Evidence map›Paper›PMID 12018483›Full record

ArticleJournal of biomolecular NMR2002

Structure-independent cross-validation between residual dipolar couplings originating from internal and external orienting media.

Renato Barbieri, Ivano Bertini, Yong-Min Lee, Claudio Luchinat, Aldrik H Velders

Abstract read
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In one paragraph

Article in Journal of biomolecular NMR, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
1.0field-weighted citation impact, top 26% 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

6 citing papers in PubMed, 15 citations in OpenAlex.

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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

5 authors at 2 institutions in 1 country.

Renato BarbieriMagnetic Resonance Center CERM, Department of Chemistry, University of Florence, Sesto Fiorentino, Italy.
Ivano Bertini
Yong-Min Lee
Claudio Luchinat
Aldrik H Velders
University of Florence · ITInteruniversity Consortium for Magnetic Resonance · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lanthanide-substituted calcium binding proteins are known to partially orient in high magnetic fields. Orientation provides residual dipolar couplings (rdc's). Two of these systems, Tm3+- and Dy3+-substituted calbindin D9k, dissolved in an external orienting medium (nonionic liquid crystalline phase) provide rdc values which are the sum of those induced by the lanthanides and by the liquid crystalline phase on the native calcium binding protein. This structure-independent check shows the innocence of the orienting medium with respect to the structure of the protein in solution. Furthermore, the simultaneous use of lanthanide substitution and external orienting media provides a further effective tool to control and tune the orientation tensor.

Indexed as

CalbindinsLanthanoid Series ElementsNuclear Magnetic Resonance, BiomolecularReproducibility of ResultsS100 Calcium Binding Protein GStatistics as TopicCalbindinsLanthanoid Series ElementsS100 Calcium Binding Protein G

Identifiers

PMID12018483
OpenAlexW150089293

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.