Evidence map›Paper›PMID 31995740›Full record

ArticleBiophysical journal2020

Study of the Expression Transition of Cardiac Myosin Using Polarization-Dependent SHG Microscopy.

Cai Yuan, Xiaolei Zhao, Zhonghai Wang, Thomas K Borg, Tong Ye, Zain I Khalpey, Raymond B Runyan, Yonghong Shao, Bruce Z Gao

Open access · bronzeAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Biophysical journal, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.7field-weighted citation impact, top 32% 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

3 citing papers in PubMed, 6 citations in OpenAlex.

  1. Review
  2. Article
  3. Recent advances in nonlinear microscopy: Deep insights and polarized revelations.The international journal of biochemistry & cell biology · 2021
    Review
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

9 authors at 4 institutions in 2 countries.

Cai YuanDepartments of Bioengineering, Clemson University, Clemson, South Carolina.
Xiaolei ZhaoElectrical and Computer Engineering, Clemson University, Clemson, South Carolina.
Zhonghai WangDepartments of Bioengineering, Clemson University, Clemson, South Carolina.
Thomas K BorgDepartment of Regenerative Medicine and Cell Biology, Medical University of South Carolina Charleston, South Carolina.
Tong YeDepartments of Bioengineering, Clemson University, Clemson, South Carolina.
Zain I KhalpeyDepartments of Surgery, University of Arizona, Tucson, Arizona.
Raymond B RunyanCellular and Molecular Medicine, University of Arizona, Tucson, Arizona.
Yonghong ShaoCollege of Optoelectronics Engineering, Shenzhen University, Shenzhen, China. Electronic address: shaoyh@szu.edu.cn.
Bruce Z GaoDepartments of Bioengineering, Clemson University, Clemson, South Carolina. Electronic address: zgao@clemson.edu.
Clemson University · USUniversity of Arizona · USMedical University of South Carolina · USShenzhen University · CN

Funding

NM-INBRE Sequencing and Bioinformatics CoreP20GM103451 · NIGMS · NEW MEXICO STATE UNIVERSITY LAS CRUCES · PI Charlotte C. Gard · 2012 to 2026
$61.2M
SOUTHWEST ENVIRONMENTAL HEALTH SCIENCES CENTERP30ES006694 · NIEHS · UNIVERSITY OF ARIZONA · PI DEAN BILLHEIMER · 1994 to 2026
$36.7M
UNDERSTANDING AND CONTROLLING TISSUE-SPECIFIC VASCULAR PATTERNINGP20RR021949 · NCRR · CLEMSON UNIVERSITY · PI MARKWALD, ROGER R · 2009 to 2011
$5.2M
Systems Mechanobiology Modeling for Patient-Specific Cardiac Fibrosis PredictionsR01HL144927 · NHLBI · UNIVERSITY OF ARKANSAS AT FAYETTEVILLE · PI RICHARDSON, WILLIAM JAMES · 2019 to 2023
$1.8M
Microfabricated coculture model: Myocyte rescue by TNT-transferred mitochondriaR01HL124782 · NHLBI · CLEMSON UNIVERSITY · PI GAO, BRUCE Z, RUNYAN, RAYMOND BRUCE · 2014 to 2017
$1.5M
NCRR NIH HHS P20 RR021949NHLBI NIH HHS R01 HL124782NHLBI NIH HHS R01 HL144927NIEHS NIH HHS P30 ES006694NIGMS NIH HHS P20 GM103451
6 · The paper itself

Abstract

Detection of the transition between the two myosin isoforms α- and β-myosin in living cardiomyocytes is essential for understanding cardiac physiology and pathology. In this study, the differences in symmetry of polarization spectra obtained from α- and β-myosin in various mammalian ventricles and propylthiouracil-treated rats are explored through polarization-dependent second harmonic generation microscopy. Here, we report for the, to our knowledge, first time that α- and β-myosin, as protein crystals, possess different symmetries: the former has C6 symmetry, and the latter has C3v. A single-sarcomere line scan further demonstrated that the differences in polarization-spectrum symmetry between α- and β-myosin came from their head regions: the head and neck domains of α- and β-myosin account for the differences in symmetry. In addition, the dynamic transition of the polarization spectrum from C6 to C3v line profile was observed in a cell culture in which norepinephrine induced an α- to β-myosin transition.

Indexed as

Cardiac MyosinsSarcomeresAnimalsMyocytes, CardiacMyosinsRatsVentricular MyosinsCardiac MyosinsMyosinsVentricular Myosins

Identifiers

PMID31995740
PMCPMC7063480
OpenAlexW2997541623

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.