Evidence map›Paper›PMID 20923654›Full record

ArticleBiophysical journal2010

Coupling of retinal, protein, and water dynamics in squid rhodopsin.

Eduardo Jardón-Valadez, Ana-Nicoleta Bondar, Douglas J Tobias

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.2field-weighted citation impact, top 25% 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

12 citing papers in PubMed, 35 citations in OpenAlex.

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  12. Water pathways in the bacteriorhodopsin proton pump.The Journal of membrane biology · 2011
    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 at 1 institution in 1 country.

Eduardo Jardón-ValadezDepartment of Chemistry, University of California, Irvine, CA, USA.
Ana-Nicoleta Bondar
Douglas J Tobias
University of California, Irvine · US

Funding

Membrane Protein Folding and AssemblyR01GM074637 · NIGMS · UNIVERSITY OF CALIFORNIA-IRVINE · PI WHITE, STEPHEN H. · 2006 to 2020
$4.5M
Concerted membrane diffraction and simulation studiesR01GM068002 · NIGMS · UNIVERSITY OF CALIFORNIA-IRVINE · PI WHITE, STEPHEN H. · 2003 to 2006
$989k
NIGMS NIH HHS GM68002NIGMS NIH HHS GM74637NIGMS NIH HHS R01 GM068002NIGMS NIH HHS R01 GM074637
6 · The paper itself

Abstract

The light-induced isomerization of the retinal from 11-cis to all-trans triggers changes in the conformation of visual rhodopsins that lead to the formation of the activated state, which is ready to interact with the G protein. To begin to understand how changes in the structure and dynamics of the retinal are transmitted to the protein, we performed molecular dynamics simulations of squid rhodopsin with 11-cis and all-trans retinal, and with two different force fields for describing the retinal molecule. The results indicate that structural rearrangements in the binding pocket, albeit small, propagate toward the cytoplasmic side of the protein, and affect the dynamics of internal water molecules. The sensitivity of the active-site interactions on the retinal force-field parameters highlights the coupling between the retinal molecule and its immediate protein environment.

Indexed as

AnimalsBinding SitesComputer SimulationDarknessDecapodiformesHydrogen BondingModels, MolecularRetinaldehydeRhodopsinTime FactorsWaterRetinaldehydeRhodopsinWater

Identifiers

PMID20923654
PMCPMC3042571
OpenAlexW2027529456

What OpenQuestion holds

Textmetadata
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.