Evidence map›Paper›PMID 19158791›Full record

ArticleNature2009

The nature of the globular- to fibrous-actin transition.

Toshiro Oda, Mitsusada Iwasa, Tomoki Aihara, Yuichiro Maéda, Akihiro Narita

Erratum issuedAbstract read
PubMed Publisher
In one paragraph

Article in Nature, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 329 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
329citing papers in PubMed, 1 pooled it
–field-weighted citation impact
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

329 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
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  3. Review
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  6. Thermally Controlled Chiral Supramolecular Polymorphism in Water.Angewandte Chemie (International ed. in English) · 2026
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269 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors.

Toshiro OdaX-ray Structural Analysis Research Team, RIKEN SPring-8 Center, RIKEN Harima Institute, 1-1-1, Kouto, Sayo, Hyogo 679-5148, Japan. toda@spring8.or.jp
Mitsusada Iwasa
Tomoki Aihara
Yuichiro Maéda
Akihiro Narita

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Actin plays crucial parts in cell motility through a dynamic process driven by polymerization and depolymerization, that is, the globular (G) to fibrous (F) actin transition. Although our knowledge about the actin-based cellular functions and the molecules that regulate the G- to F-actin transition is growing, the structural aspects of the transition remain enigmatic. We created a model of F-actin using X-ray fibre diffraction intensities obtained from well oriented sols of rabbit skeletal muscle F-actin to 3.3 A in the radial direction and 5.6 A along the equator. Here we show that the G- to F-actin conformational transition is a simple relative rotation of the two major domains by about 20 degrees. As a result of the domain rotation, the actin molecule in the filament is flat. The flat form is essential for the formation of stable, helical F-actin. Our F-actin structure model provides the basis for understanding actin polymerization as well as its molecular interactions with actin-binding proteins.

Indexed as

ActinsAnimalsBiopolymersCell MovementGlutamineHydrolysisMagneticsModels, MolecularMuscle ContractionMuscle, SkeletalProtein Structure, QuaternaryProtein SubunitsRabbitsX-Ray DiffractionActinsBiopolymersGlutamineProtein Subunits

Identifiers

PMID19158791

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.