Evidence map›Paper›PMID 25375235›Full record

ArticlePloS one2014

NMR-based detection of hydrogen/deuterium exchange in liposome-embedded membrane proteins.

Xuejun Yao, Ulrich H N Dürr, Zrinka Gattin, Yvonne Laukat, Rhagavendran L Narayanan, Ann-Kathrin Brückner, Chris Meisinger, Adam Lange, Stefan Becker, Markus Zweckstetter

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact, top 92% 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

1 citing paper in PubMed, 4 citations in OpenAlex.

  1. 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

10 authors at 3 institutions in 1 country.

Xuejun YaoMax Planck Institute for Biophysical Chemistry, Göttingen, Germany.
Ulrich H N DürrMax Planck Institute for Biophysical Chemistry, Göttingen, Germany.
Zrinka GattinMax Planck Institute for Biophysical Chemistry, Göttingen, Germany.
Yvonne LaukatMax Planck Institute for Biophysical Chemistry, Göttingen, Germany.
Rhagavendran L NarayananMax Planck Institute for Biophysical Chemistry, Göttingen, Germany.
Ann-Kathrin BrücknerMax Planck Institute for Biophysical Chemistry, Göttingen, Germany.
Chris MeisingerInstitut für Biochemie und Molekularbiologie, ZBMZ and BIOSS Centre for Biological Signalling Studies, Universität Freiburg, Freiburg, Germany.
Adam LangeMax Planck Institute for Biophysical Chemistry, Göttingen, Germany.
Stefan BeckerMax Planck Institute for Biophysical Chemistry, Göttingen, Germany.
Markus ZweckstetterMax Planck Institute for Biophysical Chemistry, Göttingen, Germany; German Center for Neurodegenerative Diseases (DZNE), Goöttingen, Germany; Center for Nanoscale Microscopy and Molecular Physiology of the Brain (CNMPB), University Medical Center, Göttingen, Germany.
Max Planck Institute for Biophysical Chemistry · DENanoscale Microscopy and Molecular Physiology of the Brain Cluster of Excellence 171 — DFG Research Center 103 · DEUniversity of Freiburg · DE

Funding

European Research Council 282008
6 · The paper itself

Abstract

Membrane proteins play key roles in biology. Determination of their structure in a membrane environment, however, is highly challenging. To address this challenge, we developed an approach that couples hydrogen/deuterium exchange of membrane proteins to rapid unfolding and detection by solution-state NMR spectroscopy. We show that the method allows analysis of the solvent protection of single residues in liposome-embedded proteins such as the 349-residue Tom40, the major protein translocation pore in the outer mitochondrial membrane, which has resisted structural analysis for many years.

Indexed as

Protein UnfoldingDeuterium Exchange MeasurementFungal ProteinsLiposomesMembrane ProteinsMitochondrial ProteinsNeurospora crassaNuclear Magnetic Resonance, BiomolecularFungal ProteinsLiposomesMembrane ProteinsMitochondrial Proteins

Identifiers

PMID25375235
PMCPMC4223039
OpenAlexW2025370110

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.