Evidence map›Paper›PMID 37529678›Full record

ArticleQRB discovery2021

Response to crowded conditions reveals compact nucleus for amyloid formation of folded protein.

Tony E R Werner, Istvan Horvath, Pernilla Wittung-Stafshede

Abstract read
In one paragraph

Article in QRB discovery, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed, 1 pooled it
–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

4 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Article
  3. Review
  4. 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.

Tony E R WernerDepartment of Biology and Biological Engineering, Chalmers University of Technology, S-41296 Gothenburg, Sweden.ORCID https://orcid.org/0000-0002-2539-0442
Istvan HorvathDepartment of Biology and Biological Engineering, Chalmers University of Technology, S-41296 Gothenburg, Sweden.ORCID https://orcid.org/0000-0003-4262-1430
Pernilla Wittung-StafshedeDepartment of Biology and Biological Engineering, Chalmers University of Technology, S-41296 Gothenburg, Sweden.ORCID https://orcid.org/0000-0003-1058-1964

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Although the consequences of the crowded cell environments may affect protein folding, function and misfolding reactions, these processes are often studied in dilute solutions

Indexed as

Amyloid formationmacromolecular crowdingosmolyteprotein aggregationβ-parvalbumin

Identifiers

PMID37529678
PMCPMC10392690

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.