Evidence map›Paper›PMID 37153862›Full record

ArticleBiochemistry and biophysics reports2023

The intrinsically disordered protein glue of the myelin major dense line: Linking AlphaFold2 predictions to experimental data.

Oda C Krokengen, Arne Raasakka, Petri Kursula

Open access · goldAbstract read
In one paragraph

Article in Biochemistry and biophysics reports, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.9field-weighted citation impact, top 25% 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

3 citing papers in PubMed, 6 citations in OpenAlex.

  1. Review
  2. Article
  3. 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 at 2 institutions in 2 countries.

Oda C KrokengenDepartment of Biomedicine, University of Bergen, Norway.
Arne RaasakkaDepartment of Biomedicine, University of Bergen, Norway.
Petri KursulaDepartment of Biomedicine, University of Bergen, Norway.
University of Bergen · NOBiocenter Finland · FI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Numerous human proteins are classified as intrinsically disordered proteins (IDPs). Due to their physicochemical properties, high-resolution structural information about IDPs is generally lacking. On the other hand, IDPs are known to adopt local ordered structures upon interactions with

Indexed as

AlphaFold2Circular dichroism spectroscopyConformationIntrinsically disordered proteinMembrane bindingMyelinSmall-angle X-ray scattering

Identifiers

PMID37153862
PMCPMC10160357
OpenAlexW4367044740

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.