ArticleJournal of muscle research and cell motility2013
Skeletal muscle myopathy mutations at the actin tropomyosin interface that cause gain- or loss-of-function.
Article in Journal of muscle research and cell motility, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 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
21 citing papers in PubMed, 29 citations in OpenAlex.
- The Structural Role of Tropomyosin in Regulating Thin Filament Activation of Actin-Myosin Interaction.Sub-cellular biochemistry · 2026Review
- Troponin and a Myopathy-Linked Mutation inInternational journal of molecular sciences · 2023Article
- Tropomyosin 3 (TPM3) function in skeletal muscle and in myopathy.Skeletal muscle · 2023Review
- Molecular and cellular basis of genetically inherited skeletal muscle disorders.Nature reviews. Molecular cell biology · 2021Review
- The R168G heterozygous mutation of tropomyosin 3 (TPM3) was identified in three family members and has manifestations ranging from asymptotic to serve scoliosis and respiratory complications.Genes & diseases · 2021Article
- The actin 'A-triad's' role in contractile regulation in health and disease.The Journal of physiology · 2020Review
- A new twist on tropomyosin binding to actin filaments: perspectives on thin filament function, assembly and biomechanics.Journal of muscle research and cell motility · 2020Review
- Small molecule studies: the fourth wave of muscle research.Journal of muscle research and cell motility · 2019Article
- Do Actomyosin Single-Molecule Mechanics Data Predict Mechanics of Contracting Muscle?International journal of molecular sciences · 2018Review
- Localization of the binding interface between leiomodin-2 and α-tropomyosin.Biochimica et biophysica acta · 2016Article
- Comprehensive analysis of tropomyosin isoforms in skeletal muscles by top-down proteomics.Journal of muscle research and cell motility · 2016Article
- TPM3 deletions cause a hypercontractile congenital muscle stiffness phenotype.Annals of neurology · 2015Article
- Muscle weakness in TPM3-myopathy is due to reduced Ca2+-sensitivity and impaired acto-myosin cross-bridge cycling in slow fibres.Human molecular genetics · 2015Article
- Poorly understood aspects of striated muscle contraction.BioMed research international · 2015Review
- Energy landscapes reveal the myopathic effects of tropomyosin mutations.Archives of biochemistry and biophysics · 2014Article
- Mutation update and genotype-phenotype correlations of novel and previously described mutations in TPM2 and TPM3 causing congenital myopathies.Human mutation · 2014Article
- Hypothesis and theory: mechanical instabilities and non-uniformities in hereditary sarcomere myopathies.Frontiers in physiology · 2014Article
- Nebulin interactions with actin and tropomyosin are altered by disease-causing mutations.Skeletal muscle · 2014Article
- Mutations in repeating structural motifs of tropomyosin cause gain of function in skeletal muscle myopathy patients.Human molecular genetics · 2013Article
- Introducing a special edition of the Journal of Muscle Research and Cell Motility on tropomyosin: form and function.Journal of muscle research and cell motility · 2013Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
It is well known that the regulation of muscle contraction relies on the ability of tropomyosin to switch between different positions on the actin filament, but it is still not well understood which amino acids are directly involved in the different states of the interaction. Recently the structure of the actin-tropomyosin interface has been determined both in the absence and presence of myosin heads. Interestingly, a number of mutations in tropomyosin that are associated with skeletal muscle myopathy are located within this interface. We first give an overview of the functional effect of mutations on amino acids that are involved in the contact with actin asp25, which represent a pattern repeated seven times along tropomyosin. It is explained how some of these amino acids (R167 and R244) which are thought to be involved in a salt bridge contact with actin in the closed state can produce a loss-of-function when mutated, while other positively charged tropomyosin amino acids positioned on the downstream side of the contact (K7, K49, R91, K168) can produce a gain-of-function when mutated. We then consider mutations of amino acids involved in another salt bridge contact between the two proteins in the closed state, actin K326N (which binds on five different points of tropomyosin) and tropomyosin ∆E139 and E181K, and we report how all of these mutations produce a gain-of-function. These observations can be important to validate the proposed structures and to understand more deeply how mutations affect the function of these proteins and to enable prediction of their outcomes.
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.