Evidence map›Paper›PMID 22737252›Full record

ArticlePloS one2012

Persistence length of human cardiac α-tropomyosin measured by single molecule direct probe microscopy.

Campion K P Loong, Huan-Xiang Zhou, P Bryant Chase

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

25 citing papers in PubMed, 32 citations in OpenAlex.

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  8. Revealing the mechanism of how cardiac myosin-binding protein C N-terminal fragments sensitize thin filaments for myosin binding.Proceedings of the National Academy of Sciences of the United States of America · 2019
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  19. Effects of non-linearity on cell-ECM interactions.Experimental cell research · 2013
    Review
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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

3 authors at 1 institution in 1 country.

Campion K P LoongDepartment of Biological Science, Florida State University, Tallahassee, Florida, United States of America. campion.loong@gmail.com
Huan-Xiang Zhou
P Bryant Chase
Florida State University · US

Funding

Modeling Crowding and Confinement of Cellular EnvironmentsR01GM088187 · NIGMS · FLORIDA STATE UNIVERSITY · PI ZHOU, HUAN-XIANG · 2010 to 2015
$1.6M
NIGMS NIH HHS GM88187NIGMS NIH HHS R01 GM088187
6 · The paper itself

Abstract

α-Tropomyosin (αTm) is the predominant tropomyosin isoform in adult human heart and constitutes a major component in Ca²+-regulated systolic contraction of cardiac muscle. We present here the first direct probe images of WT human cardiac αTm by atomic force microscopy, and quantify its mechanical flexibility with three independent analysis methods. Single molecules of bacterially-expressed human cardiac αTm were imaged on poly-lysine coated mica and their contours were analyzed. Analysis of tangent-angle (θ(s)) correlation along molecular contours, second moment of tangent angles (<θ²(s)>), and end-to-end length (L(e-e)) distributions respectively yielded values of persistence length (L(p)) of 41-46 nm, 40-45 nm, and 42-52 nm, corresponding to 1-1.3 molecular contour lengths (L(c)). We also demonstrate that a sufficiently large population, with at least 100 molecules, is required for a reliable L(p) measurement of αTm in single molecule studies. Our estimate that L(p) for αTm is only slightly longer than L(c) is consistent with a previous study showing there is little spread of cooperative activation into near-neighbor regulatory units of cardiac thin filaments. The L(p) determined here for human cardiac αTm perhaps represents an evolutionarily tuned optimum between Ca²+ sensitivity and cooperativity in cardiac thin filaments and likely constitutes an essential parameter for normal function in the human heart.

Indexed as

Aluminum SilicatesCalciumDNA, ComplementaryHeartHumansMicroscopy, Atomic ForceModels, CardiovascularModels, StatisticalModels, TheoreticalMyocardiumPolylysineSurface PropertiesSystoleTime FactorsTropomyosinAluminum SilicatesCalciumDNA, ComplementarymicaPolylysineTropomyosin

Identifiers

PMID22737252
PMCPMC3380901
OpenAlexW2062098294

What OpenQuestion holds

Textmetadata
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.