Evidence map›Paper›PMID 18341279›Full record

ArticleJournal of the American Chemical Society2008

Resolution enhancement in solid-state NMR of oriented membrane proteins by anisotropic differential linebroadening.

Thomas Vosegaard, Kresten Bertelsen, Jan M Pedersen, Lea Thøgersen, Birgit Schiøtt, Emad Tajkhorshid, Troels Skrydstrup, Niels Chr Nielsen

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

5 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
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  5. 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.

Thomas VosegaardCenter for Insoluble Protein Structures and Department of Chemistry, University of Aarhus, Langelandsgade 140, DK-8000 Aarhus C, Denmark. tv@chem.au.dk
Kresten Bertelsen
Jan M Pedersen
Lea Thøgersen
Birgit Schiøtt
Emad Tajkhorshid
Troels Skrydstrup
Niels Chr Nielsen

Funding

System-Level Simulation of a Bioenergetic MembraneR01GM067887 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI TAJKHORSHID, EMAD · 2003 to 2018
$4.0M
NIGMS NIH HHS R01 GM067887NIGMS NIH HHS R01-GM067887
6 · The paper itself

Abstract

We demonstrate that a significant improvement in the spectral resolution may be achieved in solid-state NMR experiments of proteins in inhomogeneously disordered oriented lipid bilayers. Using 1H homonuclear decoupling instead of standard 1H heteronuclear decoupling, the 15N line widths may be reduced by up to seven times for such samples. For large oriented membrane proteins, such resolution enhancements may be crucial for assignment and structural interpretation.

Indexed as

ThermodynamicsMembrane ProteinsNuclear Magnetic Resonance, BiomolecularMembrane Proteins

Identifiers

PMID18341279
PMCPMC5706113

What OpenQuestion holds

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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.