Evidence map›Paper›PMID 18854311›Full record

ArticleThe Journal of biological chemistry2008

Experimental investigation of the seesaw mechanism of the relay region that moves the myosin lever arm.

Bálint Kintses, Zhenhui Yang, András Málnási-Csizmadia

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing 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

11 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. An intermediate along the recovery stroke of myosin VI revealed by X-ray crystallography and molecular dynamics.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  6. Direct real-time detection of the structural and biochemical events in the myosin power stroke.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  7. Article
  8. Article
  9. Article
  10. Unsuspected pathway of the allosteric transition in hemoglobin.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  11. Emerging complex pathways of the actomyosin powerstroke.Trends in biochemical sciences · 2010
    Review
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.

Bálint KintsesDepartment of Biochemistry, Eötvös Loránd University, Budapest H-1117, Hungary.
Zhenhui Yang
András Málnási-Csizmadia

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A seesaw-like movement of the relay region upon the recovery step of myosin was recently simulated in silico. In this model the relay helix tilts around its pivoting point formed by a phenylalanine cluster (Phe(481), Phe(482), and Phe(652)), which moves the lever arm of myosin. To study the effect of the elimination of the proposed pivoting point, these phenylalanines were mutated to alanines in two Dictyostelium myosin II motor domain constructs (M(F481A, F482A) and M(F652A)). The relay movement was followed by the fluorescence change of Trp(501) located in the relay region. The steady-state and transient kinetic fluorescence experiments showed that the lack of the phenylalanine fulcrum perturbs the formation of the "up" lever arm state, and only moderate effects were found in the nucleotide binding, the formation of the "down" lever arm position, and the ATP hydrolysis steps. We conclude that the lack of the fulcrum decouples the distal part of the relay from the nucleotide binding site upon the recovery step. Our molecular dynamics simulations also showed that the conformation of the motor is not perturbed by the mutation in the down lever arm state, however, the lack of the pivoting point rearranges the dynamic pattern of the kink region of the relay helix.

Indexed as

ActinsAdenosine TriphosphateAnimalsBinding SitesDictyosteliumHydrolysisKineticsMutationMyosin Type IINucleotidesProtein BindingProtein ConformationSpectrometry, FluorescenceThermodynamicsTryptophanActinsAdenosine TriphosphateMyosin Type IINucleotidesTryptophan

Identifiers

PMID18854311
PMCPMC2662230

What OpenQuestion holds

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Read underepoch 390

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.