Evidence map›Paper›PMID 24096987›Full record

ArticleScientific reports2013

Mechanism of amyloid β-protein dimerization determined using single-molecule AFM force spectroscopy.

Zhengjian Lv, Robin Roychaudhuri, Margaret M Condron, David B Teplow, Yuri L Lyubchenko

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
5.1field-weighted citation impact, top 4% 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

42 citing papers in PubMed, 75 citations in OpenAlex.

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  9. Probing Changes in CaMicromachines · 2020
    Article
  10. Article
  11. AFM Probing of Amyloid-Beta 42 Dimers and Trimers.Frontiers in molecular biosciences · 2020
    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

5 authors at 3 institutions in 1 country.

Zhengjian LvDepartment of Pharmaceutical Sciences, University of Nebraska Medical Center, 986025 Nebraska Medical Center, Omaha, NE 68198, United States.
Robin Roychaudhuri
Margaret M Condron
David B Teplow
Yuri L Lyubchenko
University of California, Los Angeles · USNebraska Medical Center · USUniversity of Nebraska Medical Center · US

Funding

STRUCTURAL/KINETIC ANALYSIS OF ABETA FIBRILLOGENESISR01NS038328 · NINDS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI TEPLOW, DAVID B. · 1999 to 2014
$4.0M
Protein Self-Assembly into NanoaggregatesR01GM096039 · NIGMS · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI LYUBCHENKO, YURI L · 2011 to 2018
$2.9M
Physical Biochemistry and Biology of Amyloid Beta-ProteinR01AG041295 · NIA · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI TEPLOW, DAVID B. · 2011 to 2015
$1.6M
NIA NIH HHS AG041295NIA NIH HHS R01 AG041295NIGMS NIH HHS 5R01 GM096039-02NIGMS NIH HHS R01 GM096039NINDS NIH HHS NS038328NINDS NIH HHS R01 NS038328
6 · The paper itself

Abstract

Aβ42 and Aβ40 are the two primary alloforms of human amyloid β-protein (Aβ). The two additional C-terminal residues of Aβ42 result in elevated neurotoxicity compared with Aβ40, but the molecular mechanism underlying this effect remains unclear. Here, we used single-molecule force microscopy to characterize interpeptide interactions for Aβ42 and Aβ40 and corresponding mutants. We discovered a dramatic difference in the interaction patterns of Aβ42 and Aβ40 monomers within dimers. Although the sequence difference between the two peptides is at the C-termini, the N-terminal segment plays a key role in the peptide interaction in the dimers. This is an unexpected finding as N-terminal was considered as disordered segment with no effect on the Aβ peptide aggregation. These novel properties of Aβ proteins suggests that the stabilization of N-terminal interactions is a switch in redirecting of amyloids form the neurotoxic aggregation pathway, opening a novel avenue for the disease preventions and treatments.

Indexed as

Protein MultimerizationAmyloid beta-PeptidesHumansMicroscopy, Atomic ForceProtein FoldingAmyloid beta-Peptides

Identifiers

PMID24096987
PMCPMC3791449
OpenAlexW2083254399

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.