Evidence map›Paper›PMID 29243093›Full record

ReviewBiophysical reviews2018

Single-molecule fluorescence-based analysis of protein conformation, interaction, and oligomerization in cellular systems.

Kenji Okamoto, Michio Hiroshima, Yasushi Sako

Abstract readReview
In one paragraph

Review in Biophysical reviews, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing 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

12 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. Single-Molecule Imaging in Living Plant Cells: A Methodological Review.International journal of molecular sciences · 2021
    Review
  9. Illuminating amyloid fibrils: Fluorescence-based single-molecule approaches.Computational and structural biotechnology journal · 2021
    Review
  10. Article
  11. Article
  12. Article
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

3 authors.

Kenji OkamotoCellular Informatics Laboratory, RIKEN, 2-1 Hirosawa, Wako, 351-0198, Japan.
Michio HiroshimaCellular Informatics Laboratory, RIKEN, 2-1 Hirosawa, Wako, 351-0198, Japan.
Yasushi SakoCellular Informatics Laboratory, RIKEN, 2-1 Hirosawa, Wako, 351-0198, Japan. sako@riken.jp.ORCID http://orcid.org/0000-0002-5707-5455

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Single-molecule imaging (SMI) of proteins in operation has a history of intensive investigations over 20 years and is now widely used in various fields of biology and biotechnology. We review the recent advances in SMI of fluorescently-tagged proteins in structural biology, focusing on technical applicability of SMI to the measurements in living cells. Basic technologies and recent applications of SMI in structural biology are introduced. Distinct from other methods in structural biology, SMI directly observes single molecules and single-molecule events one-by-one, thus, explicitly analyzing the distribution of protein structures and the history of protein dynamics. It also allows one to detect single events of protein interaction. One unique feature of SMI is that it is applicable in complicated and heterogeneous environments, including living cells. The numbers, location, movements, interaction, oligomerization, and conformation of single-protein molecules have been determined using SMI in cellular systems.

Indexed as

Fluorescence resonance energy transfer (FRET)Reaction kineticsSingle-molecule imaging (SMI)Single-photon counting (SPC)Super-resolution microscope

Identifiers

PMID29243093
PMCPMC5899725

What OpenQuestion holds

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LicenceCC BY
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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.