Evidence map›Paper›PMID 8599649›Full record

ArticleBiophysical journal1995

Automated method for modeling seven-helix transmembrane receptors from experimental data.

P Herzyk, R E Hubbard

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in Biophysical journal, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
4.0field-weighted citation impact, top 5% 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

23 citing papers in PubMed, 96 citations in OpenAlex.

  1. Article
  2. Amide vibrations are delocalized across the hydrophobic interface of a transmembrane helix dimer.Proceedings of the National Academy of Sciences of the United States of America · 2006
    Article
  3. Article
  4. Optimal bundling of transmembrane helices using sparse distance constraints.Protein science : a publication of the Protein Society · 2004
    Article
  5. Article
  6. Molecular modelling studies on the ORL1-receptor and ORL1-agonists.Journal of computer-aided molecular design · 2003
    Article
  7. Article
  8. Article
  9. A sequence and structural study of transmembrane helices.Journal of computer-aided molecular design · 2001
    Article
  10. Article
  11. Article
  12. Structural organization of G-protein-coupled receptors.Journal of computer-aided molecular design · 1999
    Review
  13. The variable and conserved interfaces of modeled olfactory receptor proteins.Protein science : a publication of the Protein Society · 1999
    Article
  14. Review
  15. Article
  16. Molecular modeling of the human vasopressin V2 receptor/agonist complex.Journal of computer-aided molecular design · 1998
    Article
  17. Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

P HerzykDepartment of Chemistry, University of York, Heslington, United Kingdom. pavel@yorvic.york.ac.uk
R E Hubbard
University of York · GB

Funding

Wellcome Trust
6 · The paper itself

Abstract

A rule-based automated method is presented for modeling the structures of the seven transmembrane helices of G-protein-coupled receptors. The structures are generated by using a simulated annealing Monte Carlo procedure that positions and orients rigid helices to satisfy structural restraints. The restraints are derived from analysis of experimental information from biophysical studies on native and mutant proteins, from analysis of the sequences of related proteins, and from theoretical considerations of protein structure. Calculations are presented for two systems. The method was validated through calculations using appropriate experimental information for bacteriorhodopsin, which produced a model structure with a root mean square (rms) deviation of 1.87 A from the structure determined by electron microscopy. Calculations are also presented using experimental and theoretical information available for bovine rhodopsin to assign the helices to a projection density map and to produce a model of bovine rhodopsin that can be used as a template for modeling other G-protein-coupled receptors.

Indexed as

Models, StructuralProtein Structure, SecondaryAmino Acid SequenceAnimalsAutomationBacteriorhodopsinsCattleGTP-Binding ProteinsKineticsMathematicsMicroscopy, ElectronMolecular Sequence DataMonte Carlo MethodProtein ConformationReceptors, Cell SurfaceRetinaldehydeBacteriorhodopsinsGTP-Binding ProteinsReceptors, Cell SurfaceRetinaldehydeRhodopsin

Identifiers

PMID8599649
PMCPMC1236480
OpenAlexW2013701986

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.