@article{MTMT:2949645,
	title = {Ruling out pyridine dinucleotides as true TRPM2 channel activators reveals novel direct agonist ADP-ribose-2'-phosphate},
	url = {https://m2.mtmt.hu/api/publication/2949645},
	author = {Tóth, Balázs and Iordanov, Iordan and Csanády, László},
	doi = {10.1085/jgp.201511377},
	journal-iso = {J GEN PHYSIOL},
	journal = {JOURNAL OF GENERAL PHYSIOLOGY},
	volume = {145},
	unique-id = {2949645},
	issn = {0022-1295},
	abstract = {Transient receptor potential melastatin 2 (TRPM2), a Ca(2+)-permeable cation channel implicated in postischemic neuronal cell death, leukocyte activation, and insulin secretion, is activated by intracellular ADP ribose (ADPR). In addition, the pyridine dinucleotides nicotinamide-adenine-dinucleotide (NAD), nicotinic acid-adenine-dinucleotide (NAAD), and NAAD-2'-phosphate (NAADP) have been shown to activate TRPM2, or to enhance its activation by ADPR, when dialyzed into cells. The precise subset of nucleotides that act directly on the TRPM2 protein, however, is unknown. Here, we use a heterologously expressed, affinity-purified-specific ADPR hydrolase to purify commercial preparations of pyridine dinucleotides from substantial contaminations by ADPR or ADPR-2'-phosphate (ADPRP). Direct application of purified NAD, NAAD, or NAADP to the cytosolic face of TRPM2 channels in inside-out patches demonstrated that none of them stimulates gating, or affects channel activation by ADPR, indicating that none of these dinucleotides directly binds to TRPM2. Instead, our experiments identify for the first time ADPRP as a true direct TRPM2 agonist of potential biological interest.},
	year = {2015},
	eissn = {1540-7748},
	pages = {419-430},
	orcid-numbers = {Tóth, Balázs/0000-0002-1257-2597; Iordanov, Iordan/0000-0001-8251-5857; Csanády, László/0000-0002-6547-5889}
}

@article{MTMT:2496247,
	title = {Catalyst-like Modulation of Transitions States for CFTR Channel Opening and Closing: New Stimulation Strategy Exploits Nonequilibrium Gating},
	url = {https://m2.mtmt.hu/api/publication/2496247},
	author = {Csanády, László and Törőcsik, Beáta},
	doi = {10.1085/jgp.201311089},
	journal-iso = {J GEN PHYSIOL},
	journal = {JOURNAL OF GENERAL PHYSIOLOGY},
	volume = {143},
	unique-id = {2496247},
	issn = {0022-1295},
	year = {2014},
	eissn = {1540-7748},
	pages = {269-287},
	orcid-numbers = {Csanády, László/0000-0002-6547-5889; Törőcsik, Beáta/0000-0002-9838-3710}
}

@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:1493081,
	title = {Strict coupling between CFTR's catalytic cycle and gating of its Cl- ion pore revealed by distributions of open channel burst durations},
	url = {https://m2.mtmt.hu/api/publication/1493081},
	author = {Csanády, László and Vergani, P and Gadsby, DC},
	doi = {10.1073/pnas.0911061107},
	journal-iso = {P NATL ACAD SCI USA},
	journal = {PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA},
	volume = {107},
	unique-id = {1493081},
	issn = {0027-8424},
	year = {2010},
	eissn = {1091-6490},
	pages = {1241-1246},
	orcid-numbers = {Csanády, László/0000-0002-6547-5889}
}

@article{MTMT:1493082,
	title = {Application of rate-equilibrium free energy relationship analysis to nonequilibrium ion channel gating mechanisms},
	url = {https://m2.mtmt.hu/api/publication/1493082},
	author = {Csanády, László},
	doi = {10.1085/jgp.200910268},
	journal-iso = {J GEN PHYSIOL},
	journal = {JOURNAL OF GENERAL PHYSIOLOGY},
	volume = {134},
	unique-id = {1493082},
	issn = {0022-1295},
	year = {2009},
	eissn = {1540-7748},
	pages = {129-136},
	orcid-numbers = {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}
}

@article{MTMT:1493088,
	title = {The ABC protein turned chloride channel whose failure causes cystic fibrosis},
	url = {https://m2.mtmt.hu/api/publication/1493088},
	author = {Gadsby, DC and Vergani, P and Csanády, László},
	doi = {10.1038/nature04712},
	journal-iso = {NATURE},
	journal = {NATURE},
	volume = {440},
	unique-id = {1493088},
	issn = {0028-0836},
	year = {2006},
	eissn = {1476-4687},
	pages = {477-483},
	orcid-numbers = {Csanády, László/0000-0002-6547-5889}
}