Evidence map›Paper›PMID 12732734›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2003

The structure of nonvertebrate actin: implications for the ATP hydrolytic mechanism.

S Vorobiev, B Strokopytov, D G Drubin, C Frieden, S Ono, J Condeelis, P A Rubenstein, S C Almo

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 85 papers.

0numbers the graph read from it
0cells of the map it votes in
85citing papers in PubMed
3.7field-weighted citation impact, top 7% 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

85 citing papers in PubMed, 165 citations in OpenAlex.

  1. Review
  2. A molecular perspective of gelsolin amyloidosis: An old foe with new faces.Cellular and molecular life sciences : CMLS · 2026
    Review
  3. Review
  4. Article
  5. Building the Bacterial Divisome at the Septum.Sub-cellular biochemistry · 2024
    Review
  6. Article
  7. Article
  8. Article
  9. Structures and mechanisms of actin ATP hydrolysis.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  10. Structure of Arp2/3 complex at a branched actin filament junction resolved by single-particle cryo-electron microscopy.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  11. Article
  12. Article
  13. Article
  14. Structural basis for polarized elongation of actin filaments.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Mechanism of actin polymerization revealed by cryo-EM structures of actin filaments with three different bound nucleotides.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  20. Mutations inF1000Research · 2019
    Article

25 more citing papers are in PubMed but not listed here.

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

8 authors at 1 institution in 1 country.

S VorobievDepartment of Biochemistry, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461, USA.
B Strokopytov
D G Drubin
C Frieden
S Ono
J Condeelis
P A Rubenstein
S C Almo
Albert Einstein College of Medicine · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The structures of Saccharomyces cerevisiae, Dictyostelium, and Caenorhabditis elegans actin bound to gelsolin segment-1 have been solved and refined at resolutions between 1.9 and 1.75 A. These structures reveal several features relevant to the ATP hydrolytic mechanism, including identification of the nucleophilic water and the roles of Gln-137 and His-161 in positioning and activating the catalytic water, respectively. The involvement of these residues in the catalytic mechanism is consistent with yeast genetics studies. This work highlights both structural and mechanistic similarities with the small and trimeric G proteins and restricts the types of mechanisms responsible for the considerable enhancement of ATP hydrolysis associated with actin polymerization. The conservation of functionalities involved in nucleotide binding and catalysis also provide insights into the mechanistic features of members of the family of actin-related proteins.

Indexed as

ActinsAdenosine TriphosphateAmino Acid SequenceAnimalsBinding SitesCaenorhabditis elegansDictyosteliumGelsolinHydrogen BondingHydrolysisInvertebratesModels, MolecularProtein ConformationProtein Structure, SecondaryProtein SubunitsSaccharomyces cerevisiaeActinsAdenosine TriphosphateGelsolinProtein Subunits

Identifiers

PMID12732734
PMCPMC156274
OpenAlexW2020956640

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.