Evidence map›Paper›PMID 22739670›Full record

ArticleMolecular bioSystems2012

Intramolecular three-colour single pair FRET of intrinsically disordered proteins with increased dynamic range.

Sigrid Milles, Christine Koehler, Yann Gambin, Ashok A Deniz, Edward A Lemke

Abstract read
In one paragraph

Article in Molecular bioSystems, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing 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

18 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Choosing the Probe for Single-Molecule Fluorescence Microscopy.International journal of molecular sciences · 2022
    Review
  6. Article
  7. Review
  8. Review
  9. Article
  10. Review
  11. Article
  12. Review
  13. Review
  14. 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
  15. The bright future of single-molecule fluorescence imaging.Current opinion in chemical biology · 2014
    Review
  16. Review
  17. Article
  18. 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

5 authors.

Sigrid MillesEMBL, Structural and Computational Biology Unit, Meyerhofstrasse 1, 69117 Heidelberg, Germany.
Christine Koehler
Yann Gambin
Ashok A Deniz
Edward A Lemke

Funding

Single Molecule Studies of Protein Folding MechanismsR01GM066833 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI DENIZ, ASHOK A · 2003 to 2017
$5.2M
NIGMS NIH HHS GM066833NIGMS NIH HHS R01 GM066833
6 · The paper itself

Abstract

Single molecule observation of fluorescence resonance energy transfer can be used to provide insight into the structure and dynamics of proteins. Using a straightforward triple-colour labelling strategy, we present a measurement and analysis scheme that can simultaneously study multiple regions within single intrinsically disordered proteins.

Indexed as

CarbocyaninesColorEscherichia coliFluorescence Resonance Energy TransferFluorescent DyesHumansHydrazinesMolecular ImagingNuclear Pore Complex ProteinsOrganic ChemicalsProtein ConformationProtein Structure, TertiaryRecombinant ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSpectrometry, FluorescenceAlexa 488 hydrazideAlexa594Alexa Fluor 647CarbocyaninesFluorescent DyesHydrazinesNuclear Pore Complex ProteinsNUP49 protein, S cerevisiaeOrganic ChemicalsRecombinant ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID22739670
PMCPMC3441834

What OpenQuestion holds

Textmetadata
LicenceTDM
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.