Evidence map›Paper›PMID 19170537›Full record

ArticleBiochemistry2009

Structure of the N terminus of a nonmuscle alpha-tropomyosin in complex with the C terminus: implications for actin binding.

Norma J Greenfield, Lucy Kotlyanskaya, Sarah E Hitchcock-DeGregori

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing 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

21 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
  2. Current Approaches in Supersecondary Structures Investigation.International journal of molecular sciences · 2021
    Review
  3. Article
  4. Structural insights into the tropomodulin assembly at the pointed ends of actin filaments.Protein science : a publication of the Protein Society · 2021
    Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Atomic resolution probe for allostery in the regulatory thin filament.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  10. Article
  11. Article
  12. Structure and flexibility of the tropomyosin overlap junction.Biochemical and biophysical research communications · 2014
    Article
  13. Tropomodulins and tropomyosins: working as a team.Journal of muscle research and cell motility · 2013
    Review
  14. Tropomyosin Ser-283 pseudo-phosphorylation slows myofibril relaxation.Archives of biochemistry and biophysics · 2013
    Article
  15. Article
  16. Structure of a tropomyosin N-terminal fragment at 0.98 Å resolution.Acta crystallographica. Section D, Biological crystallography · 2011
    Article
  17. Article
  18. Article
  19. Article
  20. 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

3 authors at 1 institution in 1 country.

Norma J GreenfieldDepartment of Neuroscience and Cell Biology, Robert Wood Johnson Medical School, Piscataway, New Jersey 08854, USA.
Lucy Kotlyanskaya
Sarah E Hitchcock-DeGregori
Johnson University · US

Funding

REGULATION OF CONTRATION IN MUSCLE AND NON-MUSCLE CELLSR01GM036326 · NIGMS · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI HITCHCOCK-DEGREGORI, SARAH ELLEN · 1985 to 2006
$2.2M
NIGMS NIH HHS GM-36326NIGMS NIH HHS R01 GM036326
6 · The paper itself

Abstract

Tropomyosin is a coiled-coil actin binding protein that stabilizes the filament, protects it from severing, and cooperatively regulates actin's interaction with myosin. Depending on the first coding exon, tropomyosins are low molecular weight (LMW), found in the cytoskeleton and predominant in transformed cells, or high molecular weight (HMW), found in muscle and nonmuscle cells. The N- and C-terminal ends form a complex that allows tropomyosin to associate N terminus-to-C terminus along the actin filament. We determined the structure of a LMW tropomyosin N-terminal model peptide complexed with a smooth/nonmuscle tropomyosin C-terminal peptide. Using NMR and circular dichroism we showed that both ends become more helical upon complex formation but that the C-terminal peptide is partially unfolded at 20 degrees C. The first five residues of the N terminus that are disordered in the free peptide are more helical and are part of the overlap complex. NMR data indicate residues 2-17 bind to the C terminus in the complex. The data support a model for the LMW overlap complex that is homologous to the striated muscle tropomyosin complex in which the ends are oriented in parallel N terminus-to-C terminus with the plane of the N-terminal coiled coil perpendicular to the plane of the C terminus. The main difference is that the overlap spans 16 residues in the LMW tropomyosin complex compared to 11 residues in the HMW striated muscle overlap complex. We discuss the relevance of a stable but dynamic intermolecular junction for high-affinity binding to actin.

Indexed as

ActinsAmino Acid SequenceKineticsMagnetic Resonance SpectroscopyModels, MolecularMolecular Sequence DataMusclesPeptidesProtein BindingProtein StabilityProtein Structure, SecondaryProtein Structure, TertiaryStructure-Activity RelationshipTropomyosinActinsPeptidesTropomyosin

Identifiers

PMID19170537
PMCPMC4410877
OpenAlexW2089091329

What OpenQuestion holds

Textmetadata
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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.