| scholarly article | Q13442814 |
| P819 | ADS bibcode | 2014PLoSO...990694J |
| P356 | DOI | 10.1371/JOURNAL.PONE.0090694 |
| P932 | PMC publication ID | 3944890 |
| P698 | PubMed publication ID | 24651466 |
| P5875 | ResearchGate publication ID | 260997268 |
| P50 | author | Marta Filizola | Q41045386 |
| P2093 | author name string | Jennifer M Johnston | |
| P2860 | cites work | Structure of the human κ-opioid receptor in complex with JDTic | Q24308048 |
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| P275 | copyright license | Creative Commons Attribution 4.0 International | Q20007257 |
| P6216 | copyright status | copyrighted | Q50423863 |
| P433 | issue | 2 | |
| P407 | language of work or name | English | Q1860 |
| P304 | page(s) | e90694 | |
| P577 | publication date | 2014-02-28 | |
| P1433 | published in | PLOS One | Q564954 |
| P1476 | title | Differential stability of the crystallographic interfaces of mu- and kappa-opioid receptors | |
| P478 | volume | 9 |
| Q52660783 | Closely related, yet unique: Distinct homo- and heterodimerization patterns of G protein coupled chemokine receptors and their fine-tuning by cholesterol. |
| Q92923684 | Computational Modeling of Claudin Structure and Function |
| Q44341109 | Conformational Heterogeneity of Intracellular Loop 3 of the μ-opioid G-protein Coupled Receptor |
| Q47113820 | Excessive aggregation of membrane proteins in the Martini model |
| Q39165104 | Insights into the function of opioid receptors from molecular dynamics simulations of available crystal structures. |
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| Q39525809 | Multi-Component Protein - Protein Docking Based Protocol with External Scoring for Modeling Dimers of G Protein-Coupled Receptors |
| Q36096058 | Opioid receptors: Structural and mechanistic insights into pharmacology and signaling |
| Q27319797 | Preferred supramolecular organization and dimer interfaces of opioid receptors from simulated self-association |
| Q38292961 | Structure and function of G protein-coupled receptor oligomers: implications for drug discovery |
| Q26778330 | Understanding the fabric of protein crystals: computational classification of biological interfaces and crystal contacts |
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