Evidence map›Paper›PMID 36834792›Full record

ReviewInternational journal of molecular sciences2023

Aggregation of Disordered Proteins Associated with Neurodegeneration.

Phoebe S Tsoi, My Diem Quan, Josephine C Ferreon, Allan Chris M Ferreon

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
17.3field-weighted citation impact, top 1% 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

47 citing papers in PubMed, 84 citations in OpenAlex.

  1. Proteostasis (in)action: the role of co-pathologies in neurodegenerative disease.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026
    Review
  2. Article
  3. Combination Pharmacology for ALS: A Mechanistic Rationale.International journal of molecular sciences · 2026
    Review
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  7. Accurate conformational ensembles of intrinsically disordered proteins using reweighting based on NMR chemical shifts.Proceedings of the National Academy of Sciences of the United States of America · 2026
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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

4 authors at 1 institution in 1 country.

Phoebe S TsoiDepartment of Pharmacology and Chemical Biology, Baylor College of Medicine, Houston, TX 77030, USA.
My Diem QuanDepartment of Pharmacology and Chemical Biology, Baylor College of Medicine, Houston, TX 77030, USA.
Josephine C FerreonDepartment of Pharmacology and Chemical Biology, Baylor College of Medicine, Houston, TX 77030, USA.
Allan Chris M FerreonDepartment of Pharmacology and Chemical Biology, Baylor College of Medicine, Houston, TX 77030, USA.ORCID 0000-0002-8538-1732
Baylor College of Medicine · US

Funding

Structure and Functionof Nanog in Stem Cell PluripotencyR01GM122763 · NIGMS · BAYLOR COLLEGE OF MEDICINE · PI Josephine Chu Ferreon · 2018 to 2026
$3.4M
Phase Transition-Mediated Tau Function and DysfunctionR01NS105874 · NINDS · BAYLOR COLLEGE OF MEDICINE · PI FERREON, ALLAN CHRIS · 2019 to 2023
$2.0M
Pharmacologic inhibition of ribonucleoprotein droplet maturationR21NS109678 · NINDS · BAYLOR COLLEGE OF MEDICINE · PI FERREON, ALLAN CHRIS · 2019 to 2019
$440k
Mechanism of Pathologic hnRNP Droplet MaturationR21NS107792 · NINDS · BAYLOR COLLEGE OF MEDICINE · PI FERREON, ALLAN CHRIS · 2019 to 2019
$439k
NIGMS NIH HHS R01 GM122763NINDS NIH HHS R01 NS105874NINDS NIH HHS R21 NS107792NINDS NIH HHS R21 NS109678
6 · The paper itself

Abstract

Cellular deposition of protein aggregates, one of the hallmarks of neurodegeneration, disrupts cellular functions and leads to neuronal death. Mutations, posttranslational modifications, and truncations are common molecular underpinnings in the formation of aberrant protein conformations that seed aggregation. The major proteins involved in neurodegeneration include amyloid beta (Aβ) and tau in Alzheimer's disease, α-synuclein in Parkinson's disease, and TAR DNA-binding protein (TDP-43) in amyotrophic lateral sclerosis (ALS). These proteins are described as intrinsically disordered and possess enhanced ability to partition into biomolecular condensates. In this review, we discuss the role of protein misfolding and aggregation in neurodegenerative diseases, specifically highlighting implications of changes to the primary/secondary (mutations, posttranslational modifications, and truncations) and the quaternary/supramolecular (oligomerization and condensation) structural landscapes for the four aforementioned proteins. Understanding these aggregation mechanisms provides insights into neurodegenerative diseases and their common underlying molecular pathology.

Indexed as

Alzheimer DiseaseAmyotrophic Lateral SclerosisIntrinsically Disordered ProteinsNeurodegenerative DiseasesParkinson DiseaseAmyloid beta-PeptidesHumanstau ProteinsAmyloid beta-PeptidesIntrinsically Disordered Proteinstau ProteinsAlphaFoldAβbiomolecular condensatesintrinsically disordered proteinsliquid–liquid phase separationLLPSneurodegenerative diseasestauTDP-43α-synuclein

Identifiers

PMID36834792
PMCPMC9966039
OpenAlexW4319598987

What OpenQuestion holds

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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.