Evidence map›Paper›PMID 20414365›Full record

ReviewJournal of biomedicine & biotechnology2010

Molecular structure of sarcomere-to-membrane attachment at M-Lines in C. elegans muscle.

Hiroshi Qadota, Guy M Benian

Open access · hybridAbstract readReview
In one paragraph

Review in Journal of biomedicine & biotechnology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.3field-weighted citation impact, top 23% 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

25 citing papers in PubMed, 35 citations in OpenAlex.

  1. Role of Muscle LIM Protein in Mechanotransduction Process.International journal of molecular sciences · 2022
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  5. Molecular biology of the cell · 2017
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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

2 authors at 1 institution in 1 country.

Hiroshi QadotaDepartment of Pathology, Emory University, Atlanta, GA 30322, USA.
Guy M Benian
Emory University · US

Funding

Nematode UNC-98 functions in focal adhensions and nucleiR01AR052133 · NIAMS · EMORY UNIVERSITY · PI BENIAN, GUY MARTIN · 2005 to 2009
$1.2M
Using C. elegans to study titin and obscurin (UNC-89)R01AR051466 · NIAMS · EMORY UNIVERSITY · PI BENIAN, GUY MARTIN · 2004 to 2009
$1.2M
NIAMS NIH HHS AR051466NIAMS NIH HHS AR052133NIAMS NIH HHS R01 AR051466NIAMS NIH HHS R01 AR052133
6 · The paper itself

Abstract

C. elegans is an excellent model for studying nonmuscle cell focal adhesions and the analogous muscle cell attachment structures. In the major striated muscle of this nematode, all of the M-lines and the Z-disk analogs (dense bodies) are attached to the muscle cell membrane and underlying extracellular matrix. Accumulating at these sites are many proteins associated with integrin. We have found that nematode M-lines contain a set of protein complexes that link integrin-associated proteins to myosin thick filaments. We have also obtained evidence for intriguing additional functions for these muscle cell attachment proteins.

Indexed as

AnimalsCaenorhabditis elegansCaenorhabditis elegans ProteinsCarrier ProteinsFocal AdhesionsIntegrinsMuscle ProteinsMusclesSarcomeresCaenorhabditis elegans ProteinsCarrier ProteinsIntegrinsMuscle Proteins

Identifiers

PMID20414365
PMCPMC2857872
OpenAlexW1974684339

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.