Evidence map›Paper›PMID 19768801›Full record

ArticleProtein science : a publication of the Protein Society2009

NMR solution structures of actin depolymerizing factor homology domains.

Alexander K Goroncy, Seizo Koshiba, Naoya Tochio, Tadashi Tomizawa, Manami Sato, Makato Inoue, Satoru Watanabe, Yoshihide Hayashizaki, Akiko Tanaka, Takanori Kigawa and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

27 citing papers in PubMed, 49 citations in OpenAlex.

  1. Molecular characterization ofOpen veterinary journal · 2026
    Article
  2. Article
  3. Mechanisms of actin disassembly and turnover.The Journal of cell biology · 2023
    Review
  4. Review
  5. Review
  6. Article
  7. Article
  8. Drebrin-like (Dbnl) Controls Neuronal Migration via Regulating N-Cadherin Expression in the Developing Cerebral Cortex.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2019
    Article
  9. Article
  10. Article
  11. GMF as an Actin Network Remodeling Factor.Trends in cell biology · 2018
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Review
  19. Article
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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

11 authors at 2 institutions in 1 country.

Alexander K GoroncyRIKEN Systems and Structural Biology Center, 1-7-22 Suehiro-cho, Tsurumi-ku, Yokohama, Kanagawa, Japan.
Seizo Koshiba
Naoya Tochio
Tadashi Tomizawa
Manami Sato
Makato Inoue
Satoru Watanabe
Yoshihide Hayashizaki
Akiko Tanaka
Takanori Kigawa
Shigeyuki Yokoyama
Systems Biology Institute · JPRIKEN Center for Integrative Medical Sciences · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Actin is one of the most conserved proteins in nature. Its assembly and disassembly are regulated by many proteins, including the family of actin-depolymerizing factor homology (ADF-H) domains. ADF-H domains can be divided into five classes: ADF/cofilin, glia maturation factor (GMF), coactosin, twinfilin, and Abp1/drebrin. The best-characterized class is ADF/cofilin. The other four classes have drawn much less attention and very few structures have been reported. This study presents the solution NMR structure of the ADF-H domain of human HIP-55-drebrin-like protein, the first published structure of a drebrin-like domain (mammalian), and the first published structure of GMF beta (mouse). We also determined the structures of mouse GMF gamma, the mouse coactosin-like domain and the C-terminal ADF-H domain of mouse twinfilin 1. Although the overall fold of the five domains is similar, some significant differences provide valuable insights into filamentous actin (F-actin) and globular actin (G-actin) binding, including the identification of binding residues on the long central helix. This long helix is stabilized by three or four residues. Notably, the F-actin binding sites of mouse GMF beta and GMF gamma contain two additional beta-strands not seen in other ADF-H structures. The G-actin binding site of the ADF-H domain of human HIP-55-drebrin-like protein is absent and distorted in mouse GMF beta and GMF gamma.

Indexed as

Structural Homology, ProteinActin Depolymerizing FactorsAmino Acid SequenceAnimalsBinding SitesGlia Maturation FactorHumansMiceMicrofilament ProteinsMolecular Sequence DataNuclear Magnetic Resonance, BiomolecularPhylogenyProtein BindingProtein StabilityProtein Structure, TertiarySequence AlignmentActin Depolymerizing FactorsCotl1 protein, mouseGlia Maturation FactorMicrofilament ProteinsTwf1 protein, mouse

Identifiers

PMID19768801
PMCPMC2788292
OpenAlexW2112928445

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.