Evidence map›Paper›PMID 28762198›Full record

ReviewBiophysical reviews2017

Directly watching biomolecules in action by high-speed atomic force microscopy.

Toshio Ando

Open access · bronzeAbstract readReview
In one paragraph

Review in Biophysical reviews, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
4.5field-weighted citation impact, top 5% of its field
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

25 citing papers in PubMed, 44 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Review
  5. Article
  6. A Single Shot of Vesicles.Microbes and environments · 2022
    Article
  7. Article
  8. Article
  9. Review
  10. Review
  11. Biological physics by high-speed atomic force microscopy.Philosophical transactions. Series A, Mathematical, physical, and engineering sciences · 2020
    Review
  12. Article
  13. Review
  14. Mechanotransduction, nanotechnology, and nanomedicine.Journal of biomedical research · 2020
    Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Coarse-Grained Protein Dynamics Studies Using Elastic Network Models.International journal of molecular sciences · 2018
    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

1 author at 1 institution in 1 country.

Toshio AndoBio-AFM Frontier Research Center, Institute of Science and Engineering, Kanazawa University, Kakuma-machi, Kanazawa, 920-1192, Japan. tando@staff.kanazawa-u.ac.jp.
Japan Science and Technology Agency · JP

Funding

Japan Science and Technology Agency #JPMJCR13M1Ministry of Education, Culture, Sports, Science and Technology #21113002Ministry of Education, Culture, Sports, Science and Technology #24227005Ministry of Education, Culture, Sports, Science and Technology #26119003
6 · The paper itself

Abstract

Proteins are dynamic in nature and work at the single molecule level. Therefore, directly watching protein molecules in dynamic action at high spatiotemporal resolution must be the most straightforward approach to understanding how they function. To make this observation possible, high-speed atomic force microscopy (HS-AFM) has been developed. Its current performance allows us to film biological molecules at 10-16 frames/s, without disturbing their function. In fact, dynamic structures and processes of various proteins have been successfully visualized, including bacteriorhodopsin responding to light, myosin V walking on actin filaments, and even intrinsically disordered proteins undergoing order/disorder transitions. The molecular movies have provided insights that could not have been reached in other ways. Moreover, the cantilever tip can be used to manipulate molecules during successive imaging. This capability allows us to observe changes in molecules resulting from dissection or perturbation. This mode of imaging has been successfully applied to myosin V, peroxiredoxin and doublet microtubules, leading to new discoveries. Since HS-AFM can be combined with other techniques, such as super-resolution optical microscopy and optical tweezers, the usefulness of HS-AFM will be further expanded in the near future.

Indexed as

Dynamic processesHigh-speed AFMImagingProteinsStructural changes

Identifiers

PMID28762198
PMCPMC5578924
OpenAlexW2741035180

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.