Evidence map›Paper›PMID 21774553›Full record

ArticleJournal of the American Chemical Society2011

In situ structural characterization of a recombinant protein in native Escherichia coli membranes with solid-state magic-angle-spinning NMR.

Riqiang Fu, Xingsheng Wang, Conggang Li, Adriana N Santiago-Miranda, Gary J Pielak, Fang Tian

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
4.0field-weighted citation impact, top 5% 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

34 citing papers in PubMed, 95 citations in OpenAlex.

  1. Review
  2. Article
  3. bioRxiv : the preprint server for biology · 2025
    Article
  4. Solid-state NMR of membrane proteins in situ.Current opinion in structural biology · 2025
    Review
  5. Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  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. Article
  14. Review
  15. Article
  16. Review
  17. Membrane proteins in their native habitat as seen by solid-state NMR spectroscopy.Protein science : a publication of the Protein Society · 2015
    Review
  18. Article
  19. Article
  20. 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

6 authors at 5 institutions in 3 countries.

Riqiang FuNational High Magnetic Field Laboratory, Tallahassee, Florida 32310, United States.
Xingsheng Wang
Conggang Li
Adriana N Santiago-Miranda
Gary J Pielak
Fang Tian
Pennsylvania State University · USChinese Academy of Sciences · CNNational High Magnetic Field Laboratory · USUniversity of North Carolina at Chapel Hill · USUniversity of Puerto Rico-Mayaguez · PR

Funding

NIH Director's Pioneer AwardDP1OD000783 · OD · UNIV OF NORTH CAROLINA CHAPEL HILL · PI PIELAK, GARY JOSEPH · 2006 to 2010
$3.7M
Structure and Dynamics of Membrane Proteins from NMR Orientational ConstraintsR01GM081793 · NIGMS · UNIVERSITY OF SOUTH CAROLINA AT COLUMBIA · PI VALAFAR, HOMAYOUN · 2007 to 2010
$915k
NIGMS NIH HHS 5R01GM081793-03NIGMS NIH HHS R01 GM081793NIH HHS 5DP1OD783NIH HHS DP1 OD000783
6 · The paper itself

Abstract

The feasibility of using solid-state magic-angle-spinning NMR spectroscopy for in situ structural characterization of the LR11 (sorLA) transmembrane domain (TM) in native Escherichia coli membranes is presented. LR11 interacts with the human amyloid precursor protein (APP), a central player in the pathology of Alzheimer's disease. The background signals from E. coli lipids and membrane proteins had only minor effects on the LR11 TM resonances. Approximately 50% of the LR11 TM residues were assigned by using (13)C PARIS data. These assignments allowed comparisons of the secondary structure of the LR11 TM in native membrane environments and commonly used membrane mimics (e.g., micelles). In situ spectroscopy bypasses several obstacles in the preparation of membrane proteins for structural analysis and offers the opportunity to investigate how membrane heterogeneity, bilayer asymmetry, chemical gradients, and macromolecular crowding affect the protein structure.

Indexed as

Escherichia coliHumansLDL-Receptor Related ProteinsMembrane Transport ProteinsNuclear Magnetic Resonance, BiomolecularProtein ConformationRecombinant Fusion ProteinsLDL-Receptor Related ProteinsMembrane Transport ProteinsRecombinant Fusion ProteinsSORL1 protein, human

Identifiers

PMID21774553
PMCPMC3154996
OpenAlexW2054231753

What OpenQuestion holds

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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.