Evidence map›Paper›PMID 28584111›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2017

Phage display and kinetic selection of antibodies that specifically inhibit amyloid self-replication.

Anna Munke, Jonas Persson, Tanja Weiffert, Erwin De Genst, Georg Meisl, Paolo Arosio, Anna Carnerup, Christopher M Dobson, Michele Vendruscolo, Tuomas P J Knowles and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
5.3field-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

31 citing papers in PubMed, 67 citations in OpenAlex.

  1. Formation of a β-Endorphin Corona Mitigates Alzheimer's Amyloidogenesis.Small (Weinheim an der Bergstrasse, Germany) · 2025
    Article
  2. Article
  3. Article
  4. Review
  5. The role of shear forces in primary and secondary nucleation of amyloid fibrils.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  6. Article
  7. Article
  8. Self-replication of AProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  9. Article
  10. Article
  11. Amyloid inhibition by molecular chaperonesRSC medicinal chemistry · 2023
    Review
  12. Article
  13. Article
  14. Article
  15. Isolating Anti-amyloid Antibodies from Yeast-Displayed Libraries.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  16. Article
  17. Review
  18. Article
  19. Review
  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

11 authors at 2 institutions in 2 countries.

Anna MunkeDepartment of Biochemistry and Structural Biology, Chemical Centre, Lund University, SE221 00 Lund, Sweden.ORCID 0000-0002-5510-2245
Jonas PerssonDepartment of Biochemistry and Structural Biology, Chemical Centre, Lund University, SE221 00 Lund, Sweden.
Tanja WeiffertDepartment of Biochemistry and Structural Biology, Chemical Centre, Lund University, SE221 00 Lund, Sweden.
Erwin De GenstDepartment of Chemistry, University of Cambridge, Cambridge CB2 1EW, United Kingdom.
Georg MeislDepartment of Chemistry, University of Cambridge, Cambridge CB2 1EW, United Kingdom.ORCID 0000-0002-6562-7715
Paolo ArosioDepartment of Chemistry, University of Cambridge, Cambridge CB2 1EW, United Kingdom.
Anna CarnerupDepartment of Physical Chemistry, Chemical Centre, Lund University, SE221 00 Lund, Sweden.
Christopher M DobsonDepartment of Chemistry, University of Cambridge, Cambridge CB2 1EW, United Kingdom.
Michele VendruscoloDepartment of Chemistry, University of Cambridge, Cambridge CB2 1EW, United Kingdom.
Tuomas P J KnowlesDepartment of Chemistry, University of Cambridge, Cambridge CB2 1EW, United Kingdom.
Sara LinseDepartment of Biochemistry and Structural Biology, Chemical Centre, Lund University, SE221 00 Lund, Sweden; sara.linse@biochemistry.lu.se.ORCID 0000-0001-9629-7109
University of Cambridge · GBLund University · SE

Funding

Wellcome Trust
6 · The paper itself

Abstract

The aggregation of the amyloid β peptide (Aβ) into amyloid fibrils is a defining characteristic of Alzheimer's disease. Because of the complexity of this aggregation process, effective therapeutic inhibitors will need to target the specific microscopic steps that lead to the production of neurotoxic species. We introduce a strategy for generating fibril-specific antibodies that selectively suppress fibril-dependent secondary nucleation of the 42-residue form of Aβ (Aβ42). We target this step because it has been shown to produce the majority of neurotoxic species during aggregation of Aβ42. Starting from large phage display libraries of single-chain antibody fragments (scFvs), the three-stage approach that we describe includes (

Indexed as

Alzheimer DiseaseAmyloidAmyloid beta-PeptidesAmyloidogenic ProteinsAmyloidosisAntibodiesBacteriophagesHumansKineticsPeptide FragmentsPeptide LibraryAmyloidAmyloid beta-PeptidesAmyloidogenic ProteinsAntibodiesPeptide FragmentsPeptide LibraryAlzheimerantibodydrug developmentinhibitorself-assembly

Identifiers

PMID28584111
PMCPMC5488933
OpenAlexW2621543421

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.