Evidence map›Paper›PMID 33198410›Full record

ReviewBiology2020

Membrane Protein Structure Determination and Characterisation by Solution and Solid-State NMR.

Vivien Yeh, Alice Goode, Boyan B Bonev

Open access · goldAbstract readReview
In one paragraph

Review in Biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

15 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Review
  7. Article
  8. Conformation of influenza AM2 membrane protein in nanodiscs and liposomes.Biochimica et biophysica acta. Biomembranes · 2023
    Article
  9. Article
  10. Review
  11. The high-throughput production of membrane proteins.Emerging topics in life sciences · 2021
    Article
  12. Review
  13. Interactions of Amyloid-β with Membrane Proteins.International journal of molecular sciences · 2021
    Review
  14. Article
  15. 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

3 authors at 1 institution in 1 country.

Vivien YehSchool of Life Sciences, University of Nottingham, Nottingham NG7 2UH, UK.ORCID 0000-0003-2232-2329
Alice GoodeSchool of Life Sciences, University of Nottingham, Nottingham NG7 2UH, UK.ORCID 0000-0003-1678-6952
Boyan B BonevSchool of Life Sciences, University of Nottingham, Nottingham NG7 2UH, UK.ORCID 0000-0001-7156-2412
University of Nottingham · GB

Funding

Biotechnology and Biological Sciences Research Council BB/N010426/1Medical Research Council MR/N010477/1
6 · The paper itself

Abstract

Biological membranes define the interface of life and its basic unit, the cell. Membrane proteins play key roles in membrane functions, yet their structure and mechanisms remain poorly understood. Breakthroughs in crystallography and electron microscopy have invigorated structural analysis while failing to characterise key functional interactions with lipids, small molecules and membrane modulators, as well as their conformational polymorphism and dynamics. NMR is uniquely suited to resolving atomic environments within complex molecular assemblies and reporting on membrane organisation, protein structure, lipid and polysaccharide composition, conformational variations and molecular interactions. The main challenge in membrane protein studies at the atomic level remains the need for a membrane environment to support their fold. NMR studies in membrane mimetics and membranes of increasing complexity offer close to native environments for structural and molecular studies of membrane proteins. Solution NMR inherits high resolution from small molecule analysis, providing insights from detergent solubilised proteins and small molecular assemblies. Solid-state NMR achieves high resolution in membrane samples through fast sample spinning or sample alignment. Recent developments in dynamic nuclear polarisation NMR allow signal enhancement by orders of magnitude opening new opportunities for expanding the applications of NMR to studies of native membranes and whole cells.

Indexed as

dynamic nuclear polarisationmembrane proteinsolid-state NMRsolution NMR

Identifiers

PMID33198410
PMCPMC7697852
OpenAlexW3101183352

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.