Evidence map›Paper›PMID 18555187›Full record

ReviewTrends in cardiovascular medicine2008

Bioinformatics assessment of beta-myosin mutations reveals myosin's high sensitivity to mutations.

Massimo Buvoli, Micah Hamady, Leslie A Leinwand, Rob Knight

Erratum issuedOpen access · greenAbstract readReview
In one paragraph

Review in Trends in cardiovascular medicine, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

34 citing papers in PubMed, 47 citations in OpenAlex.

  1. Review
  2. MYH7 in cardiomyopathy and skeletal muscle myopathy.Molecular and cellular biochemistry · 2024
    Review
  3. Article
  4. Review
  5. Hypertrophic cardiomyopathy β-cardiac myosin mutation (P710R) leads to hypercontractility by disrupting super relaxed state.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. Review
  14. Article
  15. Multidimensional structure-function relationships in human β-cardiac myosin from population-scale genetic variation.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  16. Article
  17. Review
  18. Article
  19. Review
  20. Article
4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Massimo BuvoliDepartment of Molecular, Cellular, and Developmental Biology, University of Colorado, Boulder, CO 80309, USA.
Micah Hamady
Leslie A Leinwand
Rob Knight
University of Colorado Boulder · US

Funding

Trace the flow of genes in the gut microbiome of obese and lean twin pairsP01DK078669 · NIDDK · WASHINGTON UNIVERSITY · PI GORDON, JEFFREY I · 2007 to 2018
$16.0M
MYOSIN GENE DIVERSITY AND FUNCTIONR01GM029090 · NIGMS · YESHIVA UNIVERSITY · PI Leslie Anne Leinwand · 1985 to 2026
$12.3M
Predoctoral Training Molecular BiophysicsT32GM065103 · NIGMS · UNIVERSITY OF COLORADO AT BOULDER · PI FALKE, JOSEPH J · 2002 to 2021
$4.3M
Mechanisms of myopathy caused by mutations in the myosin rodR01HL085573 · NHLBI · UNIVERSITY OF COLORADO · PI LEINWAND, LESLIE ANNE · 2007 to 2010
$1.5M
NHLBI NIH HHS 5R01 HL085573-01NHLBI NIH HHS R01 HL085573NIDDK NIH HHS P01 DK078669NIGMS NIH HHS GM29090NIGMS NIH HHS R01 GM029090NIGMS NIH HHS T32 GM065103NIGMS NIH HHS T32GM065103
6 · The paper itself

Abstract

More than 200 mutations in the beta-myosin gene (MYH7) that cause clinically distinct cardiac and/or skeletal myopathies have been reported, but to date, no comprehensive statistical analysis of these mutations has been performed. As a part of this review, we developed a new interactive database and research tool called MyoMAPR (Myopathic Mutation Analysis Profiler and Repository). We report that the distribution of mutations along the beta-myosin gene is not homogeneous, and that myosin is a highly constrained molecule with an uncommon sensitivity to amino acid substitutions. Increasing knowledge of the characteristics of MH7 mutations may provide a valuable resource for scientists and clinicians studying diagnosis, risk stratification, and treatment of disease associated with these mutations.

Indexed as

Computational BiologyGenomicsMutationCardiac MyosinsCardiomyopathiesDatabases, GeneticDNA Mutational AnalysisGenetic Predisposition to DiseaseHumansMuscular DiseasesMyosin Heavy ChainsProtein ConformationProtein Structure, TertiaryCardiac MyosinsMYH7 protein, humanMyosin Heavy Chains

Identifiers

PMID18555187
PMCPMC2587080
OpenAlexW2073360367

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.