Evidence map›Paper›PMID 26728075›Full record

ArticleJournal of biomolecular NMR2016

UTOPIA NMR: activating unexploited magnetization using interleaved low-gamma detection.

Aldino Viegas, Thibault Viennet, Tsyr-Yan Yu, Frank Schumann, Wolfgang Bermel, Gerhard Wagner, Manuel Etzkorn

Abstract read
In one paragraph

Article in Journal of biomolecular NMR, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing 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

9 citing papers in PubMed.

  1. Article
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  3. OptimalNature protocols · 2024
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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

7 authors.

Aldino ViegasInstitute of Physical Biology, Heinrich-Heine-University, Düsseldorf, Germany.
Thibault ViennetInstitute of Physical Biology, Heinrich-Heine-University, Düsseldorf, Germany.
Tsyr-Yan YuDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA, USA.
Frank SchumannBruker BioSpin GmbH, Fällanden, Switzerland.
Wolfgang BermelBruker BioSpin GmbH, Rheinstetten, Germany.
Gerhard WagnerDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA, USA.
Manuel EtzkornInstitute of Physical Biology, Heinrich-Heine-University, Düsseldorf, Germany. manuel.etzkorn@hhu.de.ORCID http://orcid.org/0000-0002-9796-3246

Funding

T CELL SPECIFIC TRANSCRIPTION COMPLEXESP01GM047467 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI WAGNER, GERHARD · 1992 to 2017
$28.6M
OverallP41EB002026 · NIBIB · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI GRIFFIN, ROBERT GUY · 2003 to 2018
$17.9M
Structure and interactions of the Voltage-Dependent Anion Channel(VDAC)R01GM075879 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI WAGNER, GERHARD · 2005 to 2013
$2.3M
800 MHz Triple Resonance Observe (TXO) Detection CryoProbeS10RR026417 · NCRR · HARVARD MEDICAL SCHOOL · PI WAGNER, GERHARD · 2010 to 2010
$359k
NCRR NIH HHS S10 RR026417NIBIB NIH HHS EB002026NIBIB NIH HHS P41 EB002026NIGMS NIH HHS GM047467NIGMS NIH HHS GM075879NIGMS NIH HHS P01 GM047467NIGMS NIH HHS R01 GM075879
6 · The paper itself

Abstract

A growing number of nuclear magnetic resonance (NMR) spectroscopic studies are impaired by the limited information content provided by the standard set of experiments conventionally recorded. This is particularly true for studies of challenging biological systems including large, unstructured, membrane-embedded and/or paramagnetic proteins. Here we introduce the concept of unified time-optimized interleaved acquisition NMR (UTOPIA-NMR) for the unified acquisition of standard high-γ (e.g. (1)H) and low-γ (e.g. (13)C) detected experiments using a single receiver. Our aim is to activate the high level of polarization and information content distributed on low-γ nuclei without disturbing conventional magnetization transfer pathways. We show that using UTOPIA-NMR we are able to recover nearly all of the normally non-used magnetization without disturbing the standard experiments. In other words, additional spectra, that can significantly increase the NMR insights, are obtained for free. While we anticipate a broad range of possible applications we demonstrate for the soluble protein Bcl-xL (ca. 21 kDa) and for OmpX in nanodiscs (ca. 160 kDa) that UTOPIA-NMR is particularly useful for challenging protein systems including perdeuterated (membrane) proteins.

Indexed as

Membrane ProteinsNuclear Magnetic Resonance, BiomolecularMembrane Proteins13C-detectionInterleaved acquisitionLow-γ nucleiUTOPIA-NMR

Identifiers

PMID26728075
PMCPMC4947531

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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.