ArticleChimica oggi2010
Modeling G Protein-Coupled Receptors: a Concrete Possibility.
Article in Chimica oggi, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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.
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.
Who cites it
15 citing papers in PubMed, 26 citations in OpenAlex.
- Influence of the Structural Accuracy of Homology Models on Their Applicability to Docking-Based Virtual Screening: The βJournal of chemical information and modeling · 2019Article
- Using Dimensionality Reduction to Analyze Protein Trajectories.Frontiers in molecular biosciences · 2019Article
- Homology modeling of a Class A GPCR in the inactive conformation: A quantitative analysis of the correlation between model/template sequence identity and model accuracy.Journal of molecular graphics & modelling · 2016Article
- Computational studies to predict or explain G protein coupled receptor polypharmacology.Trends in pharmacological sciences · 2014Article
- Graph analysis of β2 adrenergic receptor structures: a "social network" of GPCR residues.In silico pharmacology · 2013Article
- G protein-coupled receptors: computer-aided ligand discovery and computational structural analyses in the 2010s.In silico pharmacology · 2013Article
- G-protein coupled receptor 83 (GPR83) signaling determined by constitutive and zinc(II)-induced activity.PloS one · 2013Article
- New insights for drug design from the X-ray crystallographic structures of G-protein-coupled receptors.Molecular pharmacology · 2012Review
- In silico screening for agonists and blockers of the β(2) adrenergic receptor: implications of inactive and activated state structures.Journal of computational chemistry · 2012Article
- Structural aspects of M₃ muscarinic acetylcholine receptor dimer formation and activation.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2012Article
- Predicting the biological activities through QSAR analysis and docking-based scoring.Methods in molecular biology (Clifton, N.J.) · 2012Article
- From laptop to benchtop to bedside: structure-based drug design on protein targets.Current pharmaceutical design · 2012Review
- Homology modeling of class a G protein-coupled receptors.Methods in molecular biology (Clifton, N.J.) · 2012Article
- Membrane-sensitive conformational states of helix 8 in the metabotropic Glu2 receptor, a class C GPCR.PloS one · 2012Article
- In silico analysis of the binding of agonists and blockers to the β2-adrenergic receptor.Journal of molecular graphics & modelling · 2011Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
1 author.
Funding
Abstract
G protein-coupled receptors (GPCRs) are a large superfamily of membrane bound signaling proteins that are involved in the regulation of a wide range of physiological functions and constitute the most common target for therapeutic intervention. Due to the paucity of crystal structures, homology modeling has become a widespread technique for the construction of GPCR models, which have been applied to the study of their structure-function relationships and to the identification of lead ligands through virtual screening. Rhodopsin has been for years the only available template. However, recent breakthroughs in GPCR crystallography have led to the solution of the structures of a few additional receptors. In light of these newly elucidated crystal structures, we have been able to produce a substantial amount of data to demonstrate that accurate models of GPCRs in complex with their ligands can be constructed through homology modeling followed by fully flexible molecular docking. These results have been confirmed by our success in the first blind assessment of GPCR modeling and docking, organized in coordination with the solution of the X-ray structure of the adenosine A(2A) receptor. Taken together, these data indicate that: a) the transmembrane helical bundle can be modeled with considerable accuracy; b) predicting the binding mode of a ligand, although doable, is challenging; c) modeling of the extracellular and intracellular loops is still problematic.
Identifiers
21253444PMC3022441W142246363What OpenQuestion holds
Registered trials
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.