Evidence map›Paper›PMID 25973959›Full record

ReviewProtein science : a publication of the Protein Society2015

Membrane proteins in their native habitat as seen by solid-state NMR spectroscopy.

Leonid S Brown, Vladimir Ladizhansky

Open access · bronzeAbstract readReview
In one paragraph

Review in Protein science : a publication of the Protein Society, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
5.1field-weighted citation impact, top 4% 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

29 citing papers in PubMed, 56 citations in OpenAlex.

  1. Article
  2. bioRxiv : the preprint server for biology · 2025
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  12. De novo resonance assignment of the transmembrane domain of LR11/SorLA in E. coli membranes.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2020
    Article
  13. Review
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  16. Article
  17. Formation of pH-Resistant Monodispersed Polymer-Lipid Nanodiscs.Angewandte Chemie (International ed. in English) · 2018
    Article
  18. Article
  19. Article
  20. Bioinspired, Size-Tunable Self-Assembly of Polymer-Lipid Bilayer Nanodiscs.Angewandte Chemie (International ed. in English) · 2017
    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

2 authors at 1 institution in 1 country.

Leonid S BrownDepartment of Physics and Biophysics Interdepartmental Group, University of Guelph, Guelph, Ontario, Canada, N1G 2W1.
Vladimir LadizhanskyDepartment of Physics and Biophysics Interdepartmental Group, University of Guelph, Guelph, Ontario, Canada, N1G 2W1.
University of Guelph · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Membrane proteins play many critical roles in cells, mediating flow of material and information across cell membranes. They have evolved to perform these functions in the environment of a cell membrane, whose physicochemical properties are often different from those of common cell membrane mimetics used for structure determination. As a result, membrane proteins are difficult to study by traditional methods of structural biology, and they are significantly underrepresented in the protein structure databank. Solid-state Nuclear Magnetic Resonance (SSNMR) has long been considered as an attractive alternative because it allows for studies of membrane proteins in both native-like membranes composed of synthetic lipids and in cell membranes. Over the past decade, SSNMR has been rapidly developing into a major structural method, and a growing number of membrane protein structures obtained by this technique highlights its potential. Here we discuss membrane protein sample requirements, review recent progress in SSNMR methodologies, and describe recent advances in characterizing membrane proteins in the environment of a cellular membrane.

Indexed as

Cell MembraneHumansLipid BilayersMembrane ProteinsModels, MolecularNuclear Magnetic Resonance, BiomolecularProtein Structure, SecondaryLipid BilayersMembrane Proteinscell membranelipid bilayermembrane proteinprotein structuresolid-state NMR

Identifiers

PMID25973959
PMCPMC4570529
OpenAlexW1509410086

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.