Evidence map›Paper›PMID 21726530›Full record

ArticleBiochemical and biophysical research communications2011

A partially folded structure of amyloid-beta(1-40) in an aqueous environment.

Subramanian Vivekanandan, Jeffrey R Brender, Shirley Y Lee, Ayyalusamy Ramamoorthy

Abstract read
In one paragraph

Article in Biochemical and biophysical research communications, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 162 papers.

0numbers the graph read from it
0cells of the map it votes in
162citing 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

162 citing papers in PubMed.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Chameleonic Nature of Aβ: Implications for Alzheimer's and Other Amyloid Diseases.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025
    Review
  11. Article
  12. Article
  13. Computational Study of AmyloidβInorganic chemistry · 2024
    Article
  14. APP-C31: An Intracellular Promoter of Both Metal-Free and Metal-Bound Amyloid-βAdvanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review

102 more citing papers are in PubMed but not listed here.

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

4 authors.

Subramanian VivekanandanDepartment of Biophysics, University of Michigan, Ann Arbor, MI 48109-1055, USA.
Jeffrey R Brender
Shirley Y Lee
Ayyalusamy Ramamoorthy

Funding

Membrane Interaction and Membrane Mediated Aggregation of AmylinR21DK078885 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI RAMAMOORTHY, AYYALUSAMY · 2009 to 2010
$411k
NIDDK NIH HHS DK078885NIDDK NIH HHS R21 DK078885
6 · The paper itself

Abstract

Aggregation of the Aβ(1-40) peptide is linked to the development of extracellular plaques characteristic of Alzheimer's disease. While previous studies commonly show the Aβ(1-40) is largely unstructured in solution, we show that Aβ(1-40) can adopt a compact, partially folded structure. In this structure (PDB ID: 2LFM), the central hydrophobic region of the peptide forms a 3(10) helix from H13 to D23 and the N- and C-termini collapse against the helix due to the clustering of hydrophobic residues. Helical intermediates have been predicted to be crucial on-pathway intermediates in amyloid fibrillogenesis, and the structure presented here presents a new target for investigation of early events in Aβ(1-40) fibrillogenesis.

Indexed as

Amino Acid SequenceAmyloid beta-PeptidesCold TemperatureHumansHydrogen-Ion ConcentrationHydrophobic and Hydrophilic InteractionsMolecular Sequence DataNuclear Magnetic Resonance, BiomolecularPeptide FragmentsProtein FoldingProtein Structure, SecondarySodium ChlorideWaterAmyloid beta-Peptidesamyloid beta-protein (1-40)Peptide FragmentsSodium ChlorideWater

Identifiers

PMID21726530
PMCPMC3148408

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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.