ArticleProceedings of the National Academy of Sciences of the United States of America1998
Myosin conformational states determined by single fluorophore polarization.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
What it found
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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.
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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.
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Who cites it
36 citing papers in PubMed, 119 citations in OpenAlex.
- Examination of conformational dynamics of AdiC transporter with fluorescence-polarization microscopy.The Journal of general physiology · 2025Article
- Article
- Dynamics of ATP-dependent and ATP-independent steppings of myosin-V on actin: catch-bond characteristics.Journal of the Royal Society, Interface · 2020Article
- Super-resolution imaging of fluorescent dipoles via polarized structured illumination microscopy.Nature communications · 2019Article
- A model for the chemomechanical coupling of myosin-V molecular motors.RSC advances · 2019Article
- Use of Single Molecule Fluorescence Polarization Microscopy to Study Protein Conformation and Dynamics of Kinesin-Microtubule Complexes.Methods in molecular biology (Clifton, N.J.) · 2018Article
- DNA-Endonuclease Complex Dynamics by Simultaneous FRET and Fluorophore Intensity in Evanescent Field.Biophysical journal · 2017Article
- Phosphorylation of myosin regulatory light chain has minimal effect on kinetics and distribution of orientations of cross bridges of rabbit skeletal muscle.American journal of physiology. Regulatory, integrative and comparative physiology · 2014Article
- Breaking the millisecond barrier: single molecule motors wobble to find their next binding sites.Biophysical journal · 2013Article
- Mesoscopic analysis of motion and conformation of cross-bridges.Biophysical reviews · 2012Review
- Mechanical coupling between myosin molecules causes differences between ensemble and single-molecule measurements.Biophysical journal · 2012Article
- Observing cycling of a few cross-bridges during isometric contraction of skeletal muscle.Cytoskeleton (Hoboken, N.J.) · 2010Article
- Single molecule kinetics in the familial hypertrophic cardiomyopathy D166V mutant mouse heart.Journal of molecular and cellular cardiology · 2010Article
- Structure and dynamics of the kinesin-microtubule interaction revealed by fluorescence polarization microscopy.Methods in cell biology · 2010Review
- Site-directed spectroscopic probes of actomyosin structural dynamics.Annual review of biophysics · 2009Review
- Measurement of single macromolecule orientation by total internal reflection fluorescence polarization microscopy.Biophysical journal · 2005Article
- Rotation of the lever arm of Myosin in contracting skeletal muscle fiber measured by two-photon anisotropy.Biophysical journal · 2004Article
- Single-molecule dynamics of the calcium-dependent activation of plasma-membrane Ca2+-ATPase by calmodulin.Biophysical journal · 2004Article
- Conformational change of the actomyosin complex drives the multiple stepping movement.Proceedings of the National Academy of Sciences of the United States of America · 2002Article
- Spectroscopy of single phycoerythrocyanin monomers: dark state identification and observation of energy transfer heterogeneities.Biophysical journal · 2002Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
Abstract
Muscle contraction is powered by the interaction of the molecular motor myosin with actin. With new techniques for single molecule manipulation and fluorescence detection, it is now possible to correlate, within the same molecule and in real time, conformational states and mechanical function of myosin. A spot-confocal microscope, capable of detecting single fluorophore polarization, was developed to measure orientational states in the smooth muscle myosin light chain domain during the process of motion generation. Fluorescently labeled turkey gizzard smooth muscle myosin was prepared by removal of endogenous regulatory light chain and re-addition of the light chain labeled at cysteine-108 with the 6-isomer of iodoacetamidotetramethylrhodamine (6-IATR). Single myosin molecule fluorescence polarization data, obtained in a motility assay, provide direct evidence that the myosin light chain domain adopts at least two orientational states during the cyclic interaction of myosin with actin, a randomly disordered state, most likely associated with myosin whereas weakly bound to actin, and an ordered state in which the light chain domain adopts a finite angular orientation whereas strongly bound after the powerstroke.
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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.