Evidence map›Paper›PMID 32632432›Full record

ReviewChemical Society reviews2020

Half a century of amyloids: past, present and future.

Pu Chun Ke, Ruhong Zhou, Louise C Serpell, Roland Riek, Tuomas P J Knowles, Hilal A Lashuel, Ehud Gazit, Ian W Hamley, Thomas P Davis, Marcus Fändrich and 5 more

Open access · hybridAbstract readReview
In one paragraph

Review in Chemical Society reviews, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 232 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
232citing papers in PubMed, 1 pooled it
40.5field-weighted citation impact, top 1% 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

232 citing papers in PubMed, 1 synthesis or guideline pooled it, 566 citations in OpenAlex.

  1. Guideline
  2. Differential proteostasis imbalance and the molecular basis of distinct synucleinopathies and tauopathies.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026
    Review
  3. De Novo Autogenic Engineered Living Functional Materials.Advanced materials (Deerfield Beach, Fla.) · 2026
    Article
  4. Review
  5. Article
  6. α-Synuclein Forms Distinct Micelle-Like Assemblies at Low Ionic Strengths.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  7. Article
  8. Article
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  11. Article
  12. Article
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  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
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  20. Review

172 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

15 authors at 13 institutions in 12 countries.

Pu Chun KeZhongshan Hospital, Fudan University, 111 Yixueyuan Rd, Xuhui District, Shanghai, China.
Ruhong Zhou
Louise C Serpell
Roland Riek
Tuomas P J Knowles
Hilal A Lashuel
Ehud Gazit
Ian W Hamley
Thomas P Davis
Marcus Fändrich
Daniel Erik Otzen
Matthew R Chapman
Christopher M Dobson
David S Eisenberg
Raffaele Mezzenga
ETH Zurich · CHUniversity of Cambridge · GBAarhus University · DKCharles Humbert 8 · CHEast Sussex County Council · GBHoward Hughes Medical Institute · USQuantitative BioSciences · USReading Museum · GBSun Yat-sen University · CNTel Aviv University · ILThe University of Queensland · AUUniversität Ulm · DEUniversity of Michigan · US

Funding

Towards Treatment of Alzheimer’s Disease by Targeting Pathogenic Tau and Beta-Amyloid StructuresR01AG070895 · NIA · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI DAVID EISENBERG · 2022 to 2026
$5.8M
Structure and Inhibition of Amyloid in Alzheimer's DiseaseRF1AG054022 · NIA · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI EISENBERG, DAVID · 2016 to 2018
$4.2M
Protein and Chemical Modulation of Curli Amyloid BiogenesisR01GM118651 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Matthew Richard Chapman · 2016 to 2026
$3.0M
Transthyretin as a generic inhibitor of amyloid and amyloid-associated biofilm infectionsR21AI137535 · NIAID · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI CHAPMAN, MATTHEW RICHARD · 2018 to 2019
$489k
NIAID NIH HHS R21 AI137535NIA NIH HHS R01 AG070895NIA NIH HHS RF1 AG054022NIGMS NIH HHS R01 GM118651
6 · The paper itself

Abstract

Amyloid diseases are global epidemics with profound health, social and economic implications and yet remain without a cure. This dire situation calls for research into the origin and pathological manifestations of amyloidosis to stimulate continued development of new therapeutics. In basic science and engineering, the cross-β architecture has been a constant thread underlying the structural characteristics of pathological and functional amyloids, and realizing that amyloid structures can be both pathological and functional in nature has fuelled innovations in artificial amyloids, whose use today ranges from water purification to 3D printing. At the conclusion of a half century since Eanes and Glenner's seminal study of amyloids in humans, this review commemorates the occasion by documenting the major milestones in amyloid research to date, from the perspectives of structural biology, biophysics, medicine, microbiology, engineering and nanotechnology. We also discuss new challenges and opportunities to drive this interdisciplinary field moving forward.

Indexed as

Alzheimer DiseaseAmyloidAmyloidosisCations, DivalentCross-Linking ReagentsHumansModels, MolecularMolecular ConformationPrinting, Three-DimensionalProtein FoldingProtein Processing, Post-TranslationalAmyloidCations, DivalentCross-Linking Reagents

Identifiers

PMID32632432
PMCPMC7445747
OpenAlexW3038168026

What Socratic 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 Socratic graph.