Evidence map›Paper›PMID 42958598›Full record

ReviewTranslational neurodegeneration2026

The pathological roles of intrinsically disordered proteins in lysosomal acidification dysfunction in neurodegenerative diseases.

Kholoud Abd-ElRaouf, Dylan T Murphy, Lenny Yi Tong Cheong, Jialiu Zeng, Chih Hung Lo

Abstract readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in Translational neurodegeneration, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

5 authors.

Kholoud Abd-ElRaouf *Department of Biology, Syracuse University, Syracuse, NY, 13244, USA.
Dylan T Murphy *Department of Biology, Syracuse University, Syracuse, NY, 13244, USA.
Lenny Yi Tong CheongSchool of Biological Sciences, Nanyang Technological University, Singapore, Singapore, 637551, Singapore.
Jialiu ZengInterdisciplinary Neuroscience Program, Syracuse University, Syracuse, NY, 13244, USA.
Chih Hung LoDepartment of Biology, Syracuse University, Syracuse, NY, 13244, USA. clo101@syr.edu.

Funding

Alzheimer's Association Research Grant 25AARG-1375299Syracuse University Start-up grant
6 · The paper itself

Abstract

Neurodegenerative diseases such as Alzheimer's disease (AD), frontotemporal dementia (FTD), and Parkinson's disease (PD) are characterized by the accumulation of intrinsically disordered proteins (IDPs), including amyloid-β (Aβ), tau, and α-synuclein (αSyn). These proteins disrupt neuronal homeostasis through toxic aggregation, impaired proteostasis, and progressive neurodegeneration, in part via dysfunction of the autophagy-lysosomal pathway (ALP). A central feature of this impairment is defective vacuolar-type (H

Indexed as

Intrinsically Disordered ProteinsLysosomesNeurodegenerative DiseasesAnimalsAutophagyHumansIntrinsically Disordered ProteinsAutophagyIntrinsically disordered proteinsLysosomal acidificationNeuroinflammation and neurodegenerationProtein degradationTherapeutic strategies

Identifiers

PMID42958598
PMCPMC13718103

What OpenQuestion holds

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Registered trials

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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.