Evidence map›Paper›PMID 29610485›Full record

ArticleNature chemical biology2018

Super-long single-molecule tracking reveals dynamic-anchorage-induced integrin function.

Taka A Tsunoyama, Yusuke Watanabe, Junri Goto, Kazuma Naito, Rinshi S Kasai, Kenichi G N Suzuki, Takahiro K Fujiwara, Akihiro Kusumi

Abstract read
PubMed Publisher
In one paragraph

Article in Nature chemical biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed
13.7field-weighted citation impact, top 1% 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

60 citing papers in PubMed, 128 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Review
  18. Article
  19. Review
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 2 institutions in 1 country.

Taka A TsunoyamaMembrane Cooperativity Unit, Okinawa Institute of Science and Technology Graduate University (OIST), Onna, Japan.ORCID http://orcid.org/0000-0003-1457-7612
Yusuke WatanabeInstitute for Integrated Cell-Material Sciences (WPI-iCeMS), Kyoto University, Kyoto, Japan.
Junri GotoInstitute for Integrated Cell-Material Sciences (WPI-iCeMS), Kyoto University, Kyoto, Japan.
Kazuma NaitoInstitute for Integrated Cell-Material Sciences (WPI-iCeMS), Kyoto University, Kyoto, Japan.
Rinshi S KasaiInstitute for Frontier Life and Medical Sciences, Kyoto University, Kyoto, Japan.
Kenichi G N SuzukiInstitute for Integrated Cell-Material Sciences (WPI-iCeMS), Kyoto University, Kyoto, Japan.
Takahiro K FujiwaraInstitute for Integrated Cell-Material Sciences (WPI-iCeMS), Kyoto University, Kyoto, Japan.
Akihiro KusumiMembrane Cooperativity Unit, Okinawa Institute of Science and Technology Graduate University (OIST), Onna, Japan. akihiro.kusumi@oist.jp.
Kyoto University · JPOkinawa Institute of Science and Technology Graduate University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Single-fluorescent-molecule imaging tracking (SMT) is becoming an important tool to study living cells. However, photobleaching and photoblinking (hereafter referred to as photobleaching/photoblinking) of the probe molecules strongly hamper SMT studies of living cells, making it difficult to observe in vivo molecular events and to evaluate their lifetimes (e.g., off rates). The methods used to suppress photobleaching/photoblinking in vitro are difficult to apply to living cells because of their toxicities. Here using 13 organic fluorophores we found that, by combining low concentrations of dissolved oxygen with a reducing-plus-oxidizing system, photobleaching/photoblinking could be strongly suppressed with only minor effects on cells, which enabled SMT for as long as 12,000 frames (~7 min at video rate, as compared to the general 10-s-order durations) with ~22-nm single-molecule localization precisions. SMT of integrins revealed that they underwent temporary (<80-s) immobilizations within the focal adhesion region, which were responsible for the mechanical linkage of the actin cytoskeleton to the extracellular matrix.

Indexed as

Microscopy, FluorescenceActin CytoskeletonAnimalsCell AdhesionCHO CellsCricetulusExtracellular MatrixFluorescent DyesHeLa CellsHumansIntegrin beta1Integrin beta3IntegrinsMiceNIH 3T3 CellsOxidation-ReductionFluorescent DyesIntegrin beta1Integrin beta3IntegrinsOxygen

Identifiers

PMID29610485
OpenAlexW2795180687

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.