Evidence map›Paper›PMID 23273426›Full record

ArticleStructure (London, England : 1993)2013

Accurate high-throughput structure mapping and prediction with transition metal ion FRET.

Xiaozhen Yu, Xiongwu Wu, Guillermo A Bermejo, Bernard R Brooks, Justin W Taraska

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
0.5field-weighted citation impact, top 37% 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

16 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. Review
  3. Deciphering DOM-metal binding using EEM-PARAFAC: Mechanisms, challenges, and perspectives.Environmental science and pollution research international · 2024
    Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Transition metal ion FRET uncovers KNature communications · 2016
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. 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 at 2 institutions in 1 country.

Xiaozhen YuLaboratory of Molecular Biophysics, National Heart Lung and Blood Institute, National Institutes of Health, Bethesda, MD 20892, USA.
Xiongwu WuLaboratory of Computational Biology, National Heart Lung and Blood Institute, National Institutes of Health, Bethesda, MD 20892, USA.
Guillermo A BermejoDivision of Computational Bioscience, Center for Information Technology, National Institutes of Health, Bethesda, MD 20892, USA.
Bernard R BrooksLaboratory of Computational Biology, National Heart Lung and Blood Institute, National Institutes of Health, Bethesda, MD 20892, USA.
Justin W TaraskaLaboratory of Molecular Biophysics, National Heart Lung and Blood Institute, National Institutes of Health, Bethesda, MD 20892, USA. Electronic address: justin.taraska@nih.gov.
National Heart Lung and Blood Institute · USNational Institutes of Health · US

Funding

Three-dimensional Structures Of Biological MacromoleculesZIAHL001027 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI BROOKS, BERNARD R · 2009 to 2025
$8.1M
Biomedical ImagingZIACT000090 · CIT · CENTER FOR INFORMATION TECHNOLOGY · PI TRUS, BENES L · 2009 to 2018
$7.8M
Imaging the structure and dynamics of membrane proteinsZIAHL006099 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI TARASKA, JUSTIN · 2011 to 2014
$1.8M
Intramural NIH HHS Z99 HL999999Intramural NIH HHS ZIA HL006099
6 · The paper itself

Abstract

Mapping the landscape of a protein's conformational space is essential to understanding its functions and regulation. The limitations of many structural methods have made this process challenging for most proteins. Here, we report that transition metal ion FRET (tmFRET) can be used in a rapid, highly parallel screen, to determine distances from multiple locations within a protein at extremely low concentrations. The distances generated through this screen for the protein maltose binding protein (MBP) match distances from the crystal structure to within a few angstroms. Furthermore, energy transfer accurately detects structural changes during ligand binding. Finally, fluorescence-derived distances can be used to guide molecular simulations to find low energy states. Our results open the door to rapid, accurate mapping and prediction of protein structures at low concentrations, in large complex systems, and in living cells.

Indexed as

Fluorescence Resonance Energy TransferAmino Acid SubstitutionApoproteinsCopperFluoresceinsFluorescence PolarizationFluorescent DyesMaltose-Binding ProteinsMolecular Dynamics SimulationMutagenesis, Site-DirectedNickelProtein Structure, SecondaryProtein Structure, TertiaryStaining and LabelingApoproteinsCopperfluorescein 5-maleimideFluoresceinsFluorescent DyesMaltose-Binding ProteinsNickel

Identifiers

PMID23273426
PMCPMC3700372
OpenAlexW2085513857

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.