ArticleBiophysical journal2007
GFP-tagged regulatory light chain monitors single myosin lever-arm orientation in a muscle fiber.
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.
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.
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.
Who cites it
18 citing papers in PubMed, 26 citations in OpenAlex.
- Illuminating cellular architecture and dynamics with fluorescence polarization microscopy.Journal of cell science · 2024Review
- Stokes polarimetry-based second harmonic generation microscopy for collagen and skeletal muscle fiber characterization.Lasers in medical science · 2021Article
- Nonlinear Actomyosin Elasticity in Muscle?Biophysical journal · 2019Article
- Auxotonic to isometric contraction transitioning in a beating heart causes myosin step-size to down shift.PloS one · 2017Article
- In vivo myosin step-size from zebrafish skeletal muscle.Open biology · 2016Article
- In vitro and in vivo single myosin step-sizes in striated muscle.Journal of muscle research and cell motility · 2015Article
- 3D fluorescence anisotropy imaging using selective plane illumination microscopy.Optics express · 2015Article
- In vivo orientation of single myosin lever arms in zebrafish skeletal muscle.Biophysical journal · 2014Article
- Regulatory light chain mutants linked to heart disease modify the cardiac myosin lever arm.Biochemistry · 2013Article
- Single myosin cross-bridge orientation in cardiac papillary muscle detects lever-arm shear strain in transduction.Biochemistry · 2011Article
- Imaging skeletal muscle using second harmonic generation and coherent anti-Stokes Raman scattering microscopy.Biomedical optics express · 2011Article
- Article
- Fluorescence polarization/anisotropy in diagnostics and imaging.Chemical reviews · 2010Review
- Around-the-objective total internal reflection fluorescence microscopy.Applied optics · 2009Article
- Total internal reflection with fluorescence correlation spectroscopy: Applications to substrate-supported planar membranes.Journal of structural biology · 2009Article
- Probing membrane order and topography in supported lipid bilayers by combined polarized total internal reflection fluorescence-atomic force microscopy.Biophysical journal · 2009Article
- Single myosin lever arm orientation in a muscle fiber detected with photoactivatable GFP.Biochemistry · 2009Article
- Mapping microscope object polarized emission to the back focal plane pattern.Journal of biomedical opticsArticle
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 1 institution in 1 country.
Funding
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
Identifiers
What OpenQuestion holds
Registered trials
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.