Evidence map›Paper›PMID 30254171›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2018

Structural evidence for the roles of divalent cations in actin polymerization and activation of ATP hydrolysis.

Clement P M Scipion, Umesh Ghoshdastider, Fernando J Ferrer, Tsz-Ying Yuen, Jantana Wongsantichon, Robert C Robinson

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.6field-weighted citation impact, top 16% 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

17 citing papers in PubMed, 32 citations in OpenAlex.

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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

6 authors at 1 institution in 2 countries.

Clement P M ScipionInstitute of Molecular and Cell Biology, Agency for Science, Technology, and Research (A*STAR), Biopolis, 138673 Singapore.ORCID 0000-0002-3753-8475
Umesh GhoshdastiderInstitute of Molecular and Cell Biology, Agency for Science, Technology, and Research (A*STAR), Biopolis, 138673 Singapore.
Fernando J Ferrerp53 Laboratory, A*STAR, Biopolis, 138648 Singapore.
Tsz-Ying YuenInstitute of Chemical and Engineering Sciences, A*STAR, Biopolis, 138665 Singapore.
Jantana WongsantichonInstitute of Molecular and Cell Biology, Agency for Science, Technology, and Research (A*STAR), Biopolis, 138673 Singapore.
Robert C RobinsonInstitute of Molecular and Cell Biology, Agency for Science, Technology, and Research (A*STAR), Biopolis, 138673 Singapore; rrobinson@imcb.a-star.edu.sg.
Agency for Science, Technology and Research · SG

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The structure of the actin filament is known at a resolution that has allowed the architecture of protein components to be unambiguously assigned. However, fully understanding the chemistry of the system requires higher resolution to identify the ions and water molecules involved in polymerization and ATP hydrolysis. Here, we find experimental evidence for the association of cations with the surfaces of G-actin in a 2.0-Å resolution X-ray structure of actin bound to a Cordon-Bleu WH2 motif and in previously determined high-resolution X-ray structures. Three of four reoccurring divalent cation sites were stable during molecular dynamics (MD) simulations of the filament, suggesting that these sites may play a functional role in stabilizing the filament. We modeled the water coordination at the ATP-bound Mg

Indexed as

ActinsAdenosine TriphosphateAnimalsCations, DivalentCrystallography, X-RayCytoskeletal ProteinsHydrolysisMagnesiumMicrofilament ProteinsModels, MolecularMolecular Dynamics SimulationProteinsRabbitsWaterActinsAdenosine TriphosphateCations, DivalentCobl protein, mouseCytoskeletal ProteinsMagnesiumMicrofilament ProteinsProteinsWateractinATP hydrolysismolecular dynamicsX-ray crystallography

Identifiers

PMID30254171
PMCPMC6187199
OpenAlexW2893106047

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.