Evidence map›Paper›PMID 15213432›Full record

ArticleJournal of biomolecular NMR2004

Novel techniques for weak alignment of proteins in solution using chemical tags coordinating lanthanide ions.

Takahisa Ikegami, Laurent Verdier, Peyman Sakhaii, Susanne Grimme, Barbara Pescatore, Krishna Saxena, Klaus M Fiebig, Christian Griesinger

Abstract read
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In one paragraph

Article in Journal of biomolecular NMR, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
4.9field-weighted citation impact, top 4% 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

46 citing papers in PubMed, 133 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Paramagnetic Ligand Tagging To Identify Protein Binding Sites.Journal of the American Chemical Society · 2015
    Article
  8. Article
  9. Visualizing transient dark states by NMR spectroscopy.Quarterly reviews of biophysics · 2015
    Article
  10. Multiple paramagnetic effects through a tagged reporter protein.Angewandte Chemie (International ed. in English) · 2015
    Article
  11. Sparse labeling of proteins: structural characterization from long range constraints.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2014
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
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  19. Review
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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

8 authors at 4 institutions in 3 countries.

Takahisa IkegamiMax-Planck Institute for Biophysical Chemistry, Department of NMR Based Structural Biology, University of Frankfurt am Fassberg 11, D-37077 Göttingen, Germany.
Laurent Verdier
Peyman Sakhaii
Susanne Grimme
Barbara Pescatore
Krishna Saxena
Klaus M Fiebig
Christian Griesinger
Marie Curie · GBMax Planck Institute for Biophysical Chemistry · DEGoethe University Frankfurt · DEUniversity of Toronto · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A molecule with an anisotropic magnetic susceptibility is spontaneously aligned in a static magnetic field. Alignment of such a molecule yields residual dipolar couplings and pseudocontact shifts. Lanthanide ions have recently been successfully used to provide an anisotropic magnetic susceptibility in target molecules either by replacing a calcium ion with a lanthanide ion in calcium-binding proteins or by attaching an EDTA derivative to a cysteine residue via a disulfide bond. Here we describe a novel enantiomerically pure EDTA derived tag that aligns stronger due to its shorter linker and does not suffer from stereochemical diversity upon lanthanide complexation. We observed residual (15)N,(1)H-dipolar couplings of up to 8 Hz at 800 MHz induced by a single alignment tensor from this tag.

Indexed as

AnisotropyCalciumCarbonic AcidDisulfidesEdetic AcidIonsLanthanoid Series ElementsMagnetic Resonance SpectroscopyModels, ChemicalModels, MolecularModels, StatisticalNitrogenProtein BindingProtein ConformationStereoisomerismCalciumCarbonic AcidDisulfidesEdetic AcidIonsLanthanoid Series ElementsNitrogen

Identifiers

PMID15213432
OpenAlexW2011397327

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.