Evidence map›Paper›PMID 21320445›Full record

ArticleBiophysical journal2011

Tropomyosin position on F-actin revealed by EM reconstruction and computational chemistry.

Xiaochuan Edward Li, Larry S Tobacman, Ji Young Mun, Roger Craig, Stefan Fischer, William Lehman

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 110 papers.

0numbers the graph read from it
0cells of the map it votes in
110citing papers in PubMed
11.9field-weighted citation impact, top 1% 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

110 citing papers in PubMed, 165 citations in OpenAlex.

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  11. A Novel Variant inInternational journal of molecular sciences · 2023
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50 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 4 institutions in 2 countries.

Xiaochuan Edward LiDepartment of Physiology and Biophysics, Boston University School of Medicine, Boston, Massachusetts, USA.
Larry S Tobacman
Ji Young Mun
Roger Craig
Stefan Fischer
William Lehman
Boston University · USUniversity of Massachusetts Chan Medical School · USHeidelberg University · DEUniversity of Illinois Chicago · US

Funding

Structure-Function of the CytoskeletonP01HL086655 · NHLBI · BOSTON UNIVERSITY (CHARLES RIVER CAMPUS) · PI MORGAN, KATHLEEN G · 2007 to 2011
$8.8M
THIN FILAMENTS AND VERTEBRATE SMOOTH MUSCLE CONTRACTIONR01HL036153 · NHLBI · BOSTON UNIVERSITY MEDICAL CAMPUS · PI William J Lehman · 1986 to 2026
$6.5M
THIN FILAMENTS WITH CARDIOMYOPATHIC MUTANT PROTEINSR01HL063774 · NHLBI · UNIVERSITY OF IOWA · PI TOBACMAN, LARRY S · 2000 to 2014
$4.5M
Thin Filaments and Muscle RegulationR37HL036153 · NHLBI · BOSTON UNIVERSITY MEDICAL CAMPUS · PI LEHMAN, WILLIAM J · 2008 to 2017
$4.1M
CARDIAC CONTRACTILE PROTEIN COOPERATIVITYR01HL038834 · NHLBI · UNIVERSITY OF IOWA · PI TOBACMAN, LARRY S · 1992 to 2009
$3.6M
STRUCTURE OF CONTRACTILE FILAMENTS OF MUSCLER01AR034711 · NIAMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI CRAIG, ROGER W · 1986 to 2013
$3.6M
CARDIAC CONTRACTILE PROTEIN COOPERATIVITYR29HL038834 · NHLBI · UNIVERSITY OF IOWA · PI TOBACMAN, LARRY S · 1987 to 1991
–
THIN FILAMENTS AND VERTEBRATE SMOOTH MUSCLE CONTRACTIONR55HL036153 · NHLBI · BOSTON UNIVERSITY MEDICAL CAMPUS · PI LEHMAN, WILLIAM J · 1992 to 1992
–
NHLBI NIH HHS HL36153NHLBI NIH HHS HL38834NHLBI NIH HHS HL63774NHLBI NIH HHS HL86655NHLBI NIH HHS P01 HL086655NHLBI NIH HHS R01 HL036153NHLBI NIH HHS R01 HL038834NHLBI NIH HHS R01 HL063774NHLBI NIH HHS R37 HL036153NIAMS NIH HHS AR34711NIAMS NIH HHS R01 AR034711
6 · The paper itself

Abstract

Electron microscopy and fiber diffraction studies of reconstituted F-actin-tropomyosin filaments reveal the azimuthal position of end-to-end linked tropomyosin molecules on the surface of actin. However, the longitudinal z-position of tropomyosin along F-actin is still uncertain. Without this information, atomic models of F-actin-tropomyosin filaments, free of constraints imposed by troponin or other actin-binding proteins, cannot be formulated, and thus optimal interfacial contacts between actin and tropomyosin remain unknown. Here, a computational search assessing electrostatic interactions for multiple azimuthal locations, z-positions, and pseudo-rotations of tropomyosin on F-actin was performed. The information gleaned was used to localize tropomyosin on F-actin, yielding an atomic model characterized by protein-protein contacts that primarily involve clusters of basic amino acids on actin subdomains 1 and 3 juxtaposed against acidic residues on the successive quasi-repeating units of tropomyosin. A virtually identical model generated by docking F-actin and tropomyosin atomic structures into electron microscopy reconstructions of F-actin-tropomyosin validated the above solution. Here, the z-position of tropomyosin alongside F-actin was defined by matching the seven broad and narrow motifs that typify tropomyosin's twisting superhelical coiled-coil to the wide and tapering tropomyosin densities seen in surface views of F-actin-tropomyosin reconstructions. The functional implications of the F-actin-tropomyosin models determined in this work are discussed.

Indexed as

Computer SimulationActinsAmino AcidsAnimalsImage Processing, Computer-AssistedImaging, Three-DimensionalMicroscopy, ElectronModels, MolecularProtein BindingRabbitsReproducibility of ResultsStatic ElectricityTropomyosinActinsAmino AcidsTropomyosin

Identifiers

PMID21320445
PMCPMC3037716
OpenAlexW2092936803

What OpenQuestion holds

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Read underepoch 390

Registered trials

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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.