Evidence map›Paper›PMID 21825020›Full record

ReviewCold Spring Harbor perspectives in biology2011

Protein solubility and protein homeostasis: a generic view of protein misfolding disorders.

Michele Vendruscolo, Tuomas P J Knowles, Christopher M Dobson

Abstract readReview
In one paragraph

Review in Cold Spring Harbor perspectives in biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing 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

40 citing papers in PubMed.

  1. Review
  2. Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. Review
  11. Article
  12. Review
  13. Chemical Chaperones Modulate the Formation of Metabolite Assemblies.International journal of molecular sciences · 2021
    Article
  14. Article
  15. Article
  16. The Amyloid Phenomenon and Its Significance in Biology and Medicine.Cold Spring Harbor perspectives in biology · 2020
    Review
  17. Review
  18. Review
  19. 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

3 authors.

Michele VendruscoloDepartment of Chemistry, University of Cambridge, United Kingdom.
Tuomas P J Knowles
Christopher M Dobson

Funding

Biotechnology and Biological Sciences Research Council BB/H003843/1Medical Research Council MC_G1000734Wellcome Trust 089703
6 · The paper itself

Abstract

According to the "generic view" of protein aggregation, the ability to self-assemble into stable and highly organized structures such as amyloid fibrils is not an unusual feature exhibited by a small group of peptides and proteins with special sequence or structural properties, but rather a property shared by most proteins. At the same time, through a wide variety of techniques, many of which were originally devised for applications in other disciplines, it has also been established that the maintenance of proteins in a soluble state is a fundamental aspect of protein homeostasis. Taken together, these advances offer a unified framework for understanding the molecular basis of protein aggregation and for the rational development of therapeutic strategies based on the biological and chemical regulation of protein solubility.

Indexed as

Protein FoldingHomeostasisHumansKineticsProteostasis DeficienciesSolubilityThermodynamics

Identifiers

PMID21825020
PMCPMC3225949

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.