Evidence map›Paper›PMID 18077356›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2007

Sequence of late molecular events in the activation of rhodopsin.

Bernhard Knierim, Klaus Peter Hofmann, Oliver P Ernst, Wayne L Hubbell

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.

0numbers the graph read from it
0cells of the map it votes in
72citing papers in PubMed
17.5field-weighted citation impact, top 1% 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

72 citing papers in PubMed, 134 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Structural aspects of rod opsin and their implication in genetic diseases.Pflugers Archiv : European journal of physiology · 2021
    Review
  6. Review
  7. Capturing Peptide-GPCR Interactions and Their Dynamics.Molecules (Basel, Switzerland) · 2020
    Review
  8. Article
  9. Article
  10. Stepwise activation of a class C GPCR begins with millisecond dimer rearrangement.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  11. Article
  12. Article
  13. Article
  14. Conformational equilibria of light-activated rhodopsin in nanodiscs.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. A Usual G-Protein-Coupled Receptor in Unusual Membranes.Angewandte Chemie (International ed. in English) · 2016
    Article
  20. Article

12 more citing papers are in PubMed but not listed here.

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.

Bernhard KnierimInstitut für Medizinische Physik und Biophysik, Charité Universitätsmedizin Berlin, Charitéplatz 1, D-10117 Berlin, Germany.
Klaus Peter Hofmann
Oliver P Ernst
Wayne L Hubbell
Charité - Universitätsmedizin Berlin · DEDoheny Eye Institute · US

Funding

MOLECULAR BASIS OF MEMBRANE EXCITATIONR01EY005216 · NEI · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI HUBBELL, WAYNE L · 1985 to 2019
$9.8M
MOLECULAR BASIS OF MEMBRANE EXCITATIONR37EY005216 · NEI · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI HUBBELL, WAYNE L · 1990 to 1999
–
NEI NIH HHS EY05216NEI NIH HHS R01 EY005216NEI NIH HHS R37 EY005216
6 · The paper itself

Abstract

Activation of the G protein-coupled receptor rhodopsin involves both the motion of transmembrane helix 6 (TM6) and proton exchange events. To study how these activation steps relate to each other, spin-labeled rhodopsin in solutions of dodecyl maltoside was used so that time-resolved TM6 motion and proton exchange could each be monitored as a function of pH and temperature after an activating light flash. The results reveal that the motion of TM6 is not synchronized with deprotonation of the Schiff base that binds the chromophore to the protein but is an order of magnitude slower at 30 degrees C. However, TM6 motion and the uptake of a proton from solution in the neutral pH range follow the same time course. Importantly, the motion of TM6 is virtually independent of pH, as is Schiff base deprotonation under the conditions used, whereas proton uptake titrates with a pK of 6.5. This finding shows that proton uptake is a consequence rather than a cause of helix motion. Activated rhodopsin binds to and subsequently activates the cognate G protein, transducin. It has been shown that peptides derived from the C terminus of the transducin alpha-subunit mimic in part binding of the intact G protein. These peptides are found to bind to rhodopsin after TM6 movement, resulting in the release of protons. Collectively, the data suggest the following temporal sequence of events involved in activation: (i) internal Schiff base proton transfer; (ii) TM6 movement; and (iii) proton uptake from solution and binding of transducin.

Indexed as

AnimalsCattleChlorocebus aethiopsCOS CellsKineticsPeptidesProtein Structure, SecondaryProtonsReceptors, G-Protein-CoupledRhodopsinTemperaturePeptidesProtonsReceptors, G-Protein-CoupledRhodopsin

Identifiers

PMID18077356
PMCPMC2154424
OpenAlexW2024847911

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.