Evidence map›Paper›PMID 10233145›Full record

ArticleMolecular biology of the cell1999

Different domains of the M-band protein myomesin are involved in myosin binding and M-band targeting.

D Auerbach, S Bantle, S Keller, V Hinderling, M Leu, E Ehler, J C Perriard

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
4.4field-weighted citation impact, top 5% 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

23 citing papers in PubMed, 88 citations in OpenAlex.

  1. Article
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  5. The M-band: The underestimated part of the sarcomere.Biochimica et biophysica acta. Molecular cell research · 2020
    Review
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  16. Nuclear localization of Myomesin-1: possible functions.Journal of muscle research and cell motility · 2008
    Article
  17. Article
  18. Article
  19. Article
  20. The sarcomeric M-band during development and in disease.Journal of muscle research and cell motility · 2005
    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

7 authors at 1 institution in 1 country.

D AuerbachInstitute of Cell Biology, Swiss Federal Institute of Technology, ETH Hönggerberg, CH-8093 Zürich.
S Bantle
S Keller
V Hinderling
M Leu
E Ehler
J C Perriard
Institute of Cell Biology · UA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Myomesin is a 185-kDa protein located in the M-band of striated muscle where it interacts with myosin and titin, possibly connecting thick filaments with the third filament system. By using expression of epitope-tagged myomesin fragments in cultured cardiomyocytes and biochemical binding assays, we could demonstrate that the M-band targeting activity and the myosin-binding site are located in different domains of the molecule. An N-terminal immunoglobulin-like domain is sufficient for targeting to the M-band, but solid-phase overlay assays between individual N-terminal domains and the thick filament protein myosin revealed that the unique head domain contains the myosin-binding site. When expressed in cardiomyocytes, the head domains of rat and chicken myomesin showed species-specific differences in their incorporation pattern. The head domain of rat myomesin localized to a central area within the A-band, whereas the head domain of chicken myomesin was diffusely distributed in the cytoplasm. We therefore conclude that the head domain of myomesin binds to myosin but that this affinity is not sufficient for the restriction of the domain to the M-band in vivo. Instead, the neighboring immunoglobulin-like domain is essential for the precise incorporation of myomesin into the M-band, possibly because of interaction with a yet unknown protein of the sarcomere.

Indexed as

AnimalsBinding SitesCells, CulturedChickensConnectinEpitopesMuscle ProteinsMutationMyocardiumMyosinsRatsRecombinant ProteinsSarcomeresSequence DeletionSpecies SpecificityConnectinEpitopesMuscle ProteinsMyosinsRecombinant Proteins

Identifiers

PMID10233145
PMCPMC25262
OpenAlexW2121049679

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.