Evidence map›Paper›PMID 21182275›Full record

ArticleJournal of the American Chemical Society2011

Engineering encodable lanthanide-binding tags into loop regions of proteins.

Katja Barthelmes, Anne M Reynolds, Ezra Peisach, Hendrik R A Jonker, Nicholas J DeNunzio, Karen N Allen, Barbara Imperiali, Harald Schwalbe

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2011. 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
–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

46 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Lanthanide Tagging of Oligonucleotides to Nucleobase for Paramagnetic NMR.Chembiochem : a European journal of chemical biology · 2020
    Article
  16. Article
  17. Paramagnetic NMR in drug discovery.Journal of biomolecular NMR · 2020
    Review
  18. A Double-Armed, Hydrophilic Transition Metal Complex as a Paramagnetic NMR Probe.Angewandte Chemie (International ed. in English) · 2019
    Review
  19. Article
  20. 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

8 authors.

Katja BarthelmesInstitute for Organic Chemistry and Chemical Biology, Center for Biomolecular Magnetic Resonance, Johann Wolfgang Goethe-University of Frankfurt, Max-von-Laue-Strasse 7, 60438 Frankfurt, Germany.
Anne M Reynolds
Ezra Peisach
Hendrik R A Jonker
Nicholas J DeNunzio
Karen N Allen
Barbara Imperiali
Harald Schwalbe

Funding

LBTs as Probes of the Trafficking of Interleukin-1 betaF32GM076931 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI REYNOLDS, ANNE M · 2006 to 2008
$129k
NIGMS NIH HHS F32 GM076931
6 · The paper itself

Abstract

Lanthanide-binding tags (LBTs) are valuable tools for investigation of protein structure, function, and dynamics by NMR spectroscopy, X-ray crystallography, and luminescence studies. We have inserted LBTs into three different loop positions (denoted L, R, and S) of the model protein interleukin-1β (IL1β) and varied the length of the spacer between the LBT and the protein (denoted 1−3). Luminescence studies demonstrate that all nine constructs bind Tb3+ tightly in the low nanomolar range. No significant change in the fusion protein occurs from insertion of the LBT, as shown by two X-ray crystallographic structures of the IL1β-S1 and IL1β-L3 constructs and for the remaining constructs by comparing the 1H−15N heteronuclear single-quantum coherence NMR spectra with that of the wild-type IL1β. Additionally, binding of LBT-loop IL1β proteins to their native binding partner in vitro remains unaltered. X-ray crystallographic phasing was successful using only the signal from the bound lanthanide. Large residual dipolar couplings (RDCs) could be determined by NMR spectroscopy for all LBT-loop constructs and revealed that the LBT-2 series were rigidly incorporated into the interleukin-1β structure. The paramagnetic NMR spectra of loop-LBT mutant IL1β-R2 were assigned and the Δχ tensor components were calculated on the basis of RDCs and pseudocontact shifts. A structural model of the IL1β-R2 construct was calculated using the paramagnetic restraints. The current data provide support that encodable LBTs serve as versatile biophysical tags when inserted into loop regions of proteins of known structure or predicted via homology modeling.

Indexed as

Amino Acid SequenceCrystallography, X-RayFeasibility StudiesHumansInterleukin-1betaLanthanoid Series ElementsModels, MolecularMolecular ProbesMolecular Sequence DataNuclear Magnetic Resonance, BiomolecularPeptidesProtein EngineeringProtein Structure, SecondaryReceptors, Interleukin-1Interleukin-1betaLanthanoid Series ElementsMolecular ProbesPeptidesReceptors, Interleukin-1

Identifiers

PMID21182275
PMCPMC3043167

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Registered trials

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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.