Evidence map›Paper›PMID 23200186›Full record

ReviewTrends in biochemical sciences2013

Bringing single-molecule spectroscopy to macromolecular protein complexes.

Chirlmin Joo, Mohamed Fareh, V Narry Kim

Abstract readReview
In one paragraph

Review in Trends in biochemical sciences, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing 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

13 citing papers in PubMed.

  1. Article
  2. Patterns (New York, N.Y.) · 2021
    Article
  3. Article
  4. Article
  5. Article
  6. Oligomerization of the tetramerization domain of p53 probed by two- and three-color single-molecule FRET.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Surface passivation for single-molecule protein studies.Journal of visualized experiments : JoVE · 2014
    Article
  12. Diversifying microRNA sequence and function.Nature reviews. Molecular cell biology · 2013
    Review
  13. 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

3 authors.

Chirlmin JooKavli Institute of NanoScience, Department of BioNanoScience, Delft University of Technology, 2628CJ, Delft, The Netherlands. c.joo@tudelft.nl
Mohamed Fareh
V Narry Kim

Funding

European Research Council 309509
6 · The paper itself

Abstract

Single-molecule fluorescence spectroscopy offers real-time, nanometer-resolution information. Over the past two decades, this emerging single-molecule technique has been rapidly adopted to investigate the structural dynamics and biological functions of proteins. Despite this remarkable achievement, single-molecule fluorescence techniques must be extended to macromolecular protein complexes that are physiologically more relevant for functional studies. In this review, we present recent major breakthroughs for investigating protein complexes within cell extracts using single-molecule fluorescence. We outline the challenges, future prospects and potential applications of these new single-molecule fluorescence techniques in biological and clinical research.

Indexed as

Spectrometry, FluorescenceAnimalsHumansModels, MolecularMultiprotein ComplexesMultiprotein Complexes

Identifiers

PMID23200186
PMCPMC3558732

What OpenQuestion holds

Textmetadata
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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.