Evidence map›Paper›PMID 17213877›Full record

ArticleThe EMBO journal2007

Reversible movement of switch 1 loop of myosin determines actin interaction.

Bálint Kintses, Máté Gyimesi, David S Pearson, Michael A Geeves, Wei Zeng, Clive R Bagshaw, András Málnási-Csizmadia

Open access · greenAbstract read
In one paragraph

Article in The EMBO journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

31 citing papers in PubMed, 51 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Molecular mechanisms underlying deoxy-ADP.Pi activation of pre-powerstroke myosin.Protein science : a publication of the Protein Society · 2017
    Article
  6. Article
  7. Biological Nanomotors with a Revolution, Linear, or Rotation Motion Mechanism.Microbiology and molecular biology reviews : MMBR · 2016
    Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Allosteric communication in Dictyostelium myosin II.Journal of muscle research and cell motility · 2012
    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

7 authors at 3 institutions in 2 countries.

Bálint KintsesDepartment of Biochemistry, Eötvös Lorand University, Budapest, Hungary.
Máté Gyimesi
David S Pearson
Michael A Geeves
Wei Zeng
Clive R Bagshaw
András Málnási-Csizmadia
Eötvös Loránd University · HUUniversity of Kent · GBUniversity of Leicester · GB

Funding

Wellcome Trust 071525
6 · The paper itself

Abstract

The conserved switch 1 loop of P-loop NTPases is implicated as a central element that transmits information between the nucleotide-binding pocket and the binding site of the partner proteins. Recent structural studies have identified two states of switch 1 in G-proteins and myosin, but their role in the transduction mechanism has yet to be clarified. Single tryptophan residues were introduced into the switch 1 region of myosin II motor domain and studied by rapid reaction methods. We found that in the presence of MgADP, two states of switch 1 exist in dynamic equilibrium. Actin binding shifts the equilibrium towards one of the MgADP states, whereas ATP strongly favors the other. In the light of electron cryo-microscopic and X-ray crystallographic results, these findings lead to a specific structural model in which the equilibrium constant between the two states of switch 1 is coupled to the strength of the actin-myosin interaction. This has implications for the enzymatic mechanism of G-proteins and possibly P-loop NTPases in general.

Indexed as

ActinsAdenosine DiphosphateAdenosine TriphosphateAnimalsCryoelectron MicroscopyCrystallography, X-RayDictyosteliumMagnesiumModels, ChemicalModels, MolecularMyosinsProtein BindingProtein ConformationProtein Structure, TertiaryTryptophanActinsAdenosine DiphosphateAdenosine TriphosphateMagnesiumMyosinsTryptophan

Identifiers

PMID17213877
PMCPMC1782383
OpenAlexW2105337558

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.