Evidence map›Paper›PMID 20423327›Full record

ReviewThe Biochemical journal2010

Complexes between photoactivated rhodopsin and transducin: progress and questions.

Beata Jastrzebska, Yaroslav Tsybovsky, Krzysztof Palczewski

Open access · greenAbstract readReview
In one paragraph

Review in The Biochemical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
3.2field-weighted citation impact, top 7% 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

24 citing papers in PubMed, 43 citations in OpenAlex.

  1. Role of VLC-PUFAs in Retinal and Macular Degeneration.Advances in experimental medicine and biology · 2023
    Article
  2. Rhodopsin as a Molecular Target to Mitigate Retinitis Pigmentosa.Advances in experimental medicine and biology · 2022
    Review
  3. Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Chemistry and biology of the initial steps in vision: the Friedenwald lecture.Investigative ophthalmology & visual science · 2014
    Article
  9. Retinal phototransduction.Neurosciences (Riyadh, Saudi Arabia) · 2014
    Review
  10. Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. Structure and activation of rhodopsin.Acta pharmacologica Sinica · 2012
    Review
  16. Article
  17. G protein-coupled receptors--recent advances.Acta biochimica Polonica · 2012
    Review
  18. Article
  19. Review
  20. 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.

Beata JastrzebskaDepartment of Pharmacology, School of Medicine, Case Western Reserve University, Cleveland, OH 44106-4965, USA. bxj27@case.edu
Yaroslav Tsybovsky
Krzysztof Palczewski
Case Western Reserve University · US

Funding

REGULATION OF RHODOPSIN KINASE AND GUANYLATE CYCLASER01EY008061 · NEI · UNIVERSITY OF WASHINGTON · PI PALCZEWSKI, KRZYSZTOF · 1994 to 2014
$9.5M
STRUCTURAL STUDIES OF G PROTEIN-COUPLED RECEPTORSR01GM079191 · NIGMS · CASE WESTERN RESERVE UNIVERSITY · PI PALCZEWSKI, KRZYSZTOF · 2007 to 2010
$845k
NEI NIH HHS R01-EY0008061NEI NIH HHS R01 EY008061NIGMS NIH HHS GM079191NIGMS NIH HHS R01 GM079191
6 · The paper itself

Abstract

Activation of GPCRs (G-protein-coupled receptors) leads to conformational changes that ultimately initiate signal transduction. Activated GPCRs transiently combine with and activate heterotrimeric G-proteins resulting in GTP replacement of GDP on the G-protein alpha subunit. Both the detailed structural changes essential for productive GDP/GTP exchange on the G-protein alpha subunit and the structure of the GPCR-G-protein complex itself have yet to be elucidated. Nevertheless, transient GPCR-G-protein complexes can be trapped by nucleotide depletion, yielding an empty-nucleotide G-protein-GPCR complex that can be isolated. Whereas early biochemical studies indicated formation of a complex between G-protein and activated receptor only, more recent results suggest that G-protein can bind to pre-activated states of receptor or even couple transiently to non-activated receptor to facilitate rapid responses to stimuli. Efficient and reproducible formation of physiologically relevant, conformationally homogenous GPCR-G-protein complexes is a prerequisite for structural studies designed to address these possibilities.

Indexed as

AnimalsHeterotrimeric GTP-Binding ProteinsHumansModels, BiologicalReceptors, G-Protein-CoupledRhodopsinSignal TransductionTransducinHeterotrimeric GTP-Binding ProteinsReceptors, G-Protein-CoupledRhodopsinTransducin

Identifiers

PMID20423327
PMCPMC2875673
OpenAlexW2146699663

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.