ArticleBiophysical journal2008
Stability and kinetic properties of C5-domain from myosin binding protein C and its mutants.
Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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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.
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Who cites it
6 citing papers in PubMed, 10 citations in OpenAlex.
- The Role of Data in Model Building and Prediction: A Survey Through Examples.Entropy (Basel, Switzerland) · 2018Article
- Cross-species mechanical fingerprinting of cardiac myosin binding protein-C.Biophysical journal · 2013Article
- In the thick of it: HCM-causing mutations in myosin binding proteins of the thick filament.Circulation research · 2011Review
- Analysis of the free-energy surface of proteins from reversible folding simulations.PLoS computational biology · 2009Article
- Selection of optimal variants of Gō-like models of proteins through studies of stretching.Biophysical journal · 2008Article
- Analyzing pathogenic mutations of C5 domain from cardiac myosin binding protein C through MD simulations.European biophysics journal : EBJ · 2008Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The impact of three mutations of domain C5 from myosin binding protein C, correlated to Familial Hypertrophic Cardiomyopathy, has been assessed through molecular dynamics simulations based on a native centric protein modeling. The severity of the phenotype correlates with the shift in unfolding temperature determined by the mutations. A contact probability analysis reveals a folding process of the C5 domain originating in the region of DE and FG loops and propagating toward the area proximal to CD and EF loops. This suggests that mutation effects gain relevance in the proximity to the area where folding originates. The scenario is also confirmed by the analysis of the kinetics of 27 test mutations evenly distributed throughout the entire C5 domain.
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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.