Evidence map›Paper›PMID 24349167›Full record

ArticlePloS one2013

Carnosine's effect on amyloid fibril formation and induced cytotoxicity of lysozyme.

Josephine W Wu, Kuan-Nan Liu, Su-Chun How, Wei-An Chen, Chia-Min Lai, Hwai-Shen Liu, Chaur-Jong Hu, Steven S-S Wang

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

15 citing papers in PubMed, 67 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

8 authors at 3 institutions in 1 country.

Josephine W WuDepartment of Optometry, Central Taiwan University of Science and Technology, Taichung, Taiwan.
Kuan-Nan LiuDepartment of Chemical Engineering, National Taiwan University, Taipei, Taiwan.
Su-Chun HowDepartment of Chemical Engineering, National Taiwan University, Taipei, Taiwan.
Wei-An ChenDepartment of Chemical Engineering, National Taiwan University, Taipei, Taiwan.
Chia-Min LaiDepartment of Chemical Engineering, National Taiwan University, Taipei, Taiwan.
Hwai-Shen LiuDepartment of Chemical Engineering, National Taiwan University, Taipei, Taiwan.
Chaur-Jong HuDepartment of Neurology, Shuang Ho Hospital, Taipei Medical University, New Taipei City, Taiwan.
Steven S-S WangDepartment of Chemical Engineering, National Taiwan University, Taipei, Taiwan.
National Taiwan University · TWCentral Taiwan University of Science and Technology · TWTaipei Medical University-Shuang Ho Hospital · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Carnosine, a common dipeptide in mammals, has previously been shown to dissemble alpha-crystallin amyloid fibrils. To date, the dipeptide's anti-fibrillogensis effect has not been thoroughly characterized in other proteins. For a more complete understanding of carnosine's mechanism of action in amyloid fibril inhibition, we have investigated the effect of the dipeptide on lysozyme fibril formation and induced cytotoxicity in human neuroblastoma SH-SY5Y cells. Our study demonstrates a positive correlation between the concentration and inhibitory effect of carnosine against lysozyme fibril formation. Molecular docking results show carnosine's mechanism of fibrillogenesis inhibition may be initiated by binding with the aggregation-prone region of the protein. The dipeptide attenuates the amyloid fibril-induced cytotoxicity of human neuronal cells by reducing both apoptotic and necrotic cell deaths. Our study provides solid support for carnosine's amyloid fibril inhibitory property and its effect against fibril-induced cytotoxicity in SH-SY5Y cells. The additional insights gained herein may pave way to the discovery of other small molecules that may exert similar effects against amyloid fibril formation and its associated neurodegenerative diseases.

Indexed as

AmyloidAnimalsApoptosisAvian ProteinsBinding SitesCarnosineCell Line, TumorChickensHumansMolecular Docking SimulationMuramidaseNeuronsProtein BindingAmyloidAvian ProteinsCarnosineMuramidase

Identifiers

PMID24349167
PMCPMC3859581
OpenAlexW2003606250

What OpenQuestion holds

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LicenceCC BY
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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.