Evidence map›Paper›PMID 18456304›Full record

ReviewVision research2008

Signal transducing membrane complexes of photoreceptor outer segments.

Theodore G Wensel

Abstract readReview
In one paragraph

Review in Vision research, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.

0numbers the graph read from it
0cells of the map it votes in
66citing papers in PubMed
5.7field-weighted citation impact, top 3% 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

66 citing papers in PubMed, 112 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. Review
  11. Review
  12. Calcium flares and compartmentalization in rod photoreceptors.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Molecular basis for photoreceptor outer segment architecture.Progress in retinal and eye research · 2016
    Review
  20. Retinal remodeling in human retinitis pigmentosa.Experimental eye research · 2016
    Review

6 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

1 author at 1 institution in 1 country.

Theodore G WenselVerna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, USA. twensel@bcm.tmc.edu
Baylor College of Medicine · US

Funding

ZERNIKE PHASE PLATE CRYOEM IN OKAZAKIP41RR002250 · NCRR · UNIVERSITY OF ARIZONA · PI CHIU, WAH · 1985 to 2011
$22.1M
TISSUE CULTURE AND HYBRIDOMA MODULEP30EY011373 · NEI · CASE WESTERN RESERVE UNIVERSITY · PI Irina A Pikuleva · 1997 to 2026
$17.7M
VISION RESEARCH CENTERP30EY002520 · NEI · BAYLOR COLLEGE OF MEDICINE · PI Samuel M Wu · 1985 to 2026
$14.8M
Trasnducin Interactions with Photoreceptor MembranesR01EY007981 · NEI · BAYLOR COLLEGE OF MEDICINE · PI WENSEL, THEODORE G · 1989 to 2016
$6.1M
RGS Protein Function in Mammalian RetinaR01EY011900 · NEI · BAYLOR COLLEGE OF MEDICINE · PI WENSEL, THEODORE G · 1998 to 2010
$4.4M
RGS Domain Function in Mammalian BrainR01DA015189 · NIDA · BAYLOR COLLEGE OF MEDICINE · PI WENSEL, THEODORE G · 2002 to 2006
$1.3M
NCRR NIH HHS P41 RR002250NEI NIH HHS P30 EY002520NEI NIH HHS P30 EY011373NEI NIH HHS R01 EY007981NEI NIH HHS R01 EY011900NIDA NIH HHS R01 DA015189
6 · The paper itself

Abstract

Signal transduction in outer segments of vertebrate photoreceptors is mediated by a series of reactions among multiple polypeptides that form protein-protein complexes within or on the surface of the disk and plasma membranes. The individual components in the activation reactions include the photon receptor rhodopsin and the products of its absorption of light, the three subunits of the G protein, transducin, the four subunits of the cGMP phosphodiesterase, PDE6 and the four subunits of the cGMP-gated cation channel. Recovery involves membrane complexes with additional polypeptides including the Na(+)/Ca(2+), K(+) exchanger, NCKX2, rhodopsin kinases RK1 and RK7, arrestin, guanylate cyclases, guanylate cyclase activating proteins, GCAP1 and GCAP2, and the GTPase accelerating complex of RGS9-1, G(beta5L), and membrane anchor R9AP. Modes of membrane binding by these polypeptides include transmembrane helices, fatty acyl or isoprenyl modifications, polar interactions with lipid head groups, non-polar interactions of hydrophobic side chains with lipid hydrocarbon phase, and both polar and non-polar protein-protein interactions. In the course of signal transduction, complexes among these polypeptides form and dissociate, and undergo structural rearrangements that are coupled to their interactions with and catalysis of reactions by small molecules and ions, including guanine nucleotides, ATP, Ca(2+), Mg(2+), and lipids. The substantial progress that has been made in understanding the composition and function of these complexes is reviewed, along with the more preliminary state of our understanding of the structures of these complexes and the challenges and opportunities that present themselves for deepening our understanding of these complexes, and how they work together to convert a light signal into an electrical signal.

Indexed as

Cell MembraneHumansLight Signal TransductionMembrane ProteinsProtein BindingRhodopsinRod Cell Outer SegmentThermodynamicsTransducinMembrane ProteinsRhodopsinTransducin

Identifiers

PMID18456304
PMCPMC2615670
OpenAlexW2010335307

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.