Evidence map›Paper›PMID 23022558›Full record

ArticleFEBS letters2012

Equilibrium self-association of tropomyosin.

Walter F Stafford, Eunhee Lee, Philip Graceffa

Abstract read
In one paragraph

Article in FEBS letters, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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.

Walter F StaffordBoston Biomedical Research Institute, Watertown, MA 02472, United States.
Eunhee Lee
Philip Graceffa

Funding

Structure-Function of the CytoskeletonP01HL086655 · NHLBI · BOSTON UNIVERSITY (CHARLES RIVER CAMPUS) · PI DOMINGUEZ, ROBERTO · 2007 to 2011
$8.8M
NHLBI NIH HHS P01 HL086655NHLBI NIH HHS P01 HL86655
6 · The paper itself

Abstract

It has recently been reported that tropomyosin exists exclusively as a dimer in physiological salt conditions. It is shown in the present work using analytical ultracentrifugation that, on the contrary, tropomyosin is in equilibrium between monomer, dimer and tetramer with a weak tendency to dimerize and tetramerize. Such a finding has consequences for the assembly of the tropomyosin-actin complex.

Indexed as

AnimalsHydrogen-Ion ConcentrationKineticsPolymerizationProtein BindingRabbitsSolutionsTemperatureThermodynamicsTropomyosinUltracentrifugationSolutionsTropomyosin

Identifiers

PMID23022558
PMCPMC3500083

What OpenQuestion holds

Textmetadata
LicenceTDM
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.