Evidence map›Paper›PMID 17526584›Full record

ArticleBiophysical journal2007

Nucleotide effects on the structure and dynamics of actin.

Xiange Zheng, Karthikeyan Diraviyam, David Sept

Abstract read
In one paragraph

Article in Biophysical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
–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

40 citing papers in PubMed.

  1. Article
  2. Journal of chemical theory and computation · 2023
    Article
  3. International journal of molecular sciences · 2021
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. 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
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. ATP and ADP actin states.Biopolymers · 2013
    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.

Xiange ZhengCenter for Computational Biology and Department of Biomedical Engineering, Washington University, St. Louis, Missouri 63130, USA.
Karthikeyan Diraviyam
David Sept

Funding

Protein interactions underlying actin-based motilityR01GM067246 · NIGMS · WASHINGTON UNIVERSITY · PI SEPT, DAVID S. · 2002 to 2006
$1.3M
NIGMS NIH HHS GM-067246NIGMS NIH HHS R01 GM067246
6 · The paper itself

Abstract

Adenosine 5'-triphosphate or ATP is the primary energy source within the cell, releasing its energy via hydrolysis into adenosine 5'-diphosphate or ADP. Actin is an important ATPase involved in many aspects of cellular function, and the binding and hydrolysis of ATP regulates its polymerization into actin filaments as well as its interaction with a host of actin-associated proteins. Here we study the dynamics of monomeric actin in ATP, ADP-Pi, and ADP states via molecular dynamics simulations. As observed in some crystal structures we see that the DNase-I loop is an alpha-helix in the ADP state but forms an unstructured coil domain in the ADP-Pi and ATP states. We also find that this secondary structure change is reversible, and by mimicking nucleotide exchange we can observe the transition between the helical and coil states. Apart from the DNase-I loop, we also see several key structural differences in the nucleotide binding cleft as well as in the hydrophobic cleft between subdomains 1 and 3 where WH2-containing proteins have been shown to interact. These differences provide a structural basis for understanding the observed differences between the various nucleotide states of actin and provide some insight into how ATP regulates the interaction of actin with itself and other proteins.

Indexed as

Actin CytoskeletonActinsAdenosine DiphosphateAdenosine TriphosphateAnimalsBinding SitesComputer SimulationDeoxyribonuclease IHumansHydrolysisHydrophobic and Hydrophilic InteractionsModels, MolecularPhosphatesProtein Structure, SecondaryActinsAdenosine DiphosphateAdenosine TriphosphateDeoxyribonuclease IPhosphates

Identifiers

PMID17526584
PMCPMC1929039

What OpenQuestion holds

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Registered trials

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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.