Evidence map›Paper›PMID 15240477›Full record

ArticleBiophysical journal2004

Structural transients of contractile proteins upon sudden ATP liberation in skeletal muscle fibers.

Jun'ichi Wakayama, Takumi Tamura, Naoto Yagi, Hiroyuki Iwamoto

Abstract read
In one paragraph

Article in Biophysical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing 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

13 citing papers in PubMed.

  1. Review
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  4. Disrupted myosin cross-bridge cycling kinetics triggers muscle weakness in nebulin-related myopathy.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2011
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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

4 authors.

Jun'ichi WakayamaLife and Environment Division, SPring-8, Japan Synchrotron Radiation Research Institute, Hyogo 679-5198, Japan.
Takumi Tamura
Naoto Yagi
Hiroyuki Iwamoto

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Structural changes of contractile proteins were examined by millisecond time-resolved two-dimensional x-ray diffraction recordings during relaxation of skinned skeletal muscle fibers from rigor after caged ATP photolysis. It is known that the initial dissociation of the rigor actomyosin complex is followed by a period of transient active contraction, which is markedly prolonged in the presence of ADP by a mechanism yet to be clarified. Both single-headed (overstretched muscle fibers with exogenous myosin subfragment-1) and two-headed (fibers with full filament overlap) preparations were used. Analyses of various actin-based layer line reflections from both specimens showed the following: 1), The dissociation of the rigor actomyosin complex was fast and only modestly decelerated by ADP and occurred in a single exponential manner without passing through any detectable transitory state. Its ADP sensitivity was greater in the two-headed preparation but fell short of explaining the large ADP effect on the transient active contraction. 2), The decay of the activated state of the thin filament followed the time course of tension more closely in an ADP-dependent manner. These results suggest that the interplay between the reattached active myosin heads and the thin filament is responsible for the prolonged active contraction in the presence of ADP.

Indexed as

ActomyosinAdenosine DiphosphateAdenosine TriphosphateAnimalsMuscle ContractionMuscle Fibers, SkeletalMyosinsPhotolysisPsoas MusclesRabbitsX-Ray DiffractionActomyosinAdenosine DiphosphateAdenosine TriphosphateMyosins

Identifiers

PMID15240477
PMCPMC1304364

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.