Evidence map›Paper›PMID 21851809›Full record

ReviewBiochimica et biophysica acta2012

Molecular simulations and solid-state NMR investigate dynamical structure in rhodopsin activation.

Blake Mertz, Andrey V Struts, Scott E Feller, Michael F Brown

Open access · greenAbstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2012. 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
1.6field-weighted citation impact, top 17% 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, 36 citations in OpenAlex.

  1. Article
  2. Coordination of bilayer properties by an inward-rectifier KJournal of structural biology: X · 2024
    Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Synthesis of 9-CDTetrahedron letters · 2018
    Article
  8. The G protein-coupled receptor rhodopsin: a historical perspective.Methods in molecular biology (Clifton, N.J.) · 2015
    Article
  9. Review
  10. Article
  11. Review
  12. Article
  13. 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

4 authors at 2 institutions in 2 countries.

Blake MertzDepartment of Chemistry and Biochemistry, University of Arizona, Tucson, AZ 85721, USA.
Andrey V Struts
Scott E Feller
Michael F Brown
University of Arizona · USWabash College · US

Funding

MEMBRANE BASIS OF VISUAL EXCITATIONR01EY012049 · NEI · UNIVERSITY OF ARIZONA · PI BROWN, MICHAEL F · 1998 to 2012
$3.3M
LIPID MODULATION OF RHODOPSIN SIGNALING IN MEMBRANESR01EY018891 · NEI · UNIVERSITY OF ARIZONA · PI BROWN, MICHAEL F · 2008 to 2010
$1.1M
Biophysical and Computational Investigation of the Rhodopsin Activation MechanismF32EY019614 · NEI · UNIVERSITY OF ARIZONA · PI MERTZ, BLAKE · 2009 to 2011
$141k
NEI NIH HHS EY012049NEI NIH HHS EY018891NEI NIH HHS EY019614NEI NIH HHS F32 EY019614NEI NIH HHS R01 EY012049NEI NIH HHS R01 EY018891
6 · The paper itself

Abstract

Rhodopsin has served as the primary model for studying G protein-coupled receptors (GPCRs)-the largest group in the human genome, and consequently a primary target for pharmaceutical development. Understanding the functions and activation mechanisms of GPCRs has proven to be extraordinarily difficult, as they are part of a complex signaling cascade and reside within the cell membrane. Although X-ray crystallography has recently solved several GPCR structures that may resemble the activated conformation, the dynamics and mechanism of rhodopsin activation continue to remain elusive. Notably solid-state ((2))H NMR spectroscopy provides key information pertinent to how local dynamics of the retinal ligand change during rhodopsin activation. When combined with molecular mechanics simulations of proteolipid membranes, a new paradigm for the rhodopsin activation process emerges. Experiment and simulation both suggest that retinal isomerization initiates the rhodopsin photocascade to yield not a single activated structure, but rather an ensemble of activated conformational states. This article is part of a Special Issue entitled: Membrane protein structure and function.

Indexed as

Molecular Dynamics SimulationCell MembraneHumansMagnetic Resonance SpectroscopyProtein ConformationRhodopsinRhodopsin

Identifiers

PMID21851809
PMCPMC5270601
OpenAlexW2072342394

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.