Evidence map›Paper›PMID 42156693›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2026

Solid-State NMR Approaches to Study Protein Structure and Protein-Lipid Interactions.

Christopher Aisenbrey, Evgeniy S Salnikov, Jesus Raya, Matthias Michalek, Burkhard Bechinger

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Article in Methods in molecular biology (Clifton, N.J.), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
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0citing papers in PubMed
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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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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.

Christopher AisenbreyInstitut de Chimie, CNRS, Université de Strasbourg, UMR 7177, 4, Rue Blaise Pascal,, 67070, Strasbourg, France.
Evgeniy S SalnikovInstitut de Chimie, CNRS, Université de Strasbourg, UMR 7177, 4, Rue Blaise Pascal,, 67070, Strasbourg, France.
Jesus RayaInstitut de Chimie, CNRS, Université de Strasbourg, UMR 7177, 4, Rue Blaise Pascal,, 67070, Strasbourg, France.
Matthias MichalekInstitut de Chimie, CNRS, Université de Strasbourg, UMR 7177, 4, Rue Blaise Pascal,, 67070, Strasbourg, France.
Burkhard BechingerInstitut de Chimie, CNRS, Université de Strasbourg, UMR 7177, 4, Rue Blaise Pascal,, 67070, Strasbourg, France. bechinge@unistra.fr.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Solid-state NMR spectroscopy has been developed for the investigation of membrane-associated polypeptides and remains one of the few techniques to reveal high-resolution structural information in liquid-disordered phospholipid bilayers. While magic angle spinning solid-state NMR remains a popular approach yielding spectra that resemble those in solution, the investigation of static, uniaxially oriented samples provides an alternative concept that has been used to investigate the structure, dynamics, and topology of membrane polypeptides. Much of the previous solid-state NMR work has been developed and performed on peptides, but the technique is constantly expanding toward larger membrane proteins. Here, a number of protocols are presented describing, among others, the reconstitution of membrane proteins into oriented membranes, monitoring membrane alignment by

Indexed as

Membrane ProteinsNuclear Magnetic Resonance, BiomolecularLipid BilayersMagnetic Resonance SpectroscopyPhospholipidsProtein ConformationLipid BilayersMembrane ProteinsPhospholipidsBicelleChannelCross polarizationDetergentHelix topologyLee–Goldburg decouplingMembrane protein structureMembrane reconstitutionOriented bilayerPISEMAProtein insertionSeparated local field spectroscopySurface alignmentTransmembrane orientation

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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.