Evidence map›Paper›PMID 23887197›Full record

ReviewBioarchitecture

Periodicities designed in the tropomyosin sequence and structure define its functions.

Bipasha Barua

Open access · bronzeAbstract readReview
In one paragraph

Review in Bioarchitecture. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
0.6field-weighted citation impact, top 25% 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

19 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
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  11. Mutations Q93H and E97K inInternational journal of molecular sciences · 2021
    Article
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  14. Review
  15. Article
  16. Article
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  19. Review
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

1 author at 1 institution in 1 country.

Bipasha BaruaDepartment of Pathology and Laboratory Medicine, Robert Wood Johnson Medical School, Piscataway, NJ, USA. baruabi@rwjms.rutgers.edu
Johnson University · US

Funding

Deciphering how tropomyosin regulates the actin filamentR01GM093065 · NIGMS · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI HITCHCOCK-DEGREGORI, SARAH ELLEN · 2010 to 2013
$1.2M
NIGMS NIH HHS GM093065NIGMS NIH HHS R01 GM093065
6 · The paper itself

Abstract

Tropomyosin is an actin binding protein that regulates actin filament dynamics and its interactions with actin binding proteins such as myosin, tropomodulin, formin, Arp2/3 and ADF-cofilin in most eukaryotic cells. Tropomyosin is the prototypical two-chained, α-helical coiled coil protein that associates end-to-end and binds to both sides of the actin filament. Each tropomyosin molecule spans four to seven actin monomers in the filament, depending on the size of the tropomyosin. Tropomyosins have a periodic heptad repeat sequence that is characteristic of coiled coil proteins as well as additional periodicities required for its interaction with the actin filament, where each periodic repeat interacts with one actin molecule. This review addresses the role of periodic features of the Tm molecule in carrying out its universal functions of binding to the actin filament and its regulation and the specific features that may determine the isoform specificity of tropomyosins.

Indexed as

ActinsAmino Acid SequenceAnimalsHumansProtein BindingProtein Structure, SecondaryTropomyosinActinsTropomyosinactin filamentcoiled coilcytoskeletonmuscle regulationtropomyosin

Identifiers

PMID23887197
PMCPMC3782539
OpenAlexW2171477546

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.