Evidence map›Paper›PMID 32272787›Full record

ArticleInternational journal of molecular sciences2020

Conformational Characterization of Native and L17A/F19A-Substituted Dutch-Type β-Amyloid Peptides.

Kai-Cyuan He, Yi-Ru Chen, Chu-Ting Liang, Shi-Jie Huang, Chung-Ying Tzeng, Chi-Fon Chang, Shing-Jong Huang, Hsien-Bin Huang, Ta-Hsien Lin

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.6field-weighted citation impact, top 33% 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

5 citing papers in PubMed, 6 citations in OpenAlex.

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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

9 authors at 5 institutions in 1 country.

Kai-Cyuan HeBasic Research Division, Medical Research Department, Taipei Veterans General Hospital, Taipei 11217, Taiwan.
Yi-Ru ChenDepartment and Institute of Pharmacology, National Yang-Ming University, Taipei 11221, Taiwan.
Chu-Ting LiangBasic Research Division, Medical Research Department, Taipei Veterans General Hospital, Taipei 11217, Taiwan.
Shi-Jie HuangInstitute of Biochemistry & Molecular Biology, National Yang-Ming University, Taipei 11221, Taiwan.
Chung-Ying TzengDepartment of Life Sciences and Institute of Genome Sciences, National Yang-Ming University, Taipei 11221, Taiwan.
Chi-Fon ChangGenomics Research Center, Academia Sinica, Taipei 11529, Taiwan.
Shing-Jong HuangInstrumentation Center, National Taiwan University, Taipei 10617, Taiwan.
Hsien-Bin HuangDepartment of Life Science and the Institute of Molecular Biology, National Chung Cheng University, Chia-yi 62102, Taiwan.
Ta-Hsien LinBasic Research Division, Medical Research Department, Taipei Veterans General Hospital, Taipei 11217, Taiwan.
National Yang Ming Chiao Tung University · TWNational Taiwan University · TWTaipei Veterans General Hospital · TWGenomics Research Center, Academia Sinica · TWNational Chung Cheng University · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Some mutations which occur in the α/β-discordant region (resides 15 to 23) of β-amyloid peptide (Aβ) lead to familial Alzheimer's disease (FAD). In vitro studies have shown that these genetic mutations could accelerate Aβ aggregation. We recently showed that mutations in this region could alter the structural propensity, resulting in a different aggregative propensity of Aβ. Whether these genetic mutations display similar effects remains largely unknown. Here, we characterized the structural propensity and aggregation kinetics of Dutch-type Aβ

Indexed as

Alzheimer DiseaseAmino Acid SubstitutionAmyloid beta-PeptidesHumansMutationPeptide FragmentsProtein Structure, SecondarySodium Dodecyl SulfateAmyloid beta-PeptidesPeptide FragmentsSodium Dodecyl SulfateAβCDDutch-type mutationE22QFADfamilial Alzheimer’s diseaseNMRα/β-discordantβ-amyloid peptide

Identifiers

PMID32272787
PMCPMC7177254
OpenAlexW3015832063

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.