Evidence map›Paper›PMID 11867466›Full record

ArticleBiophysical journal2002

Ca(2+)-induced movement of tropomyosin in skeletal muscle thin filaments observed by multi-site FRET.

Corrado Bacchiocchi, Sherwin S Lehrer

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

22 citing papers in PubMed, 51 citations in OpenAlex.

  1. Article
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  7. Tropomyosin dynamics.Journal of muscle research and cell motility · 2014
    Review
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  15. Large-scale models reveal the two-component mechanics of striated muscle.International journal of molecular sciences · 2008
    Article
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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

2 authors at 1 institution in 1 country.

Corrado BacchiocchiMuscle and Motility Group, Boston Biomedical Research Institute, Watertown, Massachusetts 02472, USA. Bacchio@bbri.org
Sherwin S Lehrer
Boston Biomedical Research Institute · US

Funding

X-ray Crystallographic Investigation of Smooth Muscle RegulationP01AR041637 · NIAMS · BOSTON BIOMEDICAL RESEARCH INSTITUTE · PI TAO, TERENCE · 1992 to 2007
$15.1M
TROPOMYOSIN-MYOSIN INTERACTION IN MUSCLER01HL022461 · NHLBI · BOSTON BIOMEDICAL RESEARCH INSTITUTE · PI LEHRER, SHERWIN · 1986 to 2009
$4.5M
NHLBI NIH HHS HL22461NIAMS NIH HHS AR41637
6 · The paper itself

Abstract

To obtain information on Ca(2+)-induced tropomyosin (Tm) movement in Ca(2+)-regulated muscle thin filaments, frequency-domain fluorescence energy transfer data were collected between 5-(2-iodoacetyl-amino-ethyl-amino)naphthalene-1-sulfonic acid at Cys-190 of Tm and phalloidin-tetramethylrhodamine B isothiocyanate bound to F-actin. Two models were used to fit the experimental data: an atomic coordinate (AC) model coupled with a search algorithm that varies the position and orientation of Tm on F-actin, and a double Gaussian distance distribution (DD) model. The AC model showed that little or no change in transfer efficiency is to be expected between different sites on F-actin and Tm if Ca(2+) causes azimuthal movement of Tm of the magnitude suggested by structural data (C. Xu, R. Craig, L. Tobacman, R. Horowitz, and W. Lehman. 1999. Biophys. J. 77:985-992). However, Ca(2+) produced a small but significant change in our phase/modulation versus frequency data, showing that changes in lifetime decay can be detected even when a change of the steady-state transfer efficiency is very small. A change in Tm azimuthal position of 17 on the actin filament obtained with the AC model indicates that solution data are in reasonable agreement with EM image reconstruction data. In addition, the data indicate that Tm also appears to rotate about its axis, resulting in a rolling motion over the F-actin surface. The DD model showed that the distance from one of the two chains of Tm to F-actin was mainly affected, further verifying that Ca(2+) causes Tm to roll over the F-actin surface. The width of the distance distributions indicated that the position of Tm in absence and in presence of Ca(2+) is well defined with appreciable local flexibility.

Indexed as

Energy TransferAdenosine TriphosphatasesAnimalsCalciumModels, MolecularModels, StatisticalMuscle, SkeletalNormal DistributionRabbitsSpectrometry, FluorescenceTropomyosinAdenosine TriphosphatasesCalciumTropomyosin

Identifiers

PMID11867466
PMCPMC1301952
OpenAlexW1976268959

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.