Evidence map›Paper›PMID 42156694›Full record

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

Solution NMR Spectroscopy for the Determination of Structures of Membrane Proteins in a Lipid Environment.

Roumya Pandey, Ashish Arora

Abstract read
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In one paragraph

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
0cells of the map it votes in
0citing 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

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

2 authors.

Roumya PandeyBiochemistry and Structural Biology Division, CSIR-Central Drug Research Institute, Lucknow, India.
Ashish AroraBiochemistry and Structural Biology Division, CSIR-Central Drug Research Institute, Lucknow, India. ashish.arora.cdri@csir.res.in.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

NMR spectroscopy has substantially benefited from the recent technical advances to maintain its position as an eminent technique for the characterization of the solution structures and dynamics of membrane proteins at the level of atomic resolution. NMR offers a combination of several versatile strategies, for example, choice of molecular assemblies, like micelles, bicelles, and nanodiscs, with appropriate deuterated or non-deuterated detergents and phospholipids; temperature, and ionic strength; isotope labeling with

Indexed as

Membrane ProteinsNuclear Magnetic Resonance, BiomolecularIsotope LabelingMagnetic Resonance SpectroscopyMicellesProtein ConformationSolutionsMembrane ProteinsMicellesSolutionsDetergent micellesDynamicsMembrane proteinsProtein structuresSolution NMRα-helical bundlesβ-barrels

Identifiers

PMID42156694

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.