7498-1524
University of Kansas · US

Funding

Synthetic Chemical Biology CoreP20GM113117 · NIGMS · UNIVERSITY OF KANSAS LAWRENCE · PI OROZCO, ROBIN C. · 2016 to 2025
$23.9M
Understanding the mechanobiology of stem cells in a microengineered 3D cardiac tissue environment with cardiomyopathyP20GM103638 · NIGMS · UNIVERSITY OF KANSAS LAWRENCE · PI LUNTE, SUSAN M · 2012 to 2021
$22.1M
TRAINING GRANT IN DYNAMIC ASPECTS OF CHEMICAL BIOLOGYT32GM008545 · NIGMS · UNIVERSITY OF KANSAS LAWRENCE · PI LAMB, AUDREY L · 1994 to 2019
$4.9M
Development of in vitro disease-relevant strains of tauR21AG069112 · NIA · UNIVERSITY OF TEXAS SAN ANTONIO · PI GAMBLIN, TRUMAN C · 2020 to 2020
$405k
NIA NIH HHS R21 AG069112NIGMS NIH HHS P20 GM103638NIGMS NIH HHS P20 GM113117NIGMS NIH HHS T32 GM008545
6 · The paper itself

Abstract

The microtubule-associated protein tau promotes the stabilization of the axonal cytoskeleton in neurons. In several neurodegenerative diseases, such as Alzheimer's disease, tau has been found to dissociate from microtubules, leading to the formation of pathological aggregates that display an amyloid fibril-like structure. Recent structural studies have shown that the tau filaments isolated from different neurodegenerative disorders have structurally distinct fibril cores that are specific to the disease. These "strains" of tau fibrils appear to propagate between neurons in a prion-like fashion that maintains their initial template structure. In addition, the strains isolated from diseased tissue appear to have structures that are different from those made by the most commonly used

Indexed as

Alzheimer DiseaseAmyloidAspergillus nidulansFungiHumansIsoquinolinesMicrotubulesNeuronsPrionsProtein AggregatesProtein Aggregation, PathologicalStructure-Activity RelationshipTauopathiestau ProteinsAmyloidisoquinolineIsoquinolinesPrionsProtein Aggregatestau Proteins

Identifiers

PMID34009955
PMCPMC8173610
OpenAlexW3160163679

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.