Evidence map›Paper›PMID 23389011›Full record

ArticleOptics express2013

Single-molecule fluorescence imaging of processive myosin with enhanced background suppression using linear zero-mode waveguides (ZMWs) and convex lens induced confinement (CLIC).

Mary Williard Elting, Sabrina R Leslie, L Stirling Churchman, Jonas Korlach, Christopher M J McFaul, Jason S Leith, Michael J Levene, Adam E Cohen, James A Spudich

Abstract read
In one paragraph

Article in Optics express, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
–field-weighted citation impact
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

20 citing papers in PubMed.

  1. Article
  2. Review
  3. Single-Molecule Mechanochemical Sensing.Accounts of chemical research · 2022
    Article
  4. Biophysical reviews · 2022
    Article
  5. Article
  6. Article
  7. Article
  8. Real-time 3D single molecule tracking.Nature communications · 2020
    Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. Review
  16. Review
  17. Adam Cohen: visualizing cellular voltage.The Journal of cell biology · 2014
    Article
  18. Article
  19. High-throughput platform for real-time monitoring of biological processes by multicolor single-molecule fluorescence.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  20. Review
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

9 authors.

Mary Williard EltingDepartment of Applied Physics, Stanford University, Stanford, California 94305, USA.
Sabrina R Leslie
L Stirling Churchman
Jonas Korlach
Christopher M J McFaul
Jason S Leith
Michael J Levene
Adam E Cohen
James A Spudich

Funding

MYOSIN MOVEMENT IN VITRO: MOLECULAR CHARACTERIZATIONR01GM033289 · NIGMS · STANFORD UNIVERSITY · PI SPUDICH, JAMES · 1985 to 2024
$13.6M
NIGMS NIH HHS GM33289NIGMS NIH HHS R01 GM033289
6 · The paper itself

Abstract

Resolving single fluorescent molecules in the presence of high fluorophore concentrations remains a challenge in single-molecule biophysics that limits our understanding of weak molecular interactions. Total internal reflection fluorescence (TIRF) imaging, the workhorse of single-molecule fluorescence microscopy, enables experiments at concentrations up to about 100 nM, but many biological interactions have considerably weaker affinities, and thus require at least one species to be at micromolar or higher concentration. Current alternatives to TIRF often require three-dimensional confinement, and thus can be problematic for extended substrates, such as cytoskeletal filaments. To address this challenge, we have demonstrated and applied two new single-molecule fluorescence microscopy techniques, linear zero-mode waveguides (ZMWs) and convex lens induced confinement (CLIC), for imaging the processive motion of molecular motors myosin V and VI along actin filaments. Both technologies will allow imaging in the presence of higher fluorophore concentrations than TIRF microscopy. They will enable new biophysical measurements of a wide range of processive molecular motors that move along filamentous tracks, such as other myosins, dynein, and kinesin. A particularly salient application of these technologies will be to examine chemomechanical coupling by directly imaging fluorescent nucleotide molecules interacting with processive motors as they traverse their actin or microtubule tracks.

Indexed as

LensesActinsAdenosine TriphosphateAnimalsBiophysicsComputer SimulationCytoskeletonDyneinsEquipment DesignInsectaKinesinsMicroscopyMicroscopy, FluorescenceMicrotubulesMyosinsOptical ImagingActinsAdenosine TriphosphateDyneinsKinesinsMyosins

Identifiers

PMID23389011
PMCPMC3632498

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

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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.