ReviewAnnual review of physical chemistry2010
Subcellular dynamics and protein conformation fluctuations measured by Fourier imaging correlation spectroscopy.
Review in Annual review of physical chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 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.
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.
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Who cites it
3 citing papers in PubMed, 10 citations in OpenAlex.
- Using microsecond single-molecule FRET to determine the assembly pathways of T4 ssDNA binding protein onto model DNA replication forks.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Using Multiorder Time-Correlation Functions (TCFs) To Elucidate Biomolecular Reaction Pathways from Microsecond Single-Molecule Fluorescence Experiments.The journal of physical chemistry. B · 2016Article
- Biological physics in México: Review and new challenges.Journal of biological physics · 2011Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Novel high signal-to-noise spectroscopic experiments that probe the dynamics of microscopic objects have the potential to reveal complex intracellular biochemical mechanisms, or the slow relaxations of soft matter systems. This article reviews the implementation of Fourier imaging correlation spectroscopy (FICS), a phase-selective approach to fluorescence fluctuation spectroscopy that employs a unique route to elevate signal levels while acquiring detailed information about molecular coordinate trajectories. The review demonstrates the broad applicability of FICS by discussing two recent studies. The dynamics of Saccharomyces cerevisiae yeast mitochondria are characterized with FICS and provide detailed information about the influence of specific cytoskeletal elements on the movement of this organelle. In another set of experiments, polarization-modulated FICS captures conformational dynamics and molecular translational dynamics of the fluorescent protein DsRed, and analyses by four-point correlation and joint distribution functions of the corresponding data reveal statistically meaningful pathways of DsRed switching between different optical conformations.
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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.