Evidence map›Paper›PMID 11200529›Full record

ArticleJournal of biomolecular NMR2000

Lanthanide induced residual dipolar couplings for the conformational investigation of peripheral 15NH2 moieties.

I Bertini, I C Felli, C Luchinat

Abstract read
PubMed Publisher
In one paragraph

Article in Journal of biomolecular NMR, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

8 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. The dynamic duo: combining NMR and small angle scattering in structural biology.Protein science : a publication of the Protein Society · 2014
    Review
  5. Article
  6. Article
  7. Article
  8. 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

3 authors at 2 institutions in 1 country.

I BertiniMagnetic Resonance Center (CERM), University of Florence, Italy. bertini@cerm.unifi.it
I C Felli
C Luchinat
University of Florence · ITInteruniversity Consortium for Magnetic Resonance · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Ca2 calbindin protein in which one calcium has been substituted with Ce(III), Yb(III) and Dy(III) displays substantial alignment in high magnetic fields due to the high anisotropy of the metal magnetic susceptibility. This property has allowed the measurement of residual dipolar coupling contributions to 1J(HN) and 2J(HH) couplings of asparagine and glutamine NH2 moieties. Such data have been used to aid structural characterization of these groups. The exploitation of auto-orientation of magnetic anisotropic metalloproteins represents a step ahead in the investigation of the conformational space of peripheral residues that are not fixed by the protein folding.

Indexed as

Metals, Rare EarthAnisotropyAsparagineBinding SitesCalbindinsCeriumDysprosiumGlutamineMagneticsMetalloproteinsNitrogen IsotopesNuclear Magnetic Resonance, BiomolecularProtein Structure, TertiaryS100 Calcium Binding Protein GYtterbiumAsparagineCalbindinsCeriumDysprosiumGlutamineMetalloproteinsMetals, Rare EarthNitrogen IsotopesS100 Calcium Binding Protein GYtterbium

Identifiers

PMID11200529
OpenAlexW239678431

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.