ArticleBiophysical journal2007
Fluorescence lifetime imaging to detect actomyosin states in mammalian muscle sarcomeres.
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 8 papers.
What it found
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Who cites it
8 citing papers in PubMed, 12 citations in OpenAlex.
- Fluorescence lifetime imaging microscopy of endogenous fluorophores in health and disease.Journal of muscle research and cell motility · 2025Review
- A revised conceptual framework for mouse vomeronasal pumping and stimulus sampling.Current biology : CB · 2024Article
- Metazoan Hsp70 machines use Hsp110 to power protein disaggregation.The EMBO journal · 2012Article
- Response of rigor cross-bridges to stretch detected by fluorescence lifetime imaging microscopy of myosin essential light chain in skeletal muscle fibers.The Journal of biological chemistry · 2011Article
- FRET characterisation for cross-bridge dynamics in single-skinned rigor muscle fibres.European biophysics journal : EBJ · 2011Article
- Fluorescence lifetime imaging reveals that the environment of the ATP binding site of myosin in muscle senses force.Biophysical journal · 2010Article
- Fluorescence lifetime measurements and biological imaging.Chemical reviews · 2010Review
- Fluorescence lifetime of actin in the familial hypertrophic cardiomyopathy transgenic heart.Biochemistry · 2009Article
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 2 countries.
Funding
Abstract
We investigated the use of fluorescence lifetime imaging microscopy (FLIM) of a fluorescently labeled ATP analog (3'-O-{N-[3-(7-diethylaminocoumarin-3-carboxamido)propyl]carbamoyl}ATP) to probe in permeabilized muscle fibers the changes in the environment of the nucleotide binding pocket caused by interaction with actin. Spatial averaging of FLIM data of muscle sarcomeres reduces photon noise, permitting detailed analysis of the fluorescence decay profiles. FLIM reveals that the lifetime of the nucleotide, in its ADP form because of the low concentration of nucleotide present, changes depending on whether the nucleotide is free in solution or bound to myosin, and on whether the myosin is bound to actin in an actomyosin complex. Characterization of the fluorescence decays by a multiexponential function allowed us to resolve the lifetimes and amplitudes of each of these populations, namely, the fluorophore bound to myosin, bound to actin, in an actomyosin complex, and free in the filament lattice. This novel application of FLIM to muscle fibers shows that with spatial averaging, detailed information about the nature of nucleotide complexes can be derived.
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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.