Evidence map›Paper›PMID 24769838›Full record

SynthesisPloS one2014

Insight of the cytotoxicity of the aggregates of peptides or aberrant proteins: a meta-analysis.

Rong Zhou, Bing Xu

Abstract readMeta-Analysis
In one paragraph

Synthesis in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing 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

8 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. 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

2 authors.

Rong ZhouDepartment of Chemistry, Brandeis University, Waltham, Massachusetts, United States of America.
Bing XuDepartment of Chemistry, Brandeis University, Waltham, Massachusetts, United States of America.

Funding

Subcellular Enzyme-instructed self-assembly for molecular anticancer nanomedicinesR01CA142746 · NCI · BRANDEIS UNIVERSITY · PI Bing Xu · 2010 to 2026
$6.4M
NCI NIH HHS R01 CA142746NCI NIH HHS R01CA142746
6 · The paper itself

Abstract

Aberrant proteins or peptide aggregates form soluble oligomers or nanofibrils that can cause a wide range of amyloidosis diseases, including Alzheimer's disease (AD). The mechanisms of their cytotoxicity, however, remain controversial and poorly understood, greatly hindering the development of AD drugs. Here we report a comprehensive evaluation of the cytotoxicity of the aggregates by meta-analysis. The analysis indicates that the cytotoxicity of the aggregates converges in a narrower range in the mass concentrations than in the molar concentrations, suggesting that it is the weight of the aggregates rather than the number of the molecules that dictates the cytotoxicity. This new perspective implies that these aggregates are likely to have non-specific interactions with cells to cause cell death. The comparison of several existing theories regarding cellular volumes supports that the aggregates may result in crowding effect and increase the free energy, thus resulting in instability of the cells.

Indexed as

Alzheimer DiseaseAmyloid beta-PeptidesAmyloidosisHumansPeptide FragmentsProtein AggregatesProtein Aggregation, PathologicalAmyloid beta-Peptidesamyloid beta-protein (1-40)amyloid beta-protein (1-42)Peptide FragmentsProtein Aggregates

Identifiers

PMID24769838
PMCPMC4000214

What OpenQuestion holds

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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.