Evidence map›Paper›PMID 25224127›Full record

ArticleJournal of computer-aided molecular design2014

Predicted 3D structures of olfactory receptors with details of odorant binding to OR1G1.

Soo-Kyung Kim, William A Goddard

Abstract read
PubMed Publisher
In one paragraph

Article in Journal of computer-aided molecular design, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed, 1 pooled it
1.0field-weighted citation impact, top 25% 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

11 citing papers in PubMed, 1 synthesis or guideline pooled it, 21 citations in OpenAlex.

  1. Microbial volatile organic compounds and olfactory receptors in wound malodor.Frontiers in cellular and infection microbiology · 2026
    Pooled it
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Molecular mechanism of activation of human musk receptors OR5AN1 and OR1A1 by (Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  8. Article
  9. Article
  10. G protein-coupled odorant receptors: From sequence to structure.Protein science : a publication of the Protein Society · 2015
    Article
  11. 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 1 institution in 1 country.

Soo-Kyung KimMaterials and Process Simulation Center (MC139-74), California Institute of Technology, 1200 E. California Blvd., Pasadena, CA, 91125, USA, skkim@wag.caltech.edu.
William A Goddard
California Institute of Technology · US

Funding

Maneuvering of Macrophage Function By Escherichia coli K1R01NS073115 · NINDS · CHILDREN'S HOSPITAL OF LOS ANGELES · PI NEMANI, PRASADARAO V · 2010 to 2014
$1.6M
A Novel Method of Nanoparticle Delivery to Brain by Targeting Ec-gp96R01NS071112 · NINDS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI DAVIS, MARK E · 2010 to 2012
$972k
NINDS NIH HHS 1R01NS073115NINDS NIH HHS R01NS071112
6 · The paper itself

Abstract

Olfactory receptors (ORs) are responsible for mediating the sense of smell; they allow humans to recognize an enormous number of odors but the connection between binding and perception is not known. We predict the ensemble of low energy structures for the human OR1G1 (hOR1G1) and also for six other diverse ORs, using the G protein-coupled receptor Ensemble of Structures in Membrane BiLayer Environment complete sampling method that samples 13 trillion different rotations and tilts using four different templates to predict the 24 structures likely to be important in binding and activation. Our predicted most stable structures of hOR1G1 have a salt-bridge between the conserved D3.49 and K6.30 in the D(E)RY region, that we expect to be associated with an inactive form. The hOR1G1 structure also has specific interaction in transmembrane domains (TMD) 3-6 (E3.39 and H6.40), which is likely an important conformational feature for all hORs because of the ~94 to 98 % conservation among all hOR sequences. Of the five ligands studied (nonanal, 9-decen-1-ol, 1-nonanol, camphor, and n-butanal), we find that the 4 expected to bind lead to similar binding energies with nonanol the strongest.

Indexed as

Protein ConformationAmino Acid SequenceBinding SitesFatty AlcoholsHumansLigandsModels, MolecularOdorantsProtein BindingProtein Structure, TertiaryReceptors, Odorant1-nonanolFatty AlcoholsLigandsOR1G1 protein, humanReceptors, Odorant

Identifiers

PMID25224127
OpenAlexW2042615414

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.