Evidence map›Paper›PMID 19134468›Full record

ArticleBiophysical journal2009

Simultaneous measurement of nucleotide occupancy and mechanical displacement in myosin-V, a processive molecular motor.

Tomotaka Komori, So Nishikawa, Takayuki Ariga, Atsuko Hikikoshi Iwane, Toshio Yanagida

Abstract read
In one paragraph

Article in Biophysical journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing 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

7 citing papers in PubMed.

  1. Article
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  3. Review
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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

5 authors.

Tomotaka KomoriLaboratories for Nanobiology, Graduate School of Frontier Biosciences, Osaka University, Osaka, Japan.
So Nishikawa
Takayuki Ariga
Atsuko Hikikoshi Iwane
Toshio Yanagida

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Adenosine triphosphate (ATP) turnover drives various processive molecular motors and adenosine diphosphate (ADP) release is a principal transition in this cycle. Biochemical and single molecule mechanical studies have led to a model in which a slow ADP release step contributes to the processivity of myosin-V. To test the relationship between force generation and ADP release, we utilized optical trapping nanometry and single molecule total internal reflection fluorescence imaging for simultaneous and direct observation of both processes in myosin-V. We found that ADP was released 69 +/- 5.3 ms after force generation and displacement of actin, providing direct evidence for slow ADP release. As proposed by several previous studies, this slow ADP release probably ensures processivity by prolonging the strong actomyosin state in the ATP turnover cycle.

Indexed as

ActinsAdenosine DiphosphateAdenosine TriphosphateFluorescenceHumansIndolesMechanical PhenomenaMyosin Heavy ChainsMyosin Type VOptical TweezersTime Factors3'(2')-O-(N-(2-((2-((1-ethyl-3,3-dimethyl-5-sulfoindol-2-yl)prop-2-enylidene)-3,3-dimethyl-5-sulfoindol-1-yl)amino)ethyl)carbamoyl)-adenosine triphosphateActinsAdenosine DiphosphateAdenosine TriphosphateIndolesMYO5A protein, humanMyosin Heavy ChainsMyosin Type V

Identifiers

PMID19134468
PMCPMC2710051

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.