Evidence map›Paper›PMID 25185540›Full record

ArticleBiophysical journal2014

Explicit spatiotemporal simulation of receptor-G protein coupling in rod cell disk membranes.

Johannes Schöneberg, Martin Heck, Klaus Peter Hofmann, Frank Noé

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2014. 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
2.7field-weighted citation impact, top 10% 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, 39 citations in OpenAlex.

  1. Supramolecular organization of rhodopsin in rod photoreceptor cell membranes.Pflugers Archiv : European journal of physiology · 2021
    Review
  2. Article
  3. Rhodopsin Oligomerization and Aggregation.The Journal of membrane biology · 2019
    Review
  4. Article
  5. Article
  6. Article
  7. Reaction-diffusion basis of retroviral infectivity.Philosophical transactions. Series A, Mathematical, physical, and engineering sciences · 2016
    Article
  8. Molecular basis for photoreceptor outer segment architecture.Progress in retinal and eye research · 2016
    Review
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 2 institutions in 1 country.

Johannes SchönebergDepartment of Mathematics, Computer Science and Bioinformatics, Freie Universität Berlin, Berlin, Germany.
Martin HeckInstitut für Medizinische Physik und Biophysik, Charité, Universitätsmedizin Berlin, Berlin, Germany. Electronic address: martin.heck@charite.de.
Klaus Peter HofmannInstitut für Medizinische Physik und Biophysik, Charité, Universitätsmedizin Berlin, Berlin, Germany.
Frank NoéDepartment of Mathematics, Computer Science and Bioinformatics, Freie Universität Berlin, Berlin, Germany. Electronic address: frank.noe@fu-berlin.de.
Charité - Universitätsmedizin Berlin · DEFreie Universität Berlin · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Dim-light vision is mediated by retinal rod cells. Rhodopsin (R), a G-protein-coupled receptor, switches to its active form (R(∗)) in response to absorbing a single photon and activates multiple copies of the G-protein transducin (G) that trigger further downstream reactions of the phototransduction cascade. The classical assumption is that R and G are uniformly distributed and freely diffusing on disk membranes. Recent experimental findings have challenged this view by showing specific R architectures, including RG precomplexes, nonuniform R density, specific R arrangements, and immobile fractions of R. Here, we derive a physical model that describes the first steps of the photoactivation cascade in spatiotemporal detail and single-molecule resolution. The model was implemented in the ReaDDy software for particle-based reaction-diffusion simulations. Detailed kinetic in vitro experiments are used to parametrize the reaction rates and diffusion constants of R and G. Particle diffusion and G activation are then studied under different conditions of R-R interaction. It is found that the classical free-diffusion model is consistent with the available kinetic data. The existence of precomplexes between inactive R and G is only consistent with the data if these precomplexes are weak, with much larger dissociation rates than suggested elsewhere. Microarchitectures of R, such as dimer racks, would effectively immobilize R but have little impact on the diffusivity of G and on the overall amplification of the cascade at the level of the G protein.

Indexed as

Computer SimulationDiffusionKineticsModels, MolecularPhotochemical ProcessesRetinal Rod Photoreceptor CellsRhodopsinSoftwareTransducinVideo RecordingRhodopsinTransducin

Identifiers

PMID25185540
PMCPMC4156778
OpenAlexW1984336745

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.