Evidence map›Paper›PMID 24594588›Full record

ArticlePloS one2014

Effect of C-terminal residues of Aβ on copper binding affinity, structural conversion and aggregation.

Shu-Hsiang Huang, Shyue-Chu Ke, Ta-Hsin Lin, Hsin-Bin Huang, Yi-Cheng Chen

Abstract read
In one paragraph

Article in PloS one, 2014. 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
–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

5 citing papers in PubMed.

  1. Review
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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

5 authors.

Shu-Hsiang HuangDepartment of Medicine, MacKay Medical College, New Taipei City, Taiwan.
Shyue-Chu KeDepartment of Physics, National Dong Hwa University, Hualien, Taiwan.
Ta-Hsin LinDepartment of Medical Research & Education, Taipei Veterans General Hospital, Taipei city, Taiwan; Institute of Biochemistry, National Yang-Ming University, Taipei, Taiwan.
Hsin-Bin HuangInstitute of Molecular Biology, National Chung-Cheng University, Chiayi, Taiwan.
Yi-Cheng ChenDepartment of Medicine, MacKay Medical College, New Taipei City, Taiwan.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Many properties of Aβ such as toxicity, aggregation and ROS formation are modulated by Cu2+. Previously, the coordination configuration and interaction of Cu2+ with the Aβ N-terminus has been extensively studied. However, the effect of Aβ C-terminal residues on related properties is still unclear. In the present study, several C-terminus-truncated Aβ peptides, including Aβ1-40, Aβ1-35, Aβ1-29, Aβ1-24 and Aβ1-16, were synthesized to characterize the effect of Aβ C-terminal residues on Cu2+ binding affinity, structure, aggregation ability and ROS formation. Results show that the Aβ C-terminal residues have effect on Cu2+ binding affinity, aggregation ability and inhibitory ability of ROS formation. Compared to the key residues responsible for Aβ aggregation and structure in the absence of Cu2+, it is more likely that residues 36-40, rather than residues 17-21 and 30-35, play a key role on the related properties of Aβ in the presence of Cu2+.

Indexed as

Amyloid beta-PeptidesCircular DichroismCopperElectron Spin Resonance SpectroscopyMicroscopy, Electron, TransmissionProtein Structure, SecondaryReactive Oxygen SpeciesSpectrometry, FluorescenceAmyloid beta-PeptidesCopperReactive Oxygen Species

Identifiers

PMID24594588
PMCPMC3940864

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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.