Evidence map›Paper›PMID 7568216›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1995

Specificity of dimer formation in tropomyosins: influence of alternatively spliced exons on homodimer and heterodimer assembly.

M Gimona, A Watakabe, D M Helfman

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
4.9field-weighted citation impact, top 4% 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

20 citing papers in PubMed, 74 citations in OpenAlex.

  1. Article
  2. Characterization of Alternative Splicing in High-Risk Wilms' Tumors.International journal of molecular sciences · 2024
    Article
  3. Article
  4. Polymorphism in tropomyosin structure and function.Journal of muscle research and cell motility · 2013
    Review
  5. Article
  6. Article
  7. New insights into the regulation of the actin cytoskeleton by tropomyosin.International review of cell and molecular biology · 2010
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Yotiao, a novel protein of neuromuscular junction and brain that interacts with specific splice variants of NMDA receptor subunit NR1.The Journal of neuroscience : the official journal of the Society for Neuroscience · 1998
    Review
  17. Article
  18. Article
  19. Article
  20. 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

3 authors at 1 institution in 1 country.

M GimonaCold Spring Harbor Laboratory, NY 11724, NY, USA.
A Watakabe
D M Helfman
Cold Spring Harbor Laboratory · US

Funding

TROPOMYOSIN IN NORMAL AND TRANSFORMED CELLSR01CA058607 · NCI · COLD SPRING HARBOR LABORATORY · PI HELFMAN, DAVID M · 1993 to 1997
–
NCI NIH HHS CA58607
6 · The paper itself

Abstract

Tropomyosins consist of nearly 100% alpha-helix and assemble into parallel and in-register coiled-coil dimers. In vitro it has been established that nonmuscle as well as native muscle tropomyosins can form homodimers. However, a mixture of muscle alpha and beta tropomyosin subunits results in the formation of the thermodynamically more stable alpha/beta heterodimer. Although the assembly preference of the muscle tropomyosin heterodimer can be understood thermodynamically, the presence of multiple tropomyosin isoforms expressed in nonmuscle cells points toward a more complex principle for determining dimer formation. We have investigated the dimerization of rat tropomyosins in living cells by the use of epitope tagging with a 16-aa sequence of the influenza hemagglutinin. Employing transfection and immunoprecipitation techniques, we have analyzed the dimers formed by muscle and nonmuscle tropomyosins in rat fibroblasts. We demonstrate that the information for homo- versus heterodimerization is contained within the tropomyosin molecule itself and that the information for the selectivity is conferred by the alternatively spliced exons. These results have important implications for models of the regulation of cytoskeletal dynamics.

Indexed as

Alternative SplicingAmino Acid SequenceAnimalsBase SequenceCytoskeletonEpitopesFibroblastsFluorescent Antibody TechniqueMolecular Sequence DataMuscle, SkeletalMuscle, SmoothProtein BindingProtein ConformationRatsRecombinant ProteinsStructure-Activity RelationshipEpitopesRecombinant ProteinsTropomyosin

Identifiers

PMID7568216
PMCPMC40885
OpenAlexW2131810538

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.