Evidence map›Paper›PMID 21875595›Full record

ArticleJournal of molecular biology2011

Characterization of a myosin VII MyTH/FERM domain.

Rebecca J Moen, Daniel O Johnsrud, David D Thomas, Margaret A Titus

Abstract read
In one paragraph

Article in Journal of molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

9 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Optimized filopodia formation requires myosin tail domain cooperation.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  6. Myosin MyTH4-FERM structures highlight important principles of convergent evolution.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  7. Article
  8. Article
  9. 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

4 authors at 2 institutions in 2 countries.

Rebecca J Moen(1)Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, MN 55455, USA.
Daniel O Johnsrud
David D Thomas
Margaret A Titus
University of Minnesota · USInstitut thématique Génétique, génomique et bioinformatique · FR

Funding

Structural Dynamics of Muscle ContractionR01AR032961 · NIAMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI THOMAS, DAVID D · 1986 to 2018
$8.0M
MOLECULAR DYNAMICS OF MUSCLE CONTRACTIONR37AR032961 · NIAMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI THOMAS, DAVID DALE · 1994 to 2003
$2.1M
Study of Cell Adhesion Through an Analysis of Myosin 7R01GM046486 · NIGMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI TITUS, MARGARET A · 1991 to 2010
$1.8M
Structural and functional effects of site-directed oxidative modification of myosF31AG037303 · NIA · UNIVERSITY OF MINNESOTA · PI MOEN, REBECCA J · 2010 to 2013
$111k
NIAMS NIH HHS AR032961NIAMS NIH HHS R01 AR032961NIAMS NIH HHS R37 AR032961NIA NIH HHS F31 AG037303NIA NIH HHS F31AG037303NIGMS NIH HHS GM046486NIGMS NIH HHS R01 GM046486
6 · The paper itself

Abstract

A group of closely related myosins is characterized by the presence of at least one MyTH/FERM (myosin tail homology; band 4.1, ezrin, radixin, moesin) domain in their C-terminal tails. This domain interacts with a variety of binding partners, and mutations in either the MyTH4 or the FERM domain of myosin VII and myosin XV result in deafness, highlighting the functional importance of each domain. The N-terminal MyTH/FERM region of Dictyostelium myosin VII (M7) has been isolated as a first step toward gaining insight into the function of this domain and its interaction with binding partners. The M7 MyTH4/FERM domain (MF1) binds to both actin and microtubules in vitro, with dissociation constants of 13.7 and 1.7 μM, respectively. Gel filtration and UV spectroscopy reveal that MF1 exists as a monomer in solution and forms a well-folded, compact conformation with a high degree of secondary structure. These results indicate that MF1 forms an integrated structural domain that serves to couple actin filaments and microtubules in specific regions of the cytoskeleton.

Indexed as

ActinsChromatography, GelDictyosteliumKineticsMicrotubulesMyosinsProtein BindingProtein ConformationProtein Structure, TertiaryProtozoan ProteinsSpectrum AnalysisActinsMyosinsmyosin VII protein, Dictyostelium discoideumProtozoan Proteins

Identifiers

PMID21875595
PMCPMC3607624
OpenAlexW2136050206

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.