Evidence map›Paper›PMID 25447537›Full record

ArticleFEBS letters2014

α-Synemin localizes to the M-band of the sarcomere through interaction with the M10 region of titin.

Bethany C Prudner, Pritam Sinha Roy, Derek S Damron, Mary A Russell

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in FEBS letters, 2014. 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
0.8field-weighted citation impact, top 32% 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, 14 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Synemin Redefined: Multiple Binding Partners Results in Multifunctionality.Frontiers in cell and developmental biology · 2020
    Review
  6. Article
  7. Review
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 1 country.

Bethany C PrudnerSchool of Biomedical Sciences, Kent State University, United States.
Pritam Sinha RoyDepartment of Biological Science, Kent State University, United States.
Derek S DamronSchool of Biomedical Sciences, Department of Biological Science, Kent State University, United States.
Mary A RussellSchool of Biomedical Sciences, Department of Biological Science, Kent State University at Trumbull, United States. Electronic address: mrussel1@kent.edu.
Kent State University · US

Funding

Propofol and Protein Kinase C: Molecular Interactions in CardiomyocytesR01HL065701 · NHLBI · KENT STATE UNIVERSITY · PI DAMRON, DEREK SCOTT · 2002 to 2011
$2.7M
NHLBI NIH HHS HL65701NHLBI NIH HHS R01 HL065701
6 · The paper itself

Abstract

α-Synemin contains a unique 312 amino acid insert near the end of its C-terminal tail. Therefore we set out to determine if the insert is a site of protein-protein interaction that regulates the sub-cellular localization of this large isoform of synemin. Yeast-two hybrid analysis indicated that this region is a binding site for the M10 region of titin. This was confirmed with GST pull-down assays. Co-immunoprecipitation of endogenous proteins indicated close association of the two proteins in vivo and immunostaining of cardiomyocytes demonstrated co-localization of the proteins at the M-band of the sarcomere.

Indexed as

AnimalsCell LineConnectinHumansIntermediate Filament ProteinsIntracellular SpaceMiceProtein BindingProtein TransportSarcomeresConnectindesmuslinIntermediate Filament ProteinsA-kinase anchoring proteinCytoskeletonIntermediate filamentProtein kinase ASignal transductionSynemin

Identifiers

PMID25447537
PMCPMC4268398
OpenAlexW2001403265

What OpenQuestion holds

Textmetadata
LicenceTDM
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.