Evidence map›Paper›PMID 19291412›Full record

ReviewThe AAPS journal2009

Recent advances in structure-based virtual screening of G-protein coupled receptors.

Subramaniam Ananthan, Wei Zhang, Judith Varady Hobrath

Open access · hybridAbstract readReview
In one paragraph

Review in The AAPS journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.9field-weighted citation impact, top 26% 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

5 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. 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.

Subramaniam AnanthanDrug Discovery Division, Southern Research Institute, 2000 Ninth Avenue South, Birmingham, AL 35205, USA. ananthan@sri.org
Wei Zhang
Judith Varady Hobrath
Southern Research Institute · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In addition to the rhodopsin crystal structure, high-resolution crystal structures of ligand-mediated G-protein-coupled receptors (GPCRs) have recently become available, and these have become attractive templates for developing homology models of several GPCRs of therapeutic interest. These crystal structures and the homology models derived from them have provided significant insights into ligand-receptor interactions. Moreover, several studies have demonstrated that the structural models are indeed suitable for virtual screening of compound databases to identify new ligands for various GPCRs. Recent examples of such virtual screening against GPCRs are discussed in this review.

Indexed as

AnimalsCrystallography, X-RayDrug DiscoveryDrug Evaluation, PreclinicalHormonesHumansLigandsModels, ChemicalModels, MolecularNeurotransmitter AgentsProtein BindingProtein ConformationReceptors, G-Protein-CoupledReceptors, NeurotransmitterReceptors, PeptideStructure-Activity RelationshipHormonesLigandsNeurotransmitter AgentsReceptors, G-Protein-CoupledReceptors, NeurotransmitterReceptors, Peptide

Identifiers

PMID19291412
PMCPMC2664893
OpenAlexW2013325166

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.