@article{MTMT:2762109,
	title = {Putative chanzyme activity of TRPM2 cation channel is unrelated to pore gating},
	url = {https://m2.mtmt.hu/api/publication/2762109},
	author = {Tóth, Balázs and Iordanov, Iordan and Csanády, László},
	doi = {10.1073/pnas.1412449111},
	journal-iso = {P NATL ACAD SCI USA},
	journal = {PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA},
	volume = {111},
	unique-id = {2762109},
	issn = {0027-8424},
	year = {2014},
	eissn = {1091-6490},
	pages = {16949-16954},
	orcid-numbers = {Tóth, Balázs/0000-0002-1257-2597; Iordanov, Iordan/0000-0001-8251-5857; Csanády, László/0000-0002-6547-5889}
}

@article{MTMT:2041974,
	title = {Pore collapse underlies irreversible inactivation of TRPM2 cation channel currents.},
	url = {https://m2.mtmt.hu/api/publication/2041974},
	author = {Tóth, Balázs and Csanády, László},
	doi = {10.1073/pnas.1204702109},
	journal-iso = {P NATL ACAD SCI USA},
	journal = {PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA},
	volume = {109},
	unique-id = {2041974},
	issn = {0027-8424},
	abstract = {The Ca(2+)-permeable cation channel transient receptor potential melastatin 2 (TRPM2) plays a key role in pathogen-evoked phagocyte activation, postischemic neuronal apoptosis, and glucose-evoked insulin secretion, by linking these cellular responses to oxidative stress. TRPM2 channels are coactivated by binding of intracellular ADP ribose and Ca(2+) to distinct cytosolically accessible sites on the channels. These ligands likely regulate the activation gate, conserved in the voltage-gated cation channel superfamily, that comprises a helix bundle formed by the intracellular ends of transmembrane helix six of each subunit. For several K(+) and TRPM family channels, activation gate opening requires the presence of phosphatidylinositol-bisphosphate (PIP(2)) in the inner membrane leaflet. Most TRPM family channels inactivate upon prolonged stimulation in inside-out patches; this "rundown" is due to PIP(2) depletion. TRPM2 currents also run down within minutes, but the molecular mechanism of this process is unknown. Here we report that high-affinity PIP(2) binding regulates Ca(2+) sensitivity of TRPM2 activation. Nevertheless, TRPM2 inactivation is not due to PIP(2) depletion; rather, it is state dependent, sensitive to permeating ions, and can be completely prevented by mutations in the extracellular selectivity filter. Introduction of two negative charges plus a single-residue insertion, to mimic the filter sequence of TRPM5, results in TRPM2 channels that maintain unabated maximal activity for over 1 h, and display altered permeation properties but intact ADP ribose/Ca(2+)-dependent gating. Thus, upon prolonged stimulation, the TRPM2 selectivity filter undergoes a conformational change reminiscent of that accompanying C-type inactivation of voltage-gated K(+) channels. The noninactivating TRPM2 variant will be invaluable for gating studies.},
	year = {2012},
	eissn = {1091-6490},
	pages = {13440-13445},
	orcid-numbers = {Tóth, Balázs/0000-0002-1257-2597; Csanády, László/0000-0002-6547-5889}
}

@article{MTMT:1493078,
	title = {Identification of Direct and Indirect Effectors of the Transient Receptor Potential Melastatin 2 (TRPM2) Cation Channel},
	url = {https://m2.mtmt.hu/api/publication/1493078},
	author = {Tóth, Balázs and Csanády, László},
	doi = {10.1074/jbc.M109.066464},
	journal-iso = {J BIOL CHEM},
	journal = {JOURNAL OF BIOLOGICAL CHEMISTRY},
	volume = {285},
	unique-id = {1493078},
	issn = {0021-9258},
	year = {2010},
	eissn = {1083-351X},
	pages = {30091-30102},
	orcid-numbers = {Tóth, Balázs/0000-0002-1257-2597; Csanády, László/0000-0002-6547-5889}
}

@article{MTMT:1502468,
	title = {Four Ca2+ Ions Activate TRPM2 Channels by Binding in Deep Crevices near the Pore but Intracellularly of the Gate},
	url = {https://m2.mtmt.hu/api/publication/1502468},
	author = {Csanády, László and Törőcsik, Beáta},
	doi = {10.1085/jgp.200810109},
	journal-iso = {J GEN PHYSIOL},
	journal = {JOURNAL OF GENERAL PHYSIOLOGY},
	volume = {133},
	unique-id = {1502468},
	issn = {0022-1295},
	year = {2009},
	eissn = {1540-7748},
	pages = {189-203},
	orcid-numbers = {Csanády, László/0000-0002-6547-5889; Törőcsik, Beáta/0000-0002-9838-3710}
}