@article{MTMT:34405999,
	title = {GproteinDb in 2024: new G protein-GPCR couplings, AlphaFold2-multimer models and interface interactions},
	url = {https://m2.mtmt.hu/api/publication/34405999},
	author = {Pándy-Szekeres, Gáspár and Taracena Herrera, Luis P and Caroli, Jimmy and Kermani, Ali A and Kulkarni, Yashraj and Keserű, György Miklós and Gloriam, David E},
	doi = {10.1093/nar/gkad1089},
	journal-iso = {NUCLEIC ACIDS RES},
	journal = {NUCLEIC ACIDS RESEARCH},
	volume = {52},
	unique-id = {34405999},
	issn = {0305-1048},
	abstract = {G proteins are the major signal proteins of ∼800 receptors for medicines, hormones, neurotransmitters, tastants and odorants. GproteinDb offers integrated genomic, structural, and pharmacological data and tools for analysis, visualization and experiment design. Here, we present the first major update of GproteinDb greatly expanding its coupling data and structural templates, adding AlphaFold2 structure models of GPCR–G protein complexes and advancing the interactive analysis tools for their interfaces underlying coupling selectivity. We present insights on coupling agreement across datasets and parameters, including constitutive activity, agonist-induced activity and kinetics. GproteinDb is accessible at https://gproteindb.org.},
	year = {2024},
	eissn = {1362-4962},
	pages = {D466-D475},
	orcid-numbers = {Gloriam, David E/0000-0002-4299-7561}
}

@article{MTMT:33845452,
	title = {SH2db, an information system for the SH2 domain},
	url = {https://m2.mtmt.hu/api/publication/33845452},
	author = {Bajusz, Dávid and Pándy-Szekeres, Gáspár and Takács, Ágnes and de Araujo, Elvin D and Keserű, György Miklós},
	doi = {10.1093/nar/gkad420},
	journal-iso = {NUCLEIC ACIDS RES},
	journal = {NUCLEIC ACIDS RESEARCH},
	volume = {51},
	unique-id = {33845452},
	issn = {0305-1048},
	abstract = {SH2 domains are key mediators of phosphotyrosine-based signalling, and therapeutic targets for diverse, mostly oncological, disease indications. They have a highly conserved structure with a central beta sheet that divides the binding surface of the protein into two main pockets, responsible for phosphotyrosine binding (pY pocket) and substrate specificity (pY + 3 pocket). In recent years, structural databases have proven to be invaluable resources for the drug discovery community, as they contain highly relevant and up-to-date information on important protein classes. Here, we present SH2db, a comprehensive structural database and webserver for SH2 domain structures. To organize these protein structures efficiently, we introduce (i) a generic residue numbering scheme to enhance the comparability of different SH2 domains, (ii) a structure-based multiple sequence alignment of all 120 human wild-type SH2 domain sequences and their PDB and AlphaFold structures. The aligned sequences and structures can be searched, browsed and downloaded from the online interface of SH2db (http://sh2db.ttk.hu), with functions to conveniently prepare multiple structures into a Pymol session, and to export simple charts on the contents of the database. Our hope is that SH2db can assist researchers in their day-to-day work by becoming a one-stop shop for SH2 domain related research.},
	year = {2023},
	eissn = {1362-4962},
	pages = {W542-W552},
	orcid-numbers = {Bajusz, Dávid/0000-0003-4277-9481}
}

@article{MTMT:33421768,
	title = {GPCRdb in 2023: state-specific structure models using AlphaFold2 and new ligand resources},
	url = {https://m2.mtmt.hu/api/publication/33421768},
	author = {Pándy-Szekeres, Gáspár and Caroli, Jimmy and Mamyrbekov, Alibek and Kermani, Ali A. and Keserű, György Miklós and Kooistra, Albert J. and Gloriam, David E.},
	doi = {10.1093/nar/gkac1013},
	journal-iso = {NUCLEIC ACIDS RES},
	journal = {NUCLEIC ACIDS RESEARCH},
	volume = {51},
	unique-id = {33421768},
	issn = {0305-1048},
	abstract = {G protein-coupled receptors (GPCRs) are physiologically abundant signaling hubs routing hundreds of extracellular signal substances and drugs into intracellular pathways. The GPCR database, GPCRdb supports > 5000 interdisciplinary researchers every month with reference data, analysis, visualization, experiment design and dissemination. Here, we present our fifth major GPCRdb release setting out with an overview of the many resources for receptor sequences, structures, and ligands. This includes recently published additions of class D generic residue numbers, a comparative structure analysis tool to identify functional determinants, trees clustering GPCR structures by 3D conformation, and mutations stabilizing inactive/active states. We provide new state-specific structure models of all human non-olfactory GPCRs built using AlphaFold2-MultiState. We also provide a new resource of endogenous ligands along with a larger number of surrogate ligands with bioactivity, vendor, and physiochemical descriptor data. The one-stop-shop ligand resources integrate ligands/data from the ChEMBL, Guide to Pharmacology, PDSP Ki and PubChem database. The GPCRdb is available athttps://gpcrdb.org.},
	year = {2023},
	eissn = {1362-4962},
	pages = {D395-D402}
}

@{MTMT:32832459,
	title = {Computational Medicinal Chemistry to Target GPCRs},
	url = {https://m2.mtmt.hu/api/publication/32832459},
	author = {Kiss, Dóra Judit and Pándy-Szekeres, Gáspár and Keserű, György Miklós},
	booktitle = {Comprehensive Pharmacology},
	doi = {10.1016/B978-0-12-820472-6.00208-5},
	unique-id = {32832459},
	year = {2022},
	pages = {84-114}
}

@article{MTMT:32544494,
	title = {The G protein database, GproteinDb},
	url = {https://m2.mtmt.hu/api/publication/32544494},
	author = {Pándy-Szekeres, Gáspár and Esguerra, Mauricio and Hauser, Alexander S and Caroli, Jimmy and Munk, Christian and Pilger, Steven and Keserű, György Miklós and Kooistra, Albert J and Gloriam, David E},
	doi = {10.1093/nar/gkab852},
	journal-iso = {NUCLEIC ACIDS RES},
	journal = {NUCLEIC ACIDS RESEARCH},
	volume = {50},
	unique-id = {32544494},
	issn = {0305-1048},
	year = {2022},
	eissn = {1362-4962},
	pages = {518-525},
	orcid-numbers = {Kooistra, Albert J/0000-0001-5514-6021; Gloriam, David E/0000-0002-4299-7561}
}

@article{MTMT:31817126,
	title = {GPCRdb in 2021: integrating GPCR sequence, structure and function},
	url = {https://m2.mtmt.hu/api/publication/31817126},
	author = {Kooistra, Albert J and Mordalski, Stefan and Pándy-Szekeres, Gáspár and Esguerra, Mauricio and Mamyrbekov, Alibek and Munk, Christian and Keserű, György Miklós and Gloriam, David E},
	doi = {10.1093/nar/gkaa1080},
	journal-iso = {NUCLEIC ACIDS RES},
	journal = {NUCLEIC ACIDS RESEARCH},
	volume = {49},
	unique-id = {31817126},
	issn = {0305-1048},
	year = {2021},
	eissn = {1362-4962},
	pages = {D335-D343},
	orcid-numbers = {Kooistra, Albert J/0000-0001-5514-6021; Gloriam, David E/0000-0002-4299-7561}
}

@article{MTMT:31799297,
	title = {Controlling receptor function from the extracellular vestibule of G-protein coupled receptors},
	url = {https://m2.mtmt.hu/api/publication/31799297},
	author = {Egyed, Attila and Domány-Kovács, Katalin and Koványi, Bence and Horti, Ferenc and Kurko, Dalma and Kiss, Dóra Judit and Pándy-Szekeres, Gáspár and Greiner, István and Keserű, György Miklós},
	doi = {10.1039/D0CC05532H},
	journal-iso = {CHEM COMMUN},
	journal = {CHEMICAL COMMUNICATIONS},
	volume = {56},
	unique-id = {31799297},
	issn = {1359-7345},
	year = {2020},
	eissn = {1364-548X},
	pages = {14167-14170}
}

@article{MTMT:30834454,
	title = {Allosteric activation of metabotropic glutamate receptor 5},
	url = {https://m2.mtmt.hu/api/publication/30834454},
	author = {Jójárt, Balázs and Orgován, Zoltán and Márki, Árpád and Pándy-Szekeres, Gáspár and Ferenczy, György and Keserű, György Miklós},
	doi = {10.1080/07391102.2019.1638302},
	journal-iso = {J BIOMOL STRUCT DYN},
	journal = {JOURNAL OF BIOMOLECULAR STRUCTURE & DYNAMICS},
	volume = {38},
	unique-id = {30834454},
	issn = {0739-1102},
	year = {2020},
	eissn = {1538-0254},
	pages = {2624-2632},
	orcid-numbers = {Márki, Árpád/0000-0002-6056-8891; Ferenczy, György/0000-0002-5771-4616}
}

@article{MTMT:31163292,
	title = {GPCRdb in 2018: adding GPCR structure models and ligands},
	url = {https://m2.mtmt.hu/api/publication/31163292},
	author = {Pándy-Szekeres, Gáspár and Munk, Christian and Tsonkov, Tsonko M and Mordalski, Stefan and Harpsøe, Kasper and Hauser, Alexander S and Bojarski, Andrzej J and Gloriam, David E},
	doi = {10.1093/nar/gkx1109},
	journal-iso = {NUCLEIC ACIDS RES},
	journal = {NUCLEIC ACIDS RESEARCH},
	volume = {46},
	unique-id = {31163292},
	issn = {0305-1048},
	year = {2018},
	eissn = {1362-4962},
	pages = {D440-D446}
}