Evidence map›Paper›PMID 30909659›Full record

ReviewMolecules (Basel, Switzerland)2019

Contributions of Mass Spectrometry to the Identification of Low Molecular Weight Molecules Able to Reduce the Toxicity of Amyloid-β Peptide to Cell Cultures and Transgenic Mouse Models of Alzheimer's Disease.

Raluca Ştefănescu, Gabriela Dumitriṭa Stanciu, Andrei Luca, Ioana Cezara Caba, Bogdan Ionel Tamba, Cosmin Teodor Mihai

Open access · goldAbstract readReview
In one paragraph

Review in Molecules (Basel, Switzerland), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

16 citing papers in PubMed, 24 citations in OpenAlex.

  1. AβACS chemical neuroscience · 2023
    Article
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  9. NeuroinflammatoryFrontiers in pharmacology · 2021
    Review
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  11. Article
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  15. Article
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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

6 authors at 1 institution in 1 country.

Raluca ŞtefănescuCenter for Advanced Research and Development in Experimental Medicine (CEMEX), "Grigore T. Popa" University of Medicine and Pharmacy, 16 Universității Street, 700115 Iaşi, Romania. raluca.stefanescu@umfiasi.ro.
Gabriela Dumitriṭa StanciuCenter for Advanced Research and Development in Experimental Medicine (CEMEX), "Grigore T. Popa" University of Medicine and Pharmacy, 16 Universității Street, 700115 Iaşi, Romania. gabriela-dumitrita.s@umfiasi.ro.
Andrei LucaCenter for Advanced Research and Development in Experimental Medicine (CEMEX), "Grigore T. Popa" University of Medicine and Pharmacy, 16 Universității Street, 700115 Iaşi, Romania. andrei.g.luca@umfiasi.ro.
Ioana Cezara CabaCenter for Advanced Research and Development in Experimental Medicine (CEMEX), "Grigore T. Popa" University of Medicine and Pharmacy, 16 Universității Street, 700115 Iaşi, Romania. ioana-cezara.grigoriu@umfiasi.ro.
Bogdan Ionel TambaCenter for Advanced Research and Development in Experimental Medicine (CEMEX), "Grigore T. Popa" University of Medicine and Pharmacy, 16 Universității Street, 700115 Iaşi, Romania. bogdan.tamba@umfiasi.ro.
Cosmin Teodor MihaiCenter for Advanced Research and Development in Experimental Medicine (CEMEX), "Grigore T. Popa" University of Medicine and Pharmacy, 16 Universității Street, 700115 Iaşi, Romania. cosmin-teodor.mihai@umfiasi.ro.
Grigore T. Popa University of Medicine and Pharmacy · RO

Funding

"Grigore T. Popa" University of Medicine and Pharmacy, from Iaşi, Romania 27498/20.12.2018
6 · The paper itself

Abstract

Alzheimer's Disease affects approximately 33 million people worldwide and is characterized by progressive loss of memory at the cognitive level. The formation of toxic amyloid oligomers, extracellular amyloid plaques and amyloid angiopathy in brain by amyloid beta peptides are considered a part of the identified mechanism involved in disease pathogenesis. The optimal treatment approach leads toward finding a chemical compound able to form a noncovalent complex with the amyloid peptide thus blocking the process of amyloid aggregation. This direction gained an increasing interest lately, many studies demonstrating that mass spectrometry is a valuable method useful for the identification and characterization of such molecules able to interact with amyloid peptides. In the present review we aim to identify in the scientific literature low molecular weight chemical compounds for which there is mass spectrometric evidence of noncovalent complex formation with amyloid peptides and also there are toxicity reduction results which verify the effects of these compounds on amyloid beta toxicity towards cell cultures and transgenic mouse models developing Alzheimer's Disease.

Indexed as

Alzheimer DiseaseAmyloid beta-PeptidesAnimalsCell LineCell SurvivalDisaccharidesDisease Models, AnimalHumansMass SpectrometryMice, TransgenicMolecular WeightNeuroprotective AgentsPeptidesTaurineAmyloid beta-PeptidesDisaccharidesNeuroprotective AgentsPeptidesTaurineAlzheimer’s Diseaseamyloid-β peptidesanti-aggregating compoundscell viabilitycognitive dysfunctionin vitro modelsmass spectrometryproteolytic enzymesspatial working memorytransgenic mouse models

Identifiers

PMID30909659
PMCPMC6471768
OpenAlexW2924658488

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.