Evidence map›Paper›PMID 28792214›Full record

ArticleBiochemistry2017

Aggregation and Fibril Structure of Aβ

Robert Silvers, Michael T Colvin, Kendra K Frederick, Angela C Jacavone, Susan Lindquist, Sara Linse, Robert G Griffin

Abstract read
In one paragraph

Article in Biochemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing 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

21 citing papers in PubMed.

  1. Article
  2. Review
  3. Aducanumab binding to AβProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  4. Aducanumab Binding to AβbioRxiv : the preprint server for biology · 2025
    Article
  5. Diamond rotors for high magic angle spinning frequencies.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2025
    Article
  6. Article
  7. Structural characterization of E22G AβPhysical chemistry chemical physics : PCCP · 2024
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  13. Charge Regulation during Amyloid Formation of α-Synuclein.Journal of the American Chemical Society · 2021
    Article
  14. Article
  15. The role of fibril structure and surface hydrophobicity in secondary nucleation of amyloid fibrils.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  16. A new era for understanding amyloid structures and disease.Nature reviews. Molecular cell biology · 2018
    Review
  17. The structure of a βNature communications · 2018
    Article
  18. Article
  19. Raman fingerprints of amyloid structures.Chemical communications (Cambridge, England) · 2018
    Article
  20. 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.

Robert SilversDepartment of Chemistry and Francis Bitter Magnet Laboratory, Massachusetts Institute of Technology , Cambridge, Massachusetts 02139, United States.
Michael T ColvinDepartment of Chemistry and Francis Bitter Magnet Laboratory, Massachusetts Institute of Technology , Cambridge, Massachusetts 02139, United States.
Kendra K FrederickWhitehead Institute for Biomedical Research , Nine Cambridge Center, Cambridge, Massachusetts 02142, United States.
Angela C JacavoneDepartment of Chemistry and Francis Bitter Magnet Laboratory, Massachusetts Institute of Technology , Cambridge, Massachusetts 02139, United States.
Susan LindquistWhitehead Institute for Biomedical Research , Nine Cambridge Center, Cambridge, Massachusetts 02142, United States.
Sara LinseDepartment of Biochemistry and Structural Biology, Lund University , SE22100 Lund, Sweden.
Robert G GriffinDepartment of Chemistry and Francis Bitter Magnet Laboratory, Massachusetts Institute of Technology , Cambridge, Massachusetts 02139, United States.ORCID 0000-0003-1589-832X

Funding

OverallP41EB002026 · NIBIB · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI GRIFFIN, ROBERT GUY · 2003 to 2018
$17.9M
Solid State NMR Studies of Membrane ProteinsR01EB001960 · NIBIB · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI GRIFFIN, ROBERT GUY · 2003 to 2017
$6.5M
TR&D 4 -- Advanced Magic Angle Spinning NMR methodsP41GM132079 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI GRIFFIN, ROBERT GUY · 2019 to 2021
$3.6M
Solid State NMR Studies of Amyloid ProteinsRF1AG058504 · NIA · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI GRIFFIN, ROBERT GUY · 2017 to 2017
$3.1M
New RF Electronics Console and Probes for 900 Mhz NMR SpectrometerS10OD023513 · OD · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI GRIFFIN, ROBERT GUY · 2018 to 2018
$1.0M
Console for an 800/89 DNP SpectrometerS10OD012023 · OD · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI GRIFFIN, ROBERT GUY · 2013 to 2013
$539k
Investigating Abeta and alpha-synuclein toxicity by analyzing single-cell dynamicR21NS087557 · NINDS · WHITEHEAD INSTITUTE FOR BIOMEDICAL RES · PI WHITESELL, LUKE J · 2014 to 2015
$536k
NIA NIH HHS RF1 AG058504NIBIB NIH HHS P41 EB002026NIBIB NIH HHS R01 EB001960NIGMS NIH HHS P41 GM132079NIH HHS S10 OD012023NIH HHS S10 OD023513NINDS NIH HHS R21 NS087557
6 · The paper itself

Abstract

A mechanistic understanding of Aβ aggregation and high-resolution structures of Aβ fibrils and oligomers are vital to elucidating relevant details of neurodegeneration in Alzheimer's disease, which will facilitate the rational design of diagnostic and therapeutic protocols. The most detailed and reproducible insights into structure and kinetics have been achieved using Aβ peptides produced by recombinant expression, which results in an additional methionine at the N-terminus. While the length of the C-terminus is well established to have a profound impact on the peptide's aggregation propensity, structure, and neurotoxicity, the impact of the N-terminal methionine on the aggregation pathways and structure is unclear. For this reason, we have developed a protocol to produce recombinant Aβ

Indexed as

Amyloid beta-PeptidesKineticsModels, MolecularPeptide FragmentsProtein BindingProtein ConformationSpectrum AnalysisAmyloid beta-Peptidesamyloid beta-protein (1-42)Peptide Fragments

Identifiers

PMID28792214
PMCPMC8254419

What OpenQuestion holds

Textmetadata
LicenceTDM
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.