Evidence map›Paper›PMID 29738067›Full record

ArticleChemistry (Weinheim an der Bergstrasse, Germany)2018

N-Terminal Charged Residues of Amyloid-β Peptide Modulate Amyloidogenesis and Interaction with Lipid Membrane.

Clifford Morris, Shirin Cupples, Thomas W Kent, Esmail A Elbassal, Ewa P Wojcikiewicz, Peng Yi, Deguo Du

Abstract read
In one paragraph

Article in Chemistry (Weinheim an der Bergstrasse, Germany), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing 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

14 citing papers in PubMed.

  1. Article
  2. Article
  3. The p3 peptides (AβNature communications · 2025
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Proteotoxicity and Neurodegenerative Diseases.International journal of molecular sciences · 2020
    Review
  11. Article
  12. Article
  13. Article
  14. 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

7 authors.

Clifford MorrisDepartment of Chemistry and Biochemistry, Florida Atlantic University, Boca Raton, FL, 33431, USA.
Shirin CupplesDepartment of Civil, Environmental and Geomatics Engineering, Florida Atlantic University, Boca Raton, FL, 33431, USA.
Thomas W KentDepartment of Chemistry and Biochemistry, Florida Atlantic University, Boca Raton, FL, 33431, USA.
Esmail A ElbassalDepartment of Chemistry and Biochemistry, Florida Atlantic University, Boca Raton, FL, 33431, USA.
Ewa P WojcikiewiczDepartment of Biomedical Science, Florida Atlantic University, Boca Raton, FL, 33431, USA.
Peng YiDepartment of Civil, Environmental and Geomatics Engineering, Florida Atlantic University, Boca Raton, FL, 33431, USA.
Deguo DuDepartment of Chemistry and Biochemistry, Florida Atlantic University, Boca Raton, FL, 33431, USA.ORCID http://orcid.org/0000-0002-8701-8208

Funding

Role of the N-terminal Region in Abeta Oligomer and Fibril FormationR15GM116006 · NIGMS · FLORIDA ATLANTIC UNIVERSITY · PI DU, DEGUO · 2015 to 2020
$735k
NIGMS NIH HHS R15 GM116006
6 · The paper itself

Abstract

Interactions of amyloid-β (Aβ) peptides and cellular membranes are proposed to be closely related with Aβ neurotoxicity in Alzheimer's disease. In this study, we systematically investigated the effect of the N-terminal hydrophilic region of Aβ40 on its amyloidogenesis and interaction with supported phospholipid bilayer. Our results show that modulation of the charge properties of the dynamic N-terminal region dramatically influences the aggregation properties of Aβ. Furthermore, our results demonstrate that the N-terminal charged residues play a crucial role in driving the early adsorption and latter remobilization of the peptide on membrane bilayer, and mediating the rigidity and viscoelasticity properties of the bound Aβ40 at the membrane interface. The results provide new mechanistic insight into the early Aβ-membrane interactions and binding, which may be critical for elucidating membrane-mediated Aβ amyloidogenesis in a physiological environment and unravelling the origin of Aβ neurotoxicity.

Indexed as

AdsorptionAmyloid beta-PeptidesAmyloid beta-Protein PrecursorCell MembraneHumansLipid BilayersAmyloid beta-PeptidesAmyloid beta-Protein PrecursorAPP protein, humanLipid Bilayersadsorption kineticsaggregationelectrostatic interactionslipidspeptides

Identifiers

PMID29738067
PMCPMC6035087

What OpenQuestion holds

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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.