Evidence map›Paper›PMID 8524807›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1995

Projection structure of frog rhodopsin in two crystal forms.

G F Schertler, P A Hargrave

Open access · greenAbstract readComparative Study
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
7.5field-weighted citation impact, top 2% 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

45 citing papers in PubMed, 217 citations in OpenAlex.

  1. Review
  2. Supramolecular organization of rhodopsin in rod photoreceptor cell membranes.Pflugers Archiv : European journal of physiology · 2021
    Review
  3. Article
  4. Unconventional Roles of Opsins.Annual review of cell and developmental biology · 2017
    Review
  5. Article
  6. Chemistry and biology of the initial steps in vision: the Friedenwald lecture.Investigative ophthalmology & visual science · 2014
    Article
  7. Article
  8. Computational approaches for modeling GPCR dimerization.Current pharmaceutical biotechnology · 2014
    Review
  9. Review
  10. Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. Review
  18. Article
  19. Article
  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

2 authors at 2 institutions in 1 country.

G F SchertlerMedical Research Council Laboratory of Molecular Biology, Cambridge, United Kingdom.
P A Hargrave
Medical Research Council · GBMRC Laboratory of Molecular Biology · GB

Funding

RHODOPSIN STRUCTURE/FUNCTIONR01EY006226 · NEI · UNIVERSITY OF FLORIDA · PI HARGRAVE, PAUL A. · 1985 to 2002
$997k
RHODOPSIN STRUCTURE AND FUNCTIONR37EY006226 · NEI · UNIVERSITY OF FLORIDA · PI HARGRAVE, PAUL A. · 1988 to 1997
–
NEI NIH HHS EY06226
6 · The paper itself

Abstract

Rhodopsin is the G protein-coupled receptor that upon light activation triggers the visual transduction cascade. Rod cell outer segment disc membranes were isolated from dark-adapted frog retinas and were extracted with Tween detergents to obtain two-dimensional rhodopsin crystals for electron crystallography. When Tween 80 was used, tubular structures with a p2 lattice (a = 32 A, b = 83 A, gamma = 91 degrees) were formed. The use of a Tween 80/Tween 20 mixture favored the formation of larger p22(1)2(1) lattices (a = 40 A, b = 146 A, gamma = 90 degrees). Micrographs from frozen hydrated frog rhodopsin crystals were processed, and projection structures to 7-A resolution for the p22(1)2(1) form and to 6-A resolution for the p2 form were calculated. The maps of frog rhodopsin in both crystal forms are very similar to the 9-A map obtained previously for bovine rhodopsin and show that the arrangement of the helices is the same. In a tentative topographic model, helices 4, 6, and 7 are nearly perpendicular to the plane of the membrane. In the higher-resolution projection maps of frog rhodopsin, helix 5 looks more tilted than it appeared previously. The quality of the two frog rhodopsin crystals suggests that they would be suitable to obtain a three-dimensional structure in which all helices would be resolved.

Indexed as

Protein Structure, SecondaryProtein Structure, TertiaryAnimalsAnuraBacteriorhodopsinsCattleCrystallographyElectronsImage Processing, Computer-AssistedRhodopsinRod Cell Outer SegmentSpecies SpecificityBacteriorhodopsinsRhodopsin

Identifiers

PMID8524807
PMCPMC40445
OpenAlexW2081884169

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.