ReviewJournal of muscle research and cell motility2004
An open or closed case for the conformation of calponin homology domains on F-actin?
Review in Journal of muscle research and cell motility, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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.
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.
Who cites it
10 citing papers in PubMed, 20 citations in OpenAlex.
- F-actin clustering and cell dysmotility induced by the pathological W148R missense mutation of filamin B at the actin-binding domain.American journal of physiology. Cell physiology · 2016Article
- The N-terminal actin-binding tandem calponin-homology (CH) domain of dystrophin is in a closed conformation in solution and when bound to F-actin.Biophysical journal · 2012Article
- Thermodynamic stability, unfolding kinetics, and aggregation of the N-terminal actin-binding domains of utrophin and dystrophin.Proteins · 2012Article
- Utrophin ABD binds to F-actin in an open conformation.FEBS open bio · 2012Article
- Large-scale opening of utrophin's tandem calponin homology (CH) domains upon actin binding by an induced-fit mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Opening of tandem calponin homology domains regulates their affinity for F-actin.Nature structural & molecular biology · 2010Article
- Regulation of actin cytoskeleton dynamics in cells.Molecules and cells · 2010Review
- Problems in fitting high resolution structures into electron microscopic reconstructions.HFSP journal · 2008Article
- High-resolution cryo-EM structure of the F-actin-fimbrin/plastin ABD2 complex.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Insights into the molecular evolution of the PDZ/LIM family and identification of a novel conserved protein motif.PloS one · 2007Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 4 institutions in 3 countries.
Funding
Abstract
Calponin homology domains link many different proteins to the surface of actin filaments. However, details of the structural interactions involved and the methods used to determine them are controversial. In the case of the actin-binding protein utrophin, for example, several models have been proposed for the binding of utrophin's calponin homology domains to actin. We review and evaluate these models and their supporting data.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.