Evidence map›Paper›PMID 24854788›Full record

ReviewNature reviews. Molecular cell biology2014

The amyloid state and its association with protein misfolding diseases.

Tuomas P J Knowles, Michele Vendruscolo, Christopher M Dobson

Erratum issued Registry-linked trialAbstract readReview
PubMed Publisher
In one paragraph

Review in Nature reviews. Molecular cell biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. It is linked to trial NCT04760171 (An ex Vivo Study to Purify Amyloid Fibrils and Solve Their 3D Structures Using Amyloid Proteins From Medullary Thyroid Cancer and Laryngeal Amyloidosis), which is not on this map. Cited by 1,059 papers.

0numbers the graph read from it
0cells of the map it votes in
1,059citing 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.

NCT04760171 unknown statusnot on this mapstarted 2021, after this paper: background citation

An ex Vivo Study to Purify Amyloid Fibrils and Solve Their 3D Structures Using Amyloid Proteins From Medullary Thyroid Cancer and Laryngeal Amyloidosis

TypeobservationalSponsorThe Leeds Teaching Hospitals NHS TrustRan2021 to 2026Enrolled10ConditionsAmyloid, Medullary Thyroid Cancer, Alzheimer Disease, Dementia
3 · Its place in the literature

Who cites it

1,059 citing papers in PubMed.

  1. Review
  2. Review
  3. Article
  4. Review
  5. Article
  6. Cellular and systemic modifiers of alpha-synuclein proteostasis.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026
    Review
  7. Review
  8. Article
  9. Protein rheostasis: quality control in metastable proteomes.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026
    Review
  10. The microbiota-proteostasis axis: implications in neurodegenerative diseases.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Article

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

4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

3 authors.

Tuomas P J KnowlesDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK.
Michele VendruscoloDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK.
Christopher M DobsonDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK.

Funding

Biotechnology and Biological Sciences Research Council BB/H003843/1
6 · The paper itself

Abstract

The phenomenon of protein aggregation and amyloid formation has become the subject of rapidly increasing research activities across a wide range of scientific disciplines. Such activities have been stimulated by the association of amyloid deposition with a range of debilitating medical disorders, from Alzheimer's disease to type II diabetes, many of which are major threats to human health and welfare in the modern world. It has become clear, however, that the ability to form the amyloid state is more general than previously imagined, and that its study can provide unique insights into the nature of the functional forms of peptides and proteins, as well as understanding the means by which protein homeostasis can be maintained and protein metastasis avoided.

Indexed as

Protein FoldingAlzheimer DiseaseAmyloidAmyloidosisAnimalsHumansProtein ConformationAmyloid

Identifiers

PMID24854788

What OpenQuestion holds

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Registered trials

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.