Evidence map›Paper›PMID 17513376›Full record

ArticleBiophysical journal2007

GFP-tagged regulatory light chain monitors single myosin lever-arm orientation in a muscle fiber.

Thomas P Burghardt, Katalin Ajtai, Daniel K Chan, Miriam F Halstead, Jinhui Li, Ye Zheng

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.6field-weighted citation impact, top 16% 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

18 citing papers in PubMed, 26 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. In vitro and in vivo single myosin step-sizes in striated muscle.Journal of muscle research and cell motility · 2015
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
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

6 authors at 1 institution in 1 country.

Thomas P BurghardtBiochemistry and Molecular Biology, Mayo Clinic College of Medicine, 200 First Street SW, Rochester, MN 55905, USA. burghardt@mayo.edu
Katalin Ajtai
Daniel K Chan
Miriam F Halstead
Jinhui Li
Ye Zheng
Mayo Clinic · US

Funding

Visualizing Actomyosin Transients by Data MergingR01AR049277 · NIAMS · MAYO CLINIC ROCHESTER · PI BURGHARDT, THOMAS P · 2004 to 2013
$3.2M
NIAMS NIH HHS R01 AR 049277NIAMS NIH HHS R01 AR049277
6 · The paper itself

Abstract

Myosin is the molecular motor in muscle-binding actin and executing a power stroke by rotating its lever arm through an angle of approximately 70 degrees to translate actin against resistive force. A green fluorescent protein (GFP)-tagged human cardiac myosin regulatory light chain (HCRLC) was constructed to study in situ lever arm orientation one molecule at a time by polarized fluorescence emitted from the GFP probe. The recombinant protein physically and functionally replaced the native RLC on myosin lever arms in the thick filaments of permeabilized skeletal muscle fibers. Detecting single molecules in fibers where myosin concentration reaches 300 microM is accomplished using total internal reflection fluorescence microscopy. With total internal reflection fluorescence, evanescent field excitation, supercritical angle fluorescence detection, and CCD detector pixel size limits detection volume to just a few attoliters. Data analysis manages both the perturbing effect of the TIR interface on probe emission and the effect of high numerical aperture collection of light. The natural myosin concentration gradient in a muscle fiber allows observation of fluorescence polarization from C-term GFP-tagged HCRLC exchanged myosin from regions in the thick filament containing low and high myosin concentrations. In rigor, cross-bridges at low concentration at the end of the thick filament maintain GFP dipole moments at two distinct polar angles relative to the fiber symmetry axis. The lower angle, where the dipole is nearly parallel to fiber axis, is more highly populated than the alternative, larger angle. Cross-bridges at higher concentration in the center of the thick filament are oriented in a homogeneous band at approximately 45 degrees to the fiber axis. The data suggests molecular crowding impacts myosin conformation, implying mutual interactions between cross-bridges alter how the muscle generates force. The GFP-tagged RLC is a novel probe to assess single-lever-arm orientation characteristics in situ.

Indexed as

Amino Acid SequenceAnimalsBiophysical PhenomenaBiophysicsFluorescence PolarizationFluorescent DyesGreen Fluorescent ProteinsHumansIn Vitro TechniquesMicroscopy, FluorescenceMolecular Motor ProteinsMolecular ProbesMuscle ContractionMuscle Fibers, SkeletalMuscle RelaxationMyocardiumFluorescent DyesGreen Fluorescent ProteinsMolecular Motor ProteinsMolecular ProbesMyosin Light ChainsRecombinant Fusion Proteins

Identifiers

PMID17513376
PMCPMC1959555
OpenAlexW1975284403

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.