Evidence map›Paper›PMID 25032938›Full record

ReviewQuarterly reviews of biophysics2014

NMR structures of membrane proteins in phospholipid bilayers.

Jasmina Radoicic, George J Lu, Stanley J Opella

Abstract readReview
In one paragraph

Review in Quarterly reviews of biophysics, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing 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

16 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Applications of In-Cell NMR in Structural Biology and Drug Discovery.International journal of molecular sciences · 2019
    Review
  8. Article
  9. Article
  10. Article
  11. Targeting the Channel Activity of Viroporins.Advances in protein chemistry and structural biology · 2016
    Review
  12. Review
  13. Article
  14. Solid-state NMR and membrane proteins.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2015
    Article
  15. Article
  16. 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.

Jasmina RadoicicDepartment of Chemistry and Biochemistry,University of California,San Diego, La Jolla, CA 92093,USA.
George J LuDepartment of Chemistry and Biochemistry,University of California,San Diego, La Jolla, CA 92093,USA.
Stanley J OpellaDepartment of Chemistry and Biochemistry,University of California,San Diego, La Jolla, CA 92093,USA.

Funding

RESOURCE FOR SOLID STATE NMR OF PROTEINSP41EB002031 · NIBIB · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI OPELLA, STANLEY J · 2003 to 2018
$16.3M
Molecular Imaging of G-Protein-Coupled Receptors for Drug DevelopmentR01EB005161 · NIBIB · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI OPELLA, STANLEY J · 2006 to 2014
$6.8M
Structure, Dynamics, and Functions of the Viroporins Vpu from HIV and p7 from HCVR01GM066978 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI OPELLA, STANLEY J · 2003 to 2016
$3.5M
Structure Determination of Membrane Proteins in Phospholipid BilyaersR01GM099986 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI OPELLA, STANLEY J · 2012 to 2015
$1.1M
NIBIB NIH HHS P41 EB002031NIBIB NIH HHS P41EB002031NIBIB NIH HHS R01 EB005161NIBIB NIH HHS R01EB005161NIGMS NIH HHS R01 GM066978NIGMS NIH HHS R01GM066978NIGMS NIH HHS R01 GM099986NIGMS NIH HHS R01GM099986
6 · The paper itself

Abstract

Membrane proteins have always presented technical challenges for structural studies because of their requirement for a lipid environment. Multiple approaches exist including X-ray crystallography and electron microscopy that can give significant insights into their structure and function. However, nuclear magnetic resonance (NMR) is unique in that it offers the possibility of determining the structures of unmodified membrane proteins in their native environment of phospholipid bilayers under physiological conditions. Furthermore, NMR enables the characterization of the structure and dynamics of backbone and side chain sites of the proteins alone and in complexes with both small molecules and other biopolymers. The learning curve has been steep for the field as most initial studies were performed under non-native environments using modified proteins until ultimately progress in both techniques and instrumentation led to the possibility of examining unmodified membrane proteins in phospholipid bilayers under physiological conditions. This review aims to provide an overview of the development and application of NMR to membrane proteins. It highlights some of the most significant structural milestones that have been reached by NMR spectroscopy of membrane proteins, especially those accomplished with the proteins in phospholipid bilayer environments where they function.

Indexed as

PhospholipidsAnimalsCell MembraneHumansLipid BilayersMagnetic Resonance SpectroscopyMembrane ProteinsLipid BilayersMembrane ProteinsPhospholipids

Identifiers

PMID25032938
PMCPMC4153756

What OpenQuestion holds

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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.