Evidence map›Paper›PMID 11333380›Full record

ArticleAmerican journal of human genetics2001

Nemaline myopathy caused by mutations in the muscle alpha-skeletal-actin gene.

B Ilkovski, S T Cooper, K Nowak, M M Ryan, N Yang, C Schnell, H J Durling, L G Roddick, I Wilkinson, A J Kornberg and 6 more

Open access · bronzeAbstract read
In one paragraph

Article in American journal of human genetics, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
6.7field-weighted citation impact, top 2% 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

38 citing papers in PubMed, 157 citations in OpenAlex.

  1. Alterations of actin in aging.Journal of cell science · 2026
    Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Case report: A novelFrontiers in neurology · 2024
    Article
  9. Article
  10. Article
  11. Variants inHGG advances · 2023
    Article
  12. Variants inmedRxiv : the preprint server for health sciences · 2023
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Actin Mutations and Their Role in Disease.International journal of molecular sciences · 2020
    Review
  18. KBTBD13 is an actin-binding protein that modulates muscle kinetics.The Journal of clinical investigation · 2020
    Article
  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

16 authors at 7 institutions in 1 country.

B IlkovskiInstitute for Neuromuscular Research, The Children's Hospital at Westmead, Westmead NSW 2145, Sydney, Australia.
S T Cooper
K Nowak
M M Ryan
N Yang
C Schnell
H J Durling
L G Roddick
I Wilkinson
A J Kornberg
K J Collins
G Wallace
P Gunning
E C Hardeman
N G Laing
K N North
The University of Sydney · AUJohn Hunter Children's Hospital · AURoyal Children's Hospital · AUThe University of Western Australia · AUChildren's Medical Research Institute · AUMater Children's Hospital · AUMurdoch University · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nemaline myopathy (NM) is a clinically and genetically heterogeneous disorder characterized by muscle weakness and the presence of nemaline bodies (rods) in skeletal muscle. Disease-causing mutations have been reported in five genes, each encoding a protein component of the sarcomeric thin filament. Recently, we identified mutations in the muscle alpha-skeletal-actin gene (ACTA1) in a subset of patients with NM. In the present study, we evaluated a new series of 35 patients with NM. We identified five novel missense mutations in ACTA1, which suggested that mutations in muscle alpha-skeletal actin account for the disease in approximately 15% of patients with NM. The mutations appeared de novo and represent new dominant mutations. One proband subsequently had two affected children, a result consistent with autosomal dominant transmission. The seven patients exhibited marked clinical variability, ranging from severe congenital-onset weakness, with death from respiratory failure during the 1st year of life, to a mild childhood-onset myopathy, with survival into adulthood. There was marked variation in both age at onset and clinical severity in the three affected members of one family. Common pathological features included abnormal fiber type differentiation, glycogen accumulation, myofibrillar disruption, and "whorling" of actin thin filaments. The percentage of fibers with rods did not correlate with clinical severity; however, the severe, lethal phenotype was associated with both severe, generalized disorganization of sarcomeric structure and abnormal localization of sarcomeric actin. The marked variability, in clinical phenotype, among patients with different mutations in ACTA1 suggests that both the site of the mutation and the nature of the amino acid change have differential effects on thin-filament formation and protein-protein interactions. The intrafamilial variability suggests that alpha-actin genotype is not the sole determinant of phenotype.

Indexed as

ActinsAdolescentAdultAmino Acid SequenceAustraliaChildChild, PreschoolCohort StudiesDNA Mutational AnalysisFemaleHumansImmunohistochemistryInfantInfant, NewbornMaleMicroscopy, ElectronActinsProtein IsoformsRNA, Messenger

Identifiers

PMID11333380
PMCPMC1226120
OpenAlexW2156585263

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.