Evidence map›Paper›PMID 36659996›Full record

ArticleBiophysical reviews2022

Structural and functional analysis of actin point mutations leading to nemaline myopathy to elucidate their role in actin function.

Anna V Glyakina, Oxana V Galzitskaya

Open access · greenAbstract read
In one paragraph

Article in Biophysical reviews, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.3field-weighted citation impact, top 37% 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

2 citing papers in PubMed, 2 citations in OpenAlex.

  1. Review
  2. 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

2 authors at 2 institutions in 1 country.

Anna V GlyakinaInstitute of Protein Research, Russian Academy of Sciences, Pushchino, Russia.
Oxana V GalzitskayaInstitute of Protein Research, Russian Academy of Sciences, Pushchino, Russia.
Institute of Mathematical Problems of Biology · RUInstitute of Protein Research · RU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In this work, we analyzed 78 mutations in the actin protein that cause the disease nemaline myopathy. We analyzed how these mutations are distributed in important regions of the actin molecule (folding nucleus, core of the filament, amyloidogenic regions, disordered regions, regions involved in interaction with other proteins). It was found that 54 mutations (43 residues) fall into the folding nucleus (

Indexed as

Accessible surface areaActinAmyloidogenic regionsExonNemaline myopathy

Identifiers

PMID36659996
PMCPMC9842827
OpenAlexW4311348973

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.