Evidence map›Paper›PMID 20643929›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2010

Single-cell mechanics provides a sensitive and quantitative means for probing amyloid-beta peptide and neuronal cell interactions.

Valentin Lulevich, Christopher C Zimmer, Hyun-seok Hong, Lee-way Jin, Gang-yu Liu

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
3.6field-weighted citation impact, top 7% 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

33 citing papers in PubMed, 80 citations in OpenAlex.

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  9. Beta-amyloid pore linked to controlled calcium influx into the cell: A new paradigm for Alzheimer's Disease.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2022
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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 at 2 institutions in 1 country.

Valentin LulevichDepartment of Chemistry, University of California, Davis, CA 95616, USA.
Christopher C Zimmer
Hyun-seok Hong
Lee-way Jin
Gang-yu Liu
University of California, Davis · USNeuroDevelopment Center · US

Funding

UC Davis Alzheimer's Disease Core CenterP30AG010129 · NIA · UNIVERSITY OF CALIFORNIA DAVIS · PI DECARLI, CHARLES · 1991 to 2020
$28.3M
Inhibition of Alzheimer's Beta-Amyloid Fibril FormationR01AG025500 · NIA · KANSAS STATE UNIVERSITY · PI HUA, DUY H · 2006 to 2009
$1.1M
Using Nanotechnology to Regulate Integrin Clustering and Tensin LocalizationR21GM077850 · NIGMS · UNIVERSITY OF CALIFORNIA AT DAVIS · PI LIU, GANG-YU · 2006 to 2008
$556k
Identify Abeta Oligomer Inhibitors By Combinatorial ChemistryR21AG031362 · NIA · UNIVERSITY OF CALIFORNIA AT DAVIS · PI JIN, LEE-WAY · 2008 to 2009
$355k
NIA NIH HHS 1R01 AG025500NIA NIH HHS 1R21 AG031362NIA NIH HHS AG010129NIA NIH HHS P30 AG010129NIA NIH HHS R01 AG025500NIA NIH HHS R21 AG031362NIGMS NIH HHS 1R21 GM077850-01NIGMS NIH HHS R21 GM077850
6 · The paper itself

Abstract

By using a highly sensitive technique of atomic force microscopy-based single-cell compression, the rigidity of cultured N2a and HT22 neuronal cells was measured as a function of amyloid-beta42 (Abeta42) protein treatment. Abeta42 oligomers led to significant cellular stiffening; for example, 90-360% higher force was required to reach 80% deformation for N2a cells. Disaggregated or fibrillar forms of Abeta42 showed much less change. These observations were explained by a combination of two factors: (i) incorporation of oligomer into cellular membrane, which resulted in an increase in the Young's modulus of the membrane from 0.9+/-0.4 to 1.85+/-0.75 MPa for N2a cells and from 1.73+/-0.90 to 5.5+/-1.4 MPa for HT22 cells, and (ii) an increase in intracellular osmotic pressure (e.g., from 7 to 40 Pa for N2a cells) through unregulated ion influx. These findings and measurements provide a deeper, more characteristic, and quantitative insight into interactions between cells and Abeta42 oligomers, which have been considered the prime suspect for initiating neuronal dysfunction in Alzheimer's disease.

Indexed as

Cell CommunicationAmyloid beta-PeptidesAnimalsCell LineMiceNeuronsNonlinear DynamicsProtein MultimerizationAmyloid beta-Peptides

Identifiers

PMID20643929
PMCPMC2922280
OpenAlexW1969264462

What OpenQuestion holds

Textmetadata
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.