Evidence map›Paper›PMID 1556170›Full record

ArticleJournal of muscle research and cell motility1992

Spatial relationship of nebulin relative to other myofibrillar proteins during myogenesis in embryonic chick skeletal muscle cells in vitro.

M Komiyama, Z H Zhou, K Maruyama, Y Shimada

Abstract read
PubMed Publisher
In one paragraph

Article in Journal of muscle research and cell motility, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

7 citing papers in PubMed, 37 citations in OpenAlex.

  1. Nebulin: big protein with big responsibilities.Journal of muscle research and cell motility · 2020
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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

4 authors at 1 institution in 2 countries.

M KomiyamaDepartment of Anatomy and Cell Biology, School of Medicine, Chiba University, Japan.
Z H Zhou
K Maruyama
Y Shimada
Chiba University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The developmental expression of nebulin was studied in embryonic chick skeletal muscle cells in vitro by means of immunofluorescence microscopy. Initially nebulin appeared homogeneously or in a punctate form in the cytoplasm, and then it was assembled into I-Z-I-like complexes containing actin and alpha-actinin but not myosin and connectin (titin). Striated patterns of nebulin ('singlets') in myofibrils appeared simultaneously with those of alpha-actinin (Z-bands), myosin (A-bands) and connectin ('doublets'), but earlier than those of actin. After actin striations were formed as myofibrils matured, each nebulin band started to exhibit 'droplets'. The delayed development of nebulin compared to the I-Z-I brush formation and the myofibril maturation seems to indicate that this giant myofibrillar protein is unnecessary for both the initial (formation of I-Z-I-like structures) and the subsequent (regular alignment of myofibrils) phases of myofibrillogenesis.

Indexed as

Protein KinasesAnimalsCells, CulturedChick EmbryoConnectinFluorescent Antibody TechniqueIn Vitro TechniquesMicrofilament ProteinsMuscle ProteinsMusclesMyosinsConnectinMicrofilament ProteinsMuscle ProteinsMyosinsnebulinProtein Kinases

Identifiers

PMID1556170
OpenAlexW2052680020

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.