Evidence map›Paper›PMID 24034903›Full record

ReviewCurrent opinion in structural biology2013

Solid state NMR and protein-protein interactions in membranes.

Yimin Miao, Timothy A Cross

Open access · greenAbstract readReview
In one paragraph

Review in Current opinion in structural biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.2field-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

17 citing papers in PubMed, 40 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Journal of magnetic resonance (San Diego, Calif. : 1997) · 2017
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Drugging Membrane Protein Interactions.Annual review of biomedical engineering · 2016
    Review
  13. Review
  14. Article
  15. Article
  16. Article
  17. Structural studies of proteins by paramagnetic solid-state NMR spectroscopy.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2015
    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.

Yimin MiaoDepartment of Chemistry and Biochemistry, Florida State University, Tallahassee, FL 32306, United States; National High Magnetic Field Lab, 1800 E. Paul Dirac Dr., Florida State University, Tallahassee, FL 32310, United States.
Timothy A Cross
Florida State University · US

Funding

Target IdentificationP01AI074805 · NIAID · FLORIDA STATE UNIVERSITY · PI CROSS, TIMOTHY A · 2009 to 2013
$8.7M
DYNAMIC AND STRUCTURAL ELUCIDATION OF GRAMICIDIN A'R01AI023007 · NIAID · FLORIDA STATE UNIVERSITY · PI CROSS, TIMOTHY A · 1987 to 2014
$5.1M
Four Mtb Membrane Proteins: Structure and FunctionR01AI073891 · NIAID · FLORIDA STATE UNIVERSITY · PI CROSS, TIMOTHY A · 2008 to 2012
$2.0M
NIAID NIH HHS AI 023007NIAID NIH HHS AI 073891NIAID NIH HHS AI 074805NIAID NIH HHS P01 AI074805NIAID NIH HHS R01 AI023007NIAID NIH HHS R01 AI073891
6 · The paper itself

Abstract

Solid state NMR spectroscopy has evolved rapidly in recent years into an excellent tool for the characterization of membrane proteins and their complexes. In the past few years it has also become clear that the structure of membrane proteins, especially helical membrane proteins is determined, in part, by the membrane environment. Therefore, the modeling of this environment by a liquid crystalline lipid bilayer for solid state NMR has generated a unique tool for the characterization of native conformational states, local and global dynamics, and high-resolution structure for these proteins. Protein-protein interactions can also benefit from this solid state NMR capability to characterize membrane proteins in a native-like environment. These complexes take the form of oligomeric structures and hetero-protein interactions both with water-soluble proteins and other membrane proteins.

Indexed as

HumansMagnetic Resonance SpectroscopyMembrane ProteinsProtein Interaction MappingMembrane Proteins

Identifiers

PMID24034903
PMCPMC3855169
OpenAlexW2091182425

What OpenQuestion holds

Textmetadata
LicenceTDM
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.