Evidence map›Paper›PMID 23721747›Full record

ReviewCurrent opinion in structural biology2013

Advances in NMR structures of integral membrane proteins.

Innokentiy Maslennikov, Senyon Choe

Abstract 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 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing 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

13 citing papers in PubMed.

  1. Article
  2. Article
  3. Applications of NMR to membrane proteins.Archives of biochemistry and biophysics · 2017
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Membrane proteins in their native habitat as seen by solid-state NMR spectroscopy.Protein science : a publication of the Protein Society · 2015
    Review
  9. Article
  10. Oncogenic and RASopathy-associated K-RAS mutations relieve membrane-dependent occlusion of the effector-binding site.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  11. Review
  12. Time-shared experiments for efficient assignment of triple-selectively labeled proteins.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2014
    Article
  13. 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.

Innokentiy MaslennikovStructural Biology Laboratory, Salk Institute, La Jolla, CA 92037, USA.
Senyon Choe

Funding

High-speed NMR methods for membrane protein analysisR01GM098630 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI CHOE, SENYON · 2011 to 2014
$1.4M
Cell-free expression of human integral membrane proteins for structural studiesR01GM095623 · NIGMS · SALK INSTITUTE FOR BIOLOGICAL STUDIES · PI CHOE, SENYON · 2010 to 2013
$1.2M
NIGMS NIH HHS GM095623NIGMS NIH HHS GM098630NIGMS NIH HHS R01 GM095623NIGMS NIH HHS R01 GM098630
6 · The paper itself

Abstract

Integral membrane proteins (IMPs) play a central role in cell communication with the environment. Their structures are essential for our understanding of the molecular mechanisms of signaling and for drug design, yet they remain badly underrepresented in the protein structure databank. Solution NMR is, aside from X-ray crystallography, the major tool in structural biology. Here we review recently reported solution NMR structures of polytopic IMPs and discuss the new approaches, which were developed in the course of these studies to overcome barriers in the field. Advances in cell-free protein expression, combinatorial isotope labeling, resonance assignment, and collection of structural data greatly accelerated IMP structure determination by solution NMR. In addition, novel membrane-mimicking media made possible determination of solution NMR structures of IMPs in a native-like lipid environment.

Indexed as

Cell CommunicationHumansMembrane ProteinsNuclear Magnetic Resonance, BiomolecularProtein Structure, TertiarySignal TransductionMembrane Proteins

Identifiers

PMID23721747
PMCPMC3737378

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.