Evidence map›Paper›PMID 22851279›Full record

ArticleProtein science : a publication of the Protein Society2012

Lanthanide binding and IgG affinity construct: potential applications in solution NMR, MRI, and luminescence microscopy.

Adam W Barb, Tienhuei Grace Ho, Heather Flanagan-Steet, James H Prestegard

Open access · bronzeAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
0.6field-weighted citation impact, top 33% 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

12 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Paramagnetic NMR in drug discovery.Journal of biomolecular NMR · 2020
    Review
  6. Review
  7. General lack of structural characterization of chemically synthesized long peptides.Protein science : a publication of the Protein Society · 2019
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Sparse labeling of proteins: structural characterization from long range constraints.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2014
    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

4 authors at 1 institution in 1 country.

Adam W BarbComplex Carbohydrate Research Center, The University of Georgia, Athens, Georgia, USA.
Tienhuei Grace Ho
Heather Flanagan-Steet
James H Prestegard
University of Georgia · US

Funding

TR&D3. Approaches to Proteoglycan Function at Biochemical and Cellular LevelsP41GM103390 · NIGMS · UNIVERSITY OF GEORGIA · PI LIVE, DAVID H · 2012 to 2019
$14.5M
NMR of Cell Surface OligosaccharidesR01GM033225 · NIGMS · YALE UNIVERSITY · PI PRESTEGARD, JAMES H. · 1985 to 2021
$4.6M
NMR Studies on the Structure and Dynamics of Glycan-Mediated IgG InteractionsF32AR058084 · NIAMS · UNIVERSITY OF GEORGIA · PI BARB, ADAM WESLEY · 2010 to 2012
$146k
NIAMS NIH HHS F32AR058084NIGMS NIH HHS P41 GM103390NIGMS NIH HHS P41GM103390NIGMS NIH HHS R01GM033225
6 · The paper itself

Abstract

Paramagnetic lanthanide ions when bound to proteins offer great potential for structural investigations that utilize solution nuclear magnetic resonance spectroscopy, magnetic resonance imaging, or optical microscopy. However, many proteins do not have native metal ion binding sites and engineering a chimeric protein to bind an ion while retaining affinity for a protein of interest represents a significant challenge. Here we report the characterization of an immunoglobulin G-binding protein redesigned to include a lanthanide binding motif in place of a loop between two helices (Z-L2LBT). It was shown to bind Tb³⁺ with 130 nM affinity. Ions such as Dy³⁺, Yb³⁺, and Ce³⁺ produce paramagnetic effects on NMR spectra and the utility of these effects is illustrated by their use in determining a structural model of the metal-complexed Z-L2LBT protein and a preliminary characterization of the dynamic distribution of IgG Fc glycan positions. Furthermore, this designed protein is demonstrated to be a novel IgG-binding reagent for magnetic resonance imaging (Z-L2LBT:Gd³⁺ complex) and luminescence microscopy (Z-L2LBT: Tb³⁺ complex).

Indexed as

GlycoproteinsHumansImmunoglobulin Fc FragmentsImmunoglobulin GIndicators and ReagentsLanthanoid Series ElementsLuminescent MeasurementsMagnetic Resonance ImagingMicroscopy, FluorescenceNuclear Magnetic Resonance, BiomolecularProtein BindingProtein EngineeringProtein Structure, TertiaryGlycoproteinsImmunoglobulin Fc FragmentsImmunoglobulin GIndicators and ReagentsLanthanoid Series Elements

Identifiers

PMID22851279
PMCPMC3526988
OpenAlexW2106739599

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.