Evidence map›Paper›PMID 1835089›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1991

Relationship between alternatively spliced exons and functional domains in tropomyosin.

Y J Cho, S E Hitchcock-DeGregori

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

24 citing papers in PubMed, 59 citations in OpenAlex.

  1. MBNL loss of function in smooth muscle as a model for myotonic dystrophy associated gastrointestinal dysmotility.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  2. Article
  3. Article
  4. Actin-tropomyosin distribution in non-muscle cells.Journal of muscle research and cell motility · 2020
    Review
  5. Article
  6. Article
  7. Mechanism of the calcium-regulation of muscle contraction--in pursuit of its structural basis.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2015
    Review
  8. Article
  9. Polymorphism in tropomyosin structure and function.Journal of muscle research and cell motility · 2013
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. The crystal structure of the C-terminal fragment of striated-muscle alpha-tropomyosin reveals a key troponin T recognition site.Proceedings of the National Academy of Sciences of the United States of America · 2002
    Article
  18. Article
  19. Article
  20. Specificity of dimer formation in tropomyosins: influence of alternatively spliced exons on homodimer and heterodimer assembly.Proceedings of the National Academy of Sciences of the United States of America · 1995
    Article
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

2 authors at 1 institution in 1 country.

Y J ChoJoint Graduate Program in Biochemistry and Molecular Biology, Rutgers University, Piscataway, NJ 08854.
S E Hitchcock-DeGregori
Johnson University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Smooth and striated muscle alpha-tropomyosins differ as a consequence of alternative splicing of exons 2 and 9 encoding amino acid residues 39-80 and 258-284, respectively [Ruiz-Opazo, N., Weinberger, J. & Nadal-Ginard, B. (1985) Nature (London) 315, 67-70]. To understand the relationship between alternatively spliced exons and functional domains in tropomyosin, recombinant unacetylated striated muscle, smooth muscle, and chimeric rat alpha-tropomyosins (+H3N-tropomyosins) expressed in and purified from Escherichia coli were analyzed. The functional differences between the isoforms can be primarily ascribed to exon 9. +H3N-Tropomyosins with the smooth muscle exon 9 bound to skeletal muscle filamentous actin with at least a 5-fold higher affinity than +H3N-tropomyosins with the striated muscle exon 9. On the other hand, in the presence of Ca2+, troponin increased the affinity of +H3N-tropomyosins with the striated muscle exon 9 at least 50-fold, whereas it had little effect on +H3N-tropomyosins with the smooth muscle exon 9. The unique striated muscle alpha-tropomyosin exon 9 seems to be specialized for Ca(2+)-insensitive interaction with troponin on the thin filament. The unique smooth muscle alpha-tropomyosin exon 2 was associated with a slightly lower actin affinity than the striated muscle exon 2. Although the regions encoded by exons 2 and 9 correspond to functional domains, they are not recognizable as independent units or structural domains in the extended coiled-coil structure of this fibrous actin binding protein.

Indexed as

ExonsRNA SplicingActinsAnimalsChimeraCloning, MolecularDNAFemaleKineticsMusclesMuscle, SmoothMyosinsProtein BindingRatsRecombinant ProteinsStomachActinsDNAMyosinsRecombinant ProteinsTropomyosin

Identifiers

PMID1835089
PMCPMC52886
OpenAlexW1977307506

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.