Evidence map›Paper›PMID 26498981›Full record

ArticleScientific reports2015

Electron microscopic recording of myosin head power stroke in hydrated myosin filaments.

Haruo Sugi, Shigeru Chaen, Tsuyoshi Akimoto, Hiroki Minoda, Takuya Miyakawa, Yumiko Miyauchi, Masaru Tanokura, Seiryo Sugiura

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.9field-weighted citation impact, top 13% 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

9 citing papers in PubMed, 23 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

8 authors at 4 institutions in 1 country.

Haruo SugiDepartment of Physiology, School of Medicine, Teikyo University, Itabashi-ku, Tokyo 173-8605, Japan.
Shigeru ChaenDepartment of Integrated Sciences in Physics and Biology, College of Humanities and Sciences, Nihon University, Setagaya-ku, Tokyo 156-8550, Japan.
Tsuyoshi AkimotoDepartment of Physiology, School of Medicine, Teikyo University, Itabashi-ku, Tokyo 173-8605, Japan.
Hiroki MinodaDepartment of Applied Physics, Tokyo University of Agriculture and Technology, Koganei-shi, Tokyo 184-8588, Japan.
Takuya MiyakawaGraduate School of Agricultural and Life Sciences, University of Tokyo, Bunkyo-ku, Tokyo 113-0032, Japan.
Yumiko MiyauchiGraduate School of Agricultural and Life Sciences, University of Tokyo, Bunkyo-ku, Tokyo 113-0032, Japan.
Masaru TanokuraGraduate School of Agricultural and Life Sciences, University of Tokyo, Bunkyo-ku, Tokyo 113-0032, Japan.
Seiryo SugiuraGraduate School of Frontier Sciences, University of Tokyo, Kashiwa-shi, Chiba 277-8563, Japan.
The University of Tokyo · JPTeikyo University · JPNihon University · JPTokyo University of Agriculture and Technology · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Muscle contraction results from cyclic attachment and detachment between myosin heads and actin filaments, coupled with ATP hydrolysis. Despite extensive studies, however, the amplitude of myosin head power stroke still remains to be a mystery. Using the gas environmental chamber, we have succeeded in recording the power stroke of position-marked myosin heads in hydrated mixture of actin and myosin filaments in a nearly isometric condition, in which myosin heads do not produce gross myofilament sliding, but only stretch adjacent elastic structures. On application of ATP, individual myosin heads move by ~3.3 nm at the distal region, and by ~2.5 nm at the proximal region of myosin head catalytic domain. After exhaustion of applied ATP, individual myosin heads return towards their initial position. At low ionic strength, the amplitude of myosin head power stroke increases to >4 nm at both distal and proximal regions of myosin heads catalytic domain, being consistent with the report that the force generated by individual myosin heads in muscle fibers is enhanced at low ionic strength. The advantages of the present study over other in vitro motility assay systems, using myosin heads detached from myosin filaments, are discussed.

Indexed as

Actin CytoskeletonActinsAdenosine TriphosphateAnimalsCatalytic DomainMaleMicroscopy, ElectronMuscle ContractionMyosinsOsmolar ConcentrationRabbitsActinsAdenosine TriphosphateMyosins

Identifiers

PMID26498981
PMCPMC4620508
OpenAlexW2234968816

What OpenQuestion holds

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LicenceCC BY
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.