Evidence map›Paper›PMID 30544720›Full record

ArticleInternational journal of molecular sciences2018

The Primary Causes of Muscle Dysfunction Associated with the Point Mutations in Tpm3.12; Conformational Analysis of Mutant Proteins as a Tool for Classification of Myopathies.

Yurii S Borovikov, Olga E Karpicheva, Armen O Simonyan, Stanislava V Avrova, Elena A Rogozovets, Vladimir V Sirenko, Charles S Redwood

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2018. 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
1.7field-weighted citation impact, top 14% 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, 17 citations in OpenAlex.

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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

7 authors at 3 institutions in 2 countries.

Yurii S BorovikovInstitute of Cytology of the Russian Academy of Sciences, Laboratory of Molecular Basis of Cell Motility, 4 Tikhoretsky Ave., 194064 Saint Petersburg, Russia, olexiya6@ya.ru (O.E.K.). borovikov@incras.ru.
Olga E KarpichevaInstitute of Cytology of the Russian Academy of Sciences, Laboratory of Molecular Basis of Cell Motility, 4 Tikhoretsky Ave., 194064 Saint Petersburg, Russia, olexiya6@ya.ru (O.E.K.). olexiya6@ya.ru.
Armen O SimonyanInstitute of Cytology of the Russian Academy of Sciences, Laboratory of Molecular Basis of Cell Motility, 4 Tikhoretsky Ave., 194064 Saint Petersburg, Russia, olexiya6@ya.ru (O.E.K.). simonyan_armen@mail.ru.ORCID 0000-0002-8045-7419
Stanislava V AvrovaInstitute of Cytology of the Russian Academy of Sciences, Laboratory of Molecular Basis of Cell Motility, 4 Tikhoretsky Ave., 194064 Saint Petersburg, Russia, olexiya6@ya.ru (O.E.K.). avrova@rambler.ru.
Elena A RogozovetsInstitute of Cytology of the Russian Academy of Sciences, Laboratory of Molecular Basis of Cell Motility, 4 Tikhoretsky Ave., 194064 Saint Petersburg, Russia, olexiya6@ya.ru (O.E.K.). elena.rogozovec@gmail.com.
Vladimir V SirenkoInstitute of Cytology of the Russian Academy of Sciences, Laboratory of Molecular Basis of Cell Motility, 4 Tikhoretsky Ave., 194064 Saint Petersburg, Russia, olexiya6@ya.ru (O.E.K.). sirw@mail.ru.ORCID 0000-0002-1383-0252
Charles S RedwoodRadcliffe Department of Medicine, University of Oxford, John Radcliffe Hospital, Oxford OX3 9DU, UK. credwood@well.ox.ac.uk.
Institute of Cytology · RUJohn Radcliffe Hospital · GBSt Petersburg University · RU

Funding

Russian Science Foundation 17-14-01224
6 · The paper itself

Abstract

Point mutations in genes encoding isoforms of skeletal muscle tropomyosin may cause nemaline myopathy, cap myopathy (Cap), congenital fiber-type disproportion (CFTD), and distal arthrogryposis. The molecular mechanisms of muscle dysfunction in these diseases remain unclear. We studied the effect of the E173A, R90P, E150A, and A155T myopathy-causing substitutions in γ-tropomyosin (Tpm3.12) on the position of tropomyosin in thin filaments, and the conformational state of actin monomers and myosin heads at different stages of the ATPase cycle using polarized fluorescence microscopy. The E173A, R90P, and E150A mutations produced abnormally large displacement of tropomyosin to the inner domains of actin and an increase in the number of myosin heads in strong-binding state at low and high Ca

Indexed as

Actin CytoskeletonActinsAnimalsCalciumFluorescence PolarizationHumansModels, BiologicalMuscle ContractionMuscle Fibers, SkeletalMuscle, SkeletalMuscular DiseasesMutant ProteinsMyosinsNucleotidesPoint MutationProtein BindingActinsCalciumMutant ProteinsMyosinsNucleotidesTPM3 protein, humanTropomyosinactin–myosin interactionATPase activity of myosinCa2+-sensitivitycongenital myopathymuscle fibermutation in tropomyosinregulation of muscle contraction

Identifiers

PMID30544720
PMCPMC6321504
OpenAlexW2903715762

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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.