Evidence map›Paper›PMID 37265546›Full record

ArticlePNAS nexus2023

Cholesterol twists the transmembrane Di-Gly region of amyloid-precursor protein.

David Tzu-Wei Wang, Tiffany Y C Tang, Chun-Ting Kuo, Yun-Ting Yu, Eric H L Chen, Ming-Tao Lee, Ruei-Fong Tsai, Hung-Ying Chen, Yun-Wei Chiang, Rita P Y Chen

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in PNAS nexus, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.2field-weighted citation impact, top 49% 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

1 citing paper in PubMed, 1 citations in OpenAlex.

  1. 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

10 authors at 4 institutions in 1 country.

David Tzu-Wei WangInstitute of Biological Chemistry, Academia Sinica, Taipei 11529, Taiwan.
Tiffany Y C TangInstitute of Biological Chemistry, Academia Sinica, Taipei 11529, Taiwan.
Chun-Ting KuoInstitute of Biological Chemistry, Academia Sinica, Taipei 11529, Taiwan.
Yun-Ting YuInstitute of Biological Chemistry, Academia Sinica, Taipei 11529, Taiwan.
Eric H L ChenInstitute of Biological Chemistry, Academia Sinica, Taipei 11529, Taiwan.
Ming-Tao LeeLife Science Group, Scientific Research Division, National Synchrotron Radiation Research Center, Hsinchu 30076, Taiwan.ORCID https://orcid.org/0000-0002-9313-6075
Ruei-Fong TsaiDepartment of Chemistry, National Tsing Hua University, Hsinchu 300044, Taiwan.
Hung-Ying ChenDepartment of Chemistry, National Tsing Hua University, Hsinchu 300044, Taiwan.
Yun-Wei ChiangDepartment of Chemistry, National Tsing Hua University, Hsinchu 300044, Taiwan.ORCID https://orcid.org/0000-0002-2101-8918
Rita P Y ChenInstitute of Biological Chemistry, Academia Sinica, Taipei 11529, Taiwan.
National Taiwan University · TWNational Tsing Hua University · TWInstitute of Biological Chemistry, Academia Sinica · TWNational Central University · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nearly 95% of Alzheimer's disease (AD) occurs sporadically without genetic linkage. Aging, hypertension, high cholesterol content, and diabetes are known nongenomic risk factors of AD. Aggregation of Aβ peptides is an initial event of AD pathogenesis. Aβ peptides are catabolic products of a type I membrane protein called amyloid precursor protein (APP). Aβ40 is the major product, whereas the 2-residue-longer version, Aβ42, induces amyloid plaque formation in the AD brain. Since cholesterol content is one risk factor for sporadic AD, we aimed to explore whether cholesterol in the membrane affects the structure of the APP transmembrane region, thereby modulating the γ-secretase cutting behavior. Here, we synthesized several peptides containing the APP transmembrane region (sequence 693-726, corresponding to the Aβ

Indexed as

Alzheimer's diseaseamyloid precursor proteinAβcholesterolelectron spin resonance spectroscopylamellar X-ray diffractionorientated circular dichroism spectroscopytransmembrane helix

Identifiers

PMID37265546
PMCPMC10230161
OpenAlexW4377044127

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.