@article{MTMT:34502176,
	title = {TRPM2 - an adjustable thermostat},
	url = {https://m2.mtmt.hu/api/publication/34502176},
	author = {Bartók, Ádám and Csanády, László},
	doi = {10.1016/j.ceca.2024.102850},
	journal-iso = {CELL CALCIUM},
	journal = {CELL CALCIUM},
	volume = {118},
	unique-id = {34502176},
	issn = {0143-4160},
	year = {2024},
	eissn = {1532-1991},
	orcid-numbers = {Bartók, Ádám/0000-0002-1232-5246; Csanády, László/0000-0002-6547-5889}
}

@article{MTMT:34507016,
	title = {Towards personalized medicine for cystic fibrosis patients with rare mutations},
	url = {https://m2.mtmt.hu/api/publication/34507016},
	author = {Csanády, László},
	doi = {10.1113/JP286135},
	journal-iso = {J PHYSIOL-LONDON},
	journal = {JOURNAL OF PHYSIOLOGY-LONDON},
	volume = {602},
	unique-id = {34507016},
	issn = {0022-3751},
	keywords = {personalized medicine; cystic fibrosis; Neurosciences},
	year = {2024},
	eissn = {1469-7793},
	pages = {257-258},
	orcid-numbers = {Csanády, László/0000-0002-6547-5889}
}

@{MTMT:34722662,
	title = {Cystás fibrosis},
	url = {https://m2.mtmt.hu/api/publication/34722662},
	author = {Csanády, László},
	booktitle = {Orvosi patobiokémia},
	unique-id = {34722662},
	year = {2023},
	pages = {307-310},
	orcid-numbers = {Csanády, László/0000-0002-6547-5889}
}

@article{MTMT:33755807,
	title = {Blue flash sheds light on the roles of individual phosphoserines in CFTR channel activation},
	url = {https://m2.mtmt.hu/api/publication/33755807},
	author = {Csanády, László},
	doi = {10.1085/jgp.202313336},
	journal-iso = {J GEN PHYSIOL},
	journal = {JOURNAL OF GENERAL PHYSIOLOGY},
	volume = {155},
	unique-id = {33755807},
	issn = {0022-1295},
	year = {2023},
	eissn = {1540-7748},
	orcid-numbers = {Csanády, László/0000-0002-6547-5889}
}

@article{MTMT:33636409,
	title = {Optimization of CFTR gating through the evolution of its extracellular loops},
	url = {https://m2.mtmt.hu/api/publication/33636409},
	author = {Simon, Márton and Csanády, László},
	doi = {10.1085/jgp.202213264},
	journal-iso = {J GEN PHYSIOL},
	journal = {JOURNAL OF GENERAL PHYSIOLOGY},
	volume = {155},
	unique-id = {33636409},
	issn = {0022-1295},
	year = {2023},
	eissn = {1540-7748},
	orcid-numbers = {Csanády, László/0000-0002-6547-5889}
}

@article{MTMT:34232792,
	title = {Estimating the true stability of the prehydrolytic outward-facing state in an ABC protein.},
	url = {https://m2.mtmt.hu/api/publication/34232792},
	author = {Simon, Márton and Iordanov, Iordan and Szöllősi, András and Csanády, László},
	doi = {10.7554/eLife.90736},
	journal-iso = {ELIFE},
	journal = {ELIFE},
	volume = {12},
	unique-id = {34232792},
	issn = {2050-084X},
	abstract = {CFTR, the anion channel mutated in cystic fibrosis patients, is a model ABC protein whose ATP-driven conformational cycle is observable at single-molecule level in patch-clamp recordings. Bursts of CFTR pore openings are coupled to tight dimerization of its two nucleotide-binding domains (NBDs) and in wild-type (WT) channels are mostly terminated by ATP hydrolysis. The slow rate of non-hydrolytic closure - which determines how tightly bursts and ATP hydrolysis are coupled - is unknown, as burst durations of catalytic site mutants span a range of ~200-fold. Here, we show that Walker A mutation K1250A, Walker B mutation D1370N, and catalytic glutamate mutations E1371S and E1371Q all completely disrupt ATP hydrolysis. True non-hydrolytic closing rate of WT CFTR approximates that of K1250A and E1371S. That rate is slowed ~15-fold in E1371Q by a non-native inter-NBD H-bond, and accelerated ~15-fold in D1370N. These findings uncover unique features of the NBD interface in human CFTR.},
	keywords = {ZEBRAFISH; Xenopus; molecular biophysics; Structural biology; D-loop; composite ATP-binding site; flickery closure; mutant cycle},
	year = {2023},
	eissn = {2050-084X},
	orcid-numbers = {Iordanov, Iordan/0000-0001-8251-5857; Szöllősi, András/0000-0002-5570-4609; Csanády, László/0000-0002-6547-5889}
}

@article{MTMT:33262968,
	title = {Dual amplification strategy turns TRPM2 channels into supersensitive central heat detectors},
	url = {https://m2.mtmt.hu/api/publication/33262968},
	author = {Bartók, Ádám and Csanády, László},
	doi = {10.1073/pnas.2212378119},
	journal-iso = {P NATL ACAD SCI USA},
	journal = {PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA},
	volume = {119},
	unique-id = {33262968},
	issn = {0027-8424},
	abstract = {The Ca 2+ and ADP ribose (ADPR)-activated cation channel TRPM2 is the closest homolog of the cold sensor TRPM8 but serves as a deep-brain warmth sensor. To unravel the molecular mechanism of heat sensing by the TRPM2 protein, we study here temperature dependence of TRPM2 currents in cell-free membrane patches across ranges of agonist concentrations. We find that channel gating remains strictly agonist-dependent even at 40°C: heating alone or in combination with just Ca 2+ , just ADPR, Ca 2+ + cyclic ADPR, or H 2 O 2 pretreatment only marginally activates TRPM2. For fully liganded TRPM2, pore opening is intrinsically endothermic, due to ~10-fold larger activation enthalpy for opening (~200 kJ/mol) than for closure (~20 kJ/mol). However, the temperature threshold is too high (>40°C) for unliganded but too low (<15°C) for fully liganded channels. Thus, warmth sensitivity around 37°C is restricted to narrow ranges of agonist concentrations. For ADPR, that range matches, but for Ca 2+ , it exceeds bulk cytosolic values. The supraphysiological [Ca 2+ ] needed for TRPM2 warmth sensitivity is provided by Ca 2+ entering through the channel’s pore. That positive feedback provides further strong amplification to the TRPM2 temperature response (Q 10 ~ 1,000), enabling the TRPM2 protein to autonomously respond to tiny temperature fluctuations around 37°C. These functional data together with published structures suggest a molecular mechanism for opposite temperature dependences of two closely related channel proteins.},
	year = {2022},
	eissn = {1091-6490},
	orcid-numbers = {Bartók, Ádám/0000-0002-1232-5246; Csanády, László/0000-0002-6547-5889}
}

@article{MTMT:32358289,
	title = {Degenerate but indispensable: How CFTR channel activity depends on the catalytically inactive ATP binding site},
	url = {https://m2.mtmt.hu/api/publication/32358289},
	author = {Csanády, László},
	doi = {10.1113/JP282278},
	journal-iso = {J PHYSIOL-LONDON},
	journal = {JOURNAL OF PHYSIOLOGY-LONDON},
	volume = {599},
	unique-id = {32358289},
	issn = {0022-3751},
	keywords = {rundown; asymmetric ABC protein; NBD dimer},
	year = {2021},
	eissn = {1469-7793},
	pages = {4523-4524},
	orcid-numbers = {Csanády, László/0000-0002-6547-5889}
}

@article{MTMT:32573094,
	title = {Molecular pathology of the R117H cystic fibrosis mutation is explained by loss of a hydrogen bond},
	url = {https://m2.mtmt.hu/api/publication/32573094},
	author = {Simon, Márton and Csanády, László},
	doi = {10.7554/eLife.74693},
	journal-iso = {ELIFE},
	journal = {ELIFE},
	volume = {10},
	unique-id = {32573094},
	issn = {2050-084X},
	abstract = {The phosphorylation-activated anion channel cystic fibrosis transmembrane conductance regulator (CFTR) is gated by an ATP hydrolysis cycle at its two cytosolic nucleotide-binding domains, and is essential for epithelial salt-water transport. A large number of CFTR mutations cause cystic fibrosis. Since recent breakthrough in targeted pharmacotherapy, CFTR mutants with impaired gating are candidates for stimulation by potentiator drugs. Thus, understanding the molecular pathology of individual mutations has become important. The relatively common R117H mutation affects an extracellular loop, but nevertheless causes a strong gating defect. Here, we identify a hydrogen bond between the side chain of arginine 117 and the backbone carbonyl group of glutamate 1124 in the cryo-electronmicroscopic structure of phosphorylated, ATP-bound CFTR. We address the functional relevance of that interaction for CFTR gating using macroscopic and microscopic inside-out patch-clamp recordings. Employing thermodynamic double-mutant cycles, we systematically track gating-state-dependent changes in the strength of the R117-E1124 interaction. We find that the H-bond is formed only in the open state, but neither in the short-lived 'flickery' nor in the long-lived 'interburst' closed state. Loss of this H-bond explains the strong gating phenotype of the R117H mutant, including robustly shortened burst durations and strongly reduced intraburst open probability. The findings may help targeted potentiator design.},
	keywords = {PHOSPHORYLATION; AMINO-ACIDS; CONFORMATIONAL-CHANGES; IDENTIFICATION; TRANSMEMBRANE CONDUCTANCE REGULATOR; KINETIC-ANALYSIS; CFTR; gating defect; ABC protein; ATP-BINDING; CL-CHANNELS; class III mutant; R117H},
	year = {2021},
	eissn = {2050-084X},
	orcid-numbers = {Csanády, László/0000-0002-6547-5889}
}

@article{MTMT:31397038,
	title = {Simple binding of protein kinase A, prior to phosphorylation, allows CFTR anion channels to be opened by nucleotides},
	url = {https://m2.mtmt.hu/api/publication/31397038},
	author = {Mihályi, Csaba and Iordanov, Iordan and Törőcsik, Beáta and Csanády, László},
	doi = {10.1073/pnas.2007910117},
	journal-iso = {P NATL ACAD SCI USA},
	journal = {PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA},
	volume = {117},
	unique-id = {31397038},
	issn = {0027-8424},
	year = {2020},
	eissn = {1091-6490},
	pages = {21740-21746},
	orcid-numbers = {Mihályi, Csaba/0000-0001-7536-3066; Iordanov, Iordan/0000-0001-8251-5857; Törőcsik, Beáta/0000-0002-9838-3710; Csanády, László/0000-0002-6547-5889}
}

@article{MTMT:31365406,
	title = {Selective profiling of N- And C-terminal nucleotide-binding sites in a TRPM2 channel},
	url = {https://m2.mtmt.hu/api/publication/31365406},
	author = {Tóth, Balázs and Iordanov, Iordan and Csanády, László},
	doi = {10.1085/jgp.201912533},
	journal-iso = {J GEN PHYSIOL},
	journal = {JOURNAL OF GENERAL PHYSIOLOGY},
	volume = {152},
	unique-id = {31365406},
	issn = {0022-1295},
	abstract = {Transient receptor potential melastatin 2 (TRPM2) is a homotetrameric Ca2+-permeable cation channel important for the immune response, body temperature regulation, and insulin secretion, and is activated by cytosolic Ca2+ and ADP ribose (ADPR). ADPR binds to two distinct locations, formed by large N- and C-terminal cytosolic domains, respectively, of the channel protein. In invertebrate TRPM2 channels, the C-terminal site is not required for channel activity but acts as an active ADPR phosphohydrolase that cleaves the activating ligand. In vertebrate TRPM2 channels, the C-terminal site is catalytically inactive but cooperates with the N-terminal site in channel activation. The precise functional contributions to channel gating and the nucleotide selectivities of the two sites in various species have not yet been deciphered. For TRPM2 of the sea anemone Nematostella vectensis (nvTRPM2), catalytic activity is solely attributable to the C-terminal site. Here, we show that nvTRPM2 channel gating properties remain unaltered upon deletion of the C-terminal domain, indicating that the N-terminal site is single-handedly responsible for channel gating. Exploiting such functional independence of the N- and C-terminal sites, we selectively measure their affinity profiles for a series of ADPR analogues, as reflected by apparent affinities for channel activation and catalysis, respectively. Using site-directed mutagenesis, we confirm that the same N-terminal site observed in vertebrate TRPM2 channels was already present in ancient cnidarians. Finally, by characterizing the functional effects of six amino acid side chain truncations in the N-terminal site, we provide first insights into the mechanistic contributions of those side chains to TRPM2 channel gating. © 2020 Tóth et al. This article is distributed under the terms of an Attribution-Noncommercial-Share Alike-No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms/). After six months it is available under a Creative Commons License (Attribution-Noncommercial-Share Alike 4.0 International license, as described at https://creativecommons.org/licenses/by-nc-sa/4.0/).},
	year = {2020},
	eissn = {1540-7748},
	orcid-numbers = {Tóth, Balázs/0000-0002-1257-2597; Iordanov, Iordan/0000-0001-8251-5857; Csanády, László/0000-0002-6547-5889}
}

@article{MTMT:30775333,
	title = {Cystic fibrosis drug ivacaftor stimulates CFTR channels at picomolar concentrations},
	url = {https://m2.mtmt.hu/api/publication/30775333},
	author = {Csanády, László and Törőcsik, Beáta},
	doi = {10.7554/eLife.46450},
	journal-iso = {ELIFE},
	journal = {ELIFE},
	volume = {8},
	unique-id = {30775333},
	issn = {2050-084X},
	abstract = {The devastating inherited disease cystic fibrosis (CF) is caused by mutations of the Cystic Fibrosis Transmembrane Conductance Regulator (CFTR) anion channel. The recent approval of the CFTR potentiator drug ivacaftor (Vx-770) for the treatment of CF patients has marked the advent of causative CF therapy. Currently, thousands of patients are being treated with the drug, and its molecular mechanism of action is under intensive investigation. Here we determine the solubility profile and true stimulatory potency of Vx-770 towards wild-type (WT) and mutant human CFTR channels in cell-free patches of membrane. We find that its aqueous solubility is ~200 fold lower (~60 nanomolar), whereas the potency of its stimulatory effect is >100 fold higher, than reported, and is unexpectedly fully reversible. Strong, but greatly delayed, channel activation by picomolar Vx-770 identifies multiple sequential slow steps in the activation pathway. These findings provide solid guidelines for the design of in vitro studies using Vx-770. © 2019, Csanády and Töröcsik.},
	keywords = {Xenopus; Solubility; cystic fibrosis; molecular biophysics; Structural biology; F508del; VX-770; G551D; potentiator drug},
	year = {2019},
	eissn = {2050-084X},
	orcid-numbers = {Csanády, László/0000-0002-6547-5889; Törőcsik, Beáta/0000-0002-9838-3710}
}

@article{MTMT:30387986,
	title = {STRUCTURE, GATING, AND REGULATION OF THE CFTR ANION CHANNEL.},
	url = {https://m2.mtmt.hu/api/publication/30387986},
	author = {Csanády, László and Vergani, Paola and Gadsby, David C},
	doi = {10.1152/physrev.00007.2018},
	journal-iso = {PHYSIOL REV},
	journal = {PHYSIOLOGICAL REVIEWS},
	volume = {99},
	unique-id = {30387986},
	issn = {0031-9333},
	abstract = {The cystic fibrosis transmembrane conductance regulator (CFTR) belongs to the ATP binding cassette (ABC) transporter superfamily but functions as an anion channel crucial for salt and water transport across epithelial cells. CFTR dysfunction, because of mutations, causes cystic fibrosis (CF). The anion-selective pore of the CFTR protein is formed by its two transmembrane domains (TMDs) and regulated by its cytosolic domains: two nucleotide binding domains (NBDs) and a regulatory (R) domain. Channel activation requires phosphorylation of the R domain by cAMP-dependent protein kinase (PKA), and pore opening and closing (gating) of phosphorylated channels is driven by ATP binding and hydrolysis at the NBDs. This review summarizes available information on structure and mechanism of the CFTR protein, with a particular focus on atomic-level insight gained from recent cryo-electron microscopic structures and on the molecular mechanisms of channel gating and its regulation. The pharmacological mechanisms of small molecules targeting CFTR's ion channel function, aimed at treating patients suffering from CF and other diseases, are briefly discussed.},
	year = {2019},
	eissn = {1522-1210},
	pages = {707-738},
	orcid-numbers = {Csanády, László/0000-0002-6547-5889}
}

@article{MTMT:30637149,
	title = {Enzyme activity and selectivity filter stability of ancient TRPM2 channels were simultaneously lost in early vertebrates},
	url = {https://m2.mtmt.hu/api/publication/30637149},
	author = {Iordanov, Iordan and Tóth, Balázs and Szöllősi, András and Csanády, László},
	doi = {10.7554/eLife.44556},
	journal-iso = {ELIFE},
	journal = {ELIFE},
	volume = {8},
	unique-id = {30637149},
	issn = {2050-084X},
	abstract = {Transient Receptor Potential Melastatin 2 (TRPM2) is a cation channel important for the immune response, insulin secretion, and body temperature regulation. It is activated by cytosolic ADP ribose (ADPR) and contains a nudix-type motif 9 (NUDT9)-homology (NUDT9-H) domain homologous to ADPR phosphohydrolases (ADPRases). Human TRPM2 (hsTRPM2) is catalytically inactive due to mutations in the conserved Nudix box sequence. Here, we show that TRPM2 Nudix motifs are canonical in all invertebrates but vestigial in vertebrates. Correspondingly, TRPM2 of the cnidarian Nematostella vectensis (nvTRPM2) and the choanoflagellate Salpingoeca rosetta (srTRPM2) are active ADPRases. Disruption of ADPRase activity fails to affect nvTRPM2 channel currents, reporting a catalytic cycle uncoupled from gating. Furthermore, pore sequence substitutions responsible for inactivation of hsTRPM2 also appeared in vertebrates. Correspondingly, zebrafish (Danio rerio) TRPM2 (drTRPM2) and hsTRPM2 channels inactivate, but srTRPM2 and nvTRPM2 currents are stable. Thus, catalysis and pore stability were lost simultaneously in vertebrate TRPM2 channels.},
	keywords = {Xenopus; E. coli; molecular biophysics; Structural biology; Selectivity filter; ADP ribose; Nudix hydrolase; channel enzyme; rundown},
	year = {2019},
	eissn = {2050-084X},
	orcid-numbers = {Iordanov, Iordan/0000-0001-8251-5857; Tóth, Balázs/0000-0002-1257-2597; Szöllősi, András/0000-0002-5570-4609; Csanády, László/0000-0002-6547-5889}
}

@article{MTMT:3287704,
	title = {Ion channels as targets to treat cystic fibrosis lung disease},
	url = {https://m2.mtmt.hu/api/publication/3287704},
	author = {Martin, SL and Saint-Criq, V and Hwang, TC and Csanády, László},
	doi = {10.1016/j.jcf.2017.10.006},
	journal-iso = {J CYST FIBROS},
	journal = {JOURNAL OF CYSTIC FIBROSIS},
	volume = {17},
	unique-id = {3287704},
	issn = {1569-1993},
	abstract = {Lung health relies on effective mucociliary clearance and innate immune defence mechanisms. In cystic fibrosis (CF), an imbalance in ion transport due to an absence of chloride ion secretion, caused by mutations in the cystic fibrosis transmembrane conductance regulator (CFTR) and a concomitant sodium hyperabsorption, caused by dyregulation of the epithelial sodium channel (ENaC), results in mucus stasis which predisposes the lungs to cycles of chronic infection and inflammation leading to lung function decline. An increased understanding of CFTR structure and function has provided opportunity for the development of a number of novel modulators targeting mutant CFTR however, it is important to also consider other ion channels and transporters present in the airways as putative targets for drug development. In this review, we discuss recent advances in CFTR biology which will contribute to further drug discovery in the field. We also examine developments to inhibit the epithelial sodium channel (ENaC) and potentially activate alternative chloride channels and transporters as a multi-tracked strategy to hydrate CF airways and restore normal mucociliary clearance mechanisms in a manner independent of CFTR mutation.},
	year = {2018},
	eissn = {1940-6029},
	pages = {S22-S27},
	orcid-numbers = {Csanády, László/0000-0002-6547-5889}
}

@article{MTMT:30465914,
	title = {Structure of a TRPM2 channel in complex with Ca2+ explains unique gating regulation},
	url = {https://m2.mtmt.hu/api/publication/30465914},
	author = {Zhang, Zhe and Tóth, Balázs and Szöllősi, András and Chen, Jue and Csanády, László},
	doi = {10.7554/eLife.36409},
	journal-iso = {ELIFE},
	journal = {ELIFE},
	volume = {7},
	unique-id = {30465914},
	issn = {2050-084X},
	abstract = {Transient receptor potential melastatin 2 (TRPM2) is a Ca2+-permeable cation channel required for immune cell activation, insulin secretion, and body heat control. TRPM2 is activated by cytosolic Ca2+, phosphatidyl-inositol-4,5-bisphosphate and ADP ribose. Here, we present the 3 A resolution electron cryo-microscopic structure of TRPM2 from Nematostella vectensis, 63% similar in sequence to human TRPM2, in the Ca2+-bound closed state. Compared to other TRPM channels, TRPM2 exhibits unique structural features that correlate with its function. The pore is larger and more negatively charged, consistent with its high Ca2+ selectivity and larger conductance. The intracellular Ca2+ binding sites are connected to the pore and cytosol, explaining the unusual dependence of TRPM2 activity on intra- and extracellular Ca2+. In addition, the absence of a post filter motif is likely the cause of the rapid inactivation of human TRPM2. Together, our cryo-EM and electrophysiology studies provide a molecular understanding of the unique gating mechanism of TRPM2.},
	year = {2018},
	eissn = {2050-084X},
	orcid-numbers = {Tóth, Balázs/0000-0002-1257-2597; Szöllősi, András/0000-0002-5570-4609; Csanády, László/0000-0002-6547-5889}
}

@article{MTMT:3211072,
	title = {CFTR gating: Invisible transitions made visible},
	url = {https://m2.mtmt.hu/api/publication/3211072},
	author = {Csanády, László},
	doi = {10.1085/jgp.201711777},
	journal-iso = {J GEN PHYSIOL},
	journal = {JOURNAL OF GENERAL PHYSIOLOGY},
	volume = {149},
	unique-id = {3211072},
	issn = {0022-1295},
	year = {2017},
	eissn = {1540-7748},
	pages = {413-416},
	orcid-numbers = {Csanády, László/0000-0002-6547-5889}
}

@article{MTMT:3287390,
	title = {Sensory neurons: A new target for G protein signaling},
	url = {https://m2.mtmt.hu/api/publication/3287390},
	author = {Csanády, László},
	doi = {10.7554/eLife.31106},
	journal-iso = {ELIFE},
	journal = {ELIFE},
	volume = {6},
	unique-id = {3287390},
	issn = {2050-084X},
	abstract = {G protein-coupled receptor stimulation inhibits TRPM3 channel activity through direct binding of the Gβγ subunit to the channel. © Csanády.},
	keywords = {PAIN; ARTICLE; signal transduction; Immunoprecipitation; gene overexpression; G protein coupled receptor; pertussis toxin; voltage gated calcium channel; guanine nucleotide binding protein beta subunit; Protein Engineering; respiration depression; transient receptor potential channel M3; guanine nucleotide binding protein gamma subunit},
	year = {2017},
	eissn = {2050-084X},
	orcid-numbers = {Csanády, László/0000-0002-6547-5889}
}

@article{MTMT:3210856,
	title = {Molecular Structure of the Human CFTR Ion Channel},
	url = {https://m2.mtmt.hu/api/publication/3210856},
	author = {Liu, F and Zhang, Z and Csanády, László and Gadsby, DC and Chen, J},
	doi = {10.1016/j.cell.2017.02.024},
	journal-iso = {CELL},
	journal = {CELL},
	volume = {169},
	unique-id = {3210856},
	issn = {0092-8674},
	abstract = {The cystic fibrosis transmembrane conductance regulator (CFTR) is an ATP-binding cassette (ABC) transporter that uniquely functions as an ion channel. Here, we present a 3.9 Å structure of dephosphorylated human CFTR without nucleotides, determined by electron cryomicroscopy (cryo-EM). Close resemblance of this human CFTR structure to zebrafish CFTR under identical conditions reinforces its relevance for understanding CFTR function. The human CFTR structure reveals a previously unresolved helix belonging to the R domain docked inside the intracellular vestibule, precluding channel opening. By analyzing the sigmoid time course of CFTR current activation, we propose that PKA phosphorylation of the R domain is enabled by its infrequent spontaneous disengagement, which also explains residual ATPase and gating activity of dephosphorylated CFTR. From comparison with MRP1, a feature distinguishing CFTR from all other ABC transporters is the helix-loop transition in transmembrane helix 8, which likely forms the structural basis for CFTR's channel function. © 2017 Elsevier Inc.},
	keywords = {ABC transporter; anion channel; human CFTR; cryo-EM},
	year = {2017},
	eissn = {1097-4172},
	pages = {85-95.e8},
	orcid-numbers = {Csanády, László/0000-0002-6547-5889}
}

@article{MTMT:3287727,
	title = {Asymmetry of movements in CFTR's two ATP sites during pore opening serves their distinct functions},
	url = {https://m2.mtmt.hu/api/publication/3287727},
	author = {Sorum, Ben and Törőcsik, Beáta and Csanády, László},
	doi = {10.7554/eLife.29013},
	journal-iso = {ELIFE},
	journal = {ELIFE},
	volume = {6},
	unique-id = {3287727},
	issn = {2050-084X},
	abstract = {CFTR, the chloride channel mutated in cystic fibrosis (CF) patients, is opened by ATP binding to two cytosolic nucleotide binding domains (NBDs), but pore-domain mutations may also impair gating. ATP-bound NBDs dimerize occluding two nucleotides at interfacial binding sites; one site hydrolyzes ATP, the other is inactive. The pore opens upon tightening, and closes upon disengagement, of the catalytic site following ATP hydrolysis. Extent, timing, and role of non-catalytic-site movements are unknown. Here we exploit equilibrium gating of a hydrolysis-deficient mutant and apply Phi value analysis to compare timing of opening-associated movements at multiple locations, from the cytoplasmic ATP sites to the extracellular surface. Marked asynchrony of motion in the two ATP sites reveals their distinct roles in channel gating. The results clarify the molecular mechanisms of functional cross-talk between canonical and degenerate ATP sites in asymmetric ABC proteins, and of the gating defects caused by two common CF mutations.},
	year = {2017},
	eissn = {2050-084X},
	orcid-numbers = {Sorum, Ben/0000-0001-6742-1094; Törőcsik, Beáta/0000-0002-9838-3710; Csanády, László/0000-0002-6547-5889}
}

@article{MTMT:3057146,
	title = {A single active catalytic site is sufficient to promote transport in P-glycoprotein},
	url = {https://m2.mtmt.hu/api/publication/3057146},
	author = {Mészáros-Bársony, Orsolya and Szalóki, Gábor and Türk, Dóra and Tarapcsák, Szabolcs and Gutay-Tóth, Zsuzsanna and Bacsó, Zsolt and Holb, Imre and Székvölgyi, Lóránt and Szabó, Gábor and Csanády, László and Szakács, Gergely and Kormosné, Goda Katalin},
	doi = {10.1038/srep24810},
	journal-iso = {SCI REP},
	journal = {SCIENTIFIC REPORTS},
	volume = {6},
	unique-id = {3057146},
	issn = {2045-2322},
	abstract = {P-glycoprotein (Pgp) is an ABC transporter responsible for 
		the ATP-dependent efflux of chemotherapeutic compounds from 
		multidrug resistant cancer cells. Better understanding of the 
		molecular mechanism of Pgp-mediated transport could promote 
		rational drug design to circumvent multidrug resistance. By 
		measuring drug binding affinity and reactivity to a 
		conformation-sensitive antibody we show here that nucleotide 
		binding drives Pgp from a high to a low substrate-affinity 
		state and this switch coincides with the flip from the 
		inward- to the outward-facing conformation. Furthermore, the 
		outward-facing conformation survives ATP hydrolysis: the 
		post-hydrolytic complex is stabilized by vanadate, and the 
		slow recovery from this state requires two functional 
		catalytic sites. The catalytically inactive double Walker A 
		mutant is stabilized in a high substrate affinity inward-open 
		conformation, but mutants with one intact catalytic center 
		preserve their ability to hydrolyze ATP and to promote drug 
		transport, suggesting that the two catalytic sites are 
		randomly recruited for ATP hydrolysis.},
	year = {2016},
	eissn = {2045-2322},
	orcid-numbers = {Csanády, László/0000-0002-6547-5889}
}

@article{MTMT:3105008,
	title = {The proposed channel-enzyme transient receptor potential melastatin 2 does not possess ADP ribose hydrolase activity},
	url = {https://m2.mtmt.hu/api/publication/3105008},
	author = {Iordanov, Iordan and Mihályi, Csaba and Tóth, Balázs and Csanády, László},
	doi = {10.7554/eLife.17600},
	journal-iso = {ELIFE},
	journal = {ELIFE},
	volume = {5},
	unique-id = {3105008},
	issn = {2050-084X},
	year = {2016},
	eissn = {2050-084X},
	orcid-numbers = {Iordanov, Iordan/0000-0001-8251-5857; Mihályi, Csaba/0000-0001-7536-3066; Tóth, Balázs/0000-0002-1257-2597; Csanády, László/0000-0002-6547-5889}
}

@article{MTMT:3083629,
	title = {Obligate coupling of CFTR pore opening to tight nucleotide-binding domain dimerization},
	url = {https://m2.mtmt.hu/api/publication/3083629},
	author = {Mihályi, Csaba and Törőcsik, Beáta and Csanády, László},
	doi = {10.7554/eLife.18164},
	journal-iso = {ELIFE},
	journal = {ELIFE},
	volume = {5},
	unique-id = {3083629},
	issn = {2050-084X},
	abstract = {In CFTR, the chloride channel mutated in cystic fibrosis (CF) patients, ATP-binding-induced dimerization of two cytosolic nucleotide binding domains (NBDs) opens the pore, and dimer disruption following ATP hydrolysis closes it. Spontaneous openings without ATP are rare in wild-type CFTR, but in certain CF mutants constitute the only gating mechanism, stimulated by ivacaftor, a clinically approved CFTR potentiator. The molecular motions underlying spontaneous gating are unclear. Here we correlate energetic coupling between residues across the dimer interface with spontaneous pore opening/closure in single CFTR channels. We show that spontaneous openings are also strictly coupled to NBD dimerization, which may therefore occur even without ATP. Coordinated NBD/pore movements are therefore intrinsic to CFTR: ATP alters the stability, but not the fundamental structural architecture, of open- and closed-pore conformations. This explains correlated effects of phosphorylation, mutations, and drugs on ATP-driven and spontaneous activity, providing insights for understanding CF mutation and drug mechanisms.},
	year = {2016},
	eissn = {2050-084X},
	orcid-numbers = {Mihályi, Csaba/0000-0001-7536-3066; Törőcsik, Beáta/0000-0002-9838-3710; Csanády, László/0000-0002-6547-5889}
}

@article{MTMT:2964742,
	title = {Timing of CFTR Pore Opening and Structure of Its Transition State.},
	url = {https://m2.mtmt.hu/api/publication/2964742},
	author = {Sorum, Ben and Czégé, Dávid and Csanády, László},
	doi = {10.1016/j.cell.2015.09.052},
	journal-iso = {CELL},
	journal = {CELL},
	volume = {163},
	unique-id = {2964742},
	issn = {0092-8674},
	abstract = {In CFTR, the chloride ion channel mutated in cystic fibrosis (CF) patients, pore opening is coupled to ATP-binding-induced dimerization of two cytosolic nucleotide binding domains (NBDs) and closure to dimer disruption following ATP hydrolysis. CFTR opening rate, unusually slow because of its high-energy transition state, is further slowed by CF mutation DeltaF508. Here, we exploit equilibrium gating of hydrolysis-deficient CFTR mutant D1370N and apply rate-equilibrium free-energy relationship analysis to estimate relative timing of opening movements in distinct protein regions. We find clear directionality of motion along the longitudinal protein axis and identify an opening transition-state structure with the NBD dimer formed but the pore still closed. Thus, strain at the NBD/pore-domain interface, the DeltaF508 mutation locus, underlies the energetic barrier for opening. Our findings suggest a therapeutic opportunity to stabilize this transition-state structure pharmacologically in DeltaF508-CFTR to correct its opening defect, an essential step toward restoring CFTR function.},
	year = {2015},
	eissn = {1097-4172},
	pages = {724-733},
	orcid-numbers = {Sorum, Ben/0000-0001-6742-1094; Czégé, Dávid/0000-0001-7746-5816; Csanády, László/0000-0002-6547-5889}
}

@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:2761953,
	title = {Structure-activity analysis of a CFTR channel potentiator: Distinct molecular parts underlie dual gating effects.},
	url = {https://m2.mtmt.hu/api/publication/2761953},
	author = {Csanády, László and Törőcsik, Beáta},
	doi = {10.1085/jgp.201411246},
	journal-iso = {J GEN PHYSIOL},
	journal = {JOURNAL OF GENERAL PHYSIOLOGY},
	volume = {144},
	unique-id = {2761953},
	issn = {0022-1295},
	abstract = {The cystic fibrosis (CF) transmembrane conductance regulator (CFTR) is a member of the ATP-binding cassette transporter superfamily that functions as an epithelial chloride channel. Gating of the CFTR ion conduction pore involves a conserved irreversible cyclic mechanism driven by ATP binding and hydrolysis at two cytosolic nucleotide-binding domains (NBDs): formation of an intramolecular NBD dimer that occludes two ATP molecules opens the pore, whereas dimer disruption after ATP hydrolysis closes it. CFTR dysfunction resulting from inherited mutations causes CF. The most common CF mutation, deletion of phenylalanine 508 (DeltaF508), impairs both protein folding and processing and channel gating. Development of DeltaF508 CFTR correctors (to increase cell surface expression) and potentiators (to enhance open probability, Po) is therefore a key focus of CF research. The practical utility of 5-nitro-2-(3-phenylpropylamino)benzoate (NPPB), one of the most efficacious potentiators of DeltaF508 CFTR identified to date, is limited by its pore-blocking side effect. NPPB-mediated stimulation of Po is unique in that it involves modulation of gating transition state stability. Although stabilization by NPPB of the transition state for pore opening enhances both the rate of channel opening and the very slow rate of nonhydrolytic closure, because of CFTR's cyclic gating mechanism, the net effect is Po stimulation. In addition, slowing of ATP hydrolysis by NPPB delays pore closure, further enhancing Po. Here we show that NPPB stimulates gating at a site outside the pore and that these individual actions of NPPB on CFTR are fully attributable to one or the other of its two complementary molecular parts, 3-nitrobenzoate (3NB) and 3-phenylpropylamine (3PP), both of which stimulate Po: the pore-blocking 3NB selectively stabilizes the transition state for opening, whereas the nonblocking 3PP selectively slows the ATP hydrolysis step. Understanding structure-activity relationships of NPPB might prove useful for designing potent, clinically relevant CFTR potentiators.},
	year = {2014},
	eissn = {1540-7748},
	pages = {321-336},
	orcid-numbers = {Csanády, László/0000-0002-6547-5889; Törőcsik, Beáta/0000-0002-9838-3710}
}

@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:2333381,
	title = {Conformational changes in the catalytically inactive nucleotide-binding site of CFTR},
	url = {https://m2.mtmt.hu/api/publication/2333381},
	author = {Csanády, László and Mihályi, Csaba and Szöllősi, András and Törőcsik, Beáta and Vergani, P},
	doi = {10.1085/jgp.201210954},
	journal-iso = {J GEN PHYSIOL},
	journal = {JOURNAL OF GENERAL PHYSIOLOGY},
	volume = {142},
	unique-id = {2333381},
	issn = {0022-1295},
	abstract = {A central step in the gating of the cystic fibrosis transmembrane conductance regulator (CFTR) chloride channel is the association of its two cytosolic nucleotide-binding domains (NBDs) into a head-to-tail dimer, with two nucleotides bound at the interface. Channel opening and closing, respectively, are coupled to formation and disruption of this tight NBD dimer. CFTR is an asymmetric adenosine triphosphate (ATP)-binding cassette protein in which the two interfacial-binding sites (composite sites 1 and 2) are functionally different. During gating, the canonical, catalytically active nucleotide-binding site (site 2) cycles between dimerized prehydrolytic (state O1), dimerized post-hydrolytic (state O2), and dissociated (state C) forms in a preferential C-->O1-->O2-->C sequence. In contrast, the catalytically inactive nucleotide-binding site (site 1) is believed to remain associated, ATP-bound, for several gating cycles. Here, we have examined the possibility of conformational changes in site 1 during gating, by studying gating effects of perturbations in site 1.Previous work showed that channel closure is slowed, both under hydrolytic and nonhydrolytic conditions, by occupancy of site 1 by N6-(2-phenylethyl)-ATP (P-ATP) as well as by the site-1 mutation H1348A (NBD2 signature sequence). Here, we found that P-ATP prolongs wild-type (WT) CFTR burst durations by selectively slowing (>2x) transition O1-->O2 and decreases the nonhydrolytic closing rate (transition O1-->C) of CFTR mutants K1250A ( approximately 4x) and E1371S ( approximately 3x). Mutation H1348A also slowed ( approximately 3x) the O1-->O2 transition in the WT background and decreased the nonhydrolytic closing rate of both K1250A ( approximately 3x) and E1371S ( approximately 3x) background mutants. Neither P-ATP nor the H1348A mutation affected the 1:1 stoichiometry between ATP occlusion and channel burst events characteristic to WT CFTR gating in ATP. The marked effect that different structural perturbations at site 1 have on both steps O1-->C and O1-->O2 suggests that the overall conformational changes that CFTR undergoes upon opening and coincident with hydrolysis at the active site 2 include significant structural rearrangement at site 1.},
	year = {2013},
	eissn = {1540-7748},
	pages = {61-73},
	orcid-numbers = {Csanády, László/0000-0002-6547-5889; Mihályi, Csaba/0000-0001-7536-3066; Szöllősi, András/0000-0002-5570-4609; Törőcsik, Beáta/0000-0002-9838-3710}
}

@{MTMT:2221309,
	title = {CFTR, an Ion Channel Evolved from ABC Transporter},
	url = {https://m2.mtmt.hu/api/publication/2221309},
	author = {Vergani, P and Gadsby, DC and Csanády, László},
	booktitle = {Encyclopedia of Biophysics},
	doi = {10.1007/978-3-642-16712-6_364},
	unique-id = {2221309},
	year = {2013},
	pages = {254-265},
	orcid-numbers = {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:32730112,
	title = {Electrophysiological, Biochemical, and Bioinformatic Methods for Studying CFTR Channel Gating and Its Regulation},
	url = {https://m2.mtmt.hu/api/publication/32730112},
	isbn = {9781617791161},
	author = {Csanády, László and Vergani, Paola and Gulyas-Kovacs, Attila and Gadsby, David C.},
	doi = {10.1007/978-1-61779-117-8_28},
	journal-iso = {METHODS MOL BIOL},
	journal = {METHODS IN MOLECULAR BIOLOGY},
	volume = {741},
	unique-id = {32730112},
	issn = {1064-3745},
	abstract = {CFTR is the only member of the ABC (ATP-binding cassette) protein superfamily known to function as an ion channel. Most other ABC proteins are ATP-driven transporters, in which a cycle of ATP binding and hydrolysis, at intracellular nucleotide binding domains (NBDs), powers uphill substrate translocation across the membrane. In CFTR, this same ATP-driven cycle opens and closes a transmembrane pore through which chloride ions flow rapidly down their electrochemical gradient. Detailed analysis of the pattern of gating of CFTR channels thus offers the opportunity to learn about mechanisms of function not only of CFTR channels but also of their ABC transporter ancestors. In addition, CFTR channel gating is subject to complex regulation by kinase-mediated phosphorylation at multiple consensus sites in a cytoplasmic regulatory domain that is unique to CFTR. Here we offer a practical guide to extract useful information about the mechanisms that control opening and closing of CFTR channels: on how to plan (including information obtained from analysis of multiple sequence alignments), carry out, and analyze electrophysiological and biochemical experiments, as well as on how to circumvent potential pitfalls.},
	keywords = {PROTEIN-KINASE-C; TRANSMEMBRANE CONDUCTANCE REGULATOR; KINETIC-ANALYSIS; kinetic analysis; chloride channel; Multiple channels; Biochemistry & Molecular Biology; Biochemical Research Methods; Single channels; NUCLEOTIDE-BINDING DOMAINS; ATP-BINDING; Energetic analysis; cysteine modification; R-DOMAIN; ACETYLCHOLINE-RECEPTOR CHANNEL; COEVOLVING POSITIONS},
	year = {2011},
	eissn = {1940-6029},
	pages = {443-469},
	orcid-numbers = {Csanády, László/0000-0002-6547-5889; Vergani, Paola/0000-0002-5422-4662}
}

@article{MTMT:1690127,
	title = {Mitoxantrone is expelled by the ABCG2 multidrug transporter directly from the plasma membrane},
	url = {https://m2.mtmt.hu/api/publication/1690127},
	author = {Homolya, László and Orbán, Tamás I. and Csanády, László and Sarkadi, Balázs},
	doi = {10.1016/j.bbamem.2010.07.031},
	journal-iso = {BBA-BIOMEMBRANES},
	journal = {BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES},
	volume = {1808},
	unique-id = {1690127},
	issn = {0005-2736},
	abstract = {ABC multidrug transporter proteins expel a wide variety of structurally unrelated, mostly hydrophobic compounds from cells. The special role of these transporters both at the physiological barriers and in cancer cells is based on their extremely broad substrate recognition. Since hydrophobic compounds are known to partition into the lipid bilayer and accumulate in membranes. the "classical pump" model for the mechanism of multidrug transporter proteins has been challenged, and alternative models suggesting substrate recognition within the lipid bilayer have been proposed. Although much effort has been made to validate this concept, unambiguous evidence for direct drug extrusion from the plasma membrane has not been provided yet. Here we show a detailed on-line microscopic analysis of cellular extrusion of fluorescent anti-cancer drugs, mitoxantrone and pheophorbide A, by a key human multidrug transporter, ABCG2. Using the fully active GFP-tagged ABCG2 and exploiting the special character of mitoxantrone that gains fluorescence in the lipid environment, we were able to determine transporter-modulated drug concentrations separately in the plasma membrane and the intracellular compartments. Different kinetic models describing the various transport mechanisms were generated and the experimental data were analyzed using these models. On the basis of the kinetic analysis, drug extrusion from the cytoplasm can be excluded, thus, our results indicate that ABCG2 extrudes mitoxantrone directly from the plasma membrane. (C) 2010 Elsevier B.V. All rights reserved.},
	year = {2011},
	eissn = {1879-2642},
	pages = {154-163},
	orcid-numbers = {Homolya, László/0000-0003-1639-8140; Orbán, Tamás I./0000-0002-3424-3428; Csanády, László/0000-0002-6547-5889; Sarkadi, Balázs/0000-0003-0592-4539}
}

@article{MTMT:1690126,
	title = {Mutant cycles at CFTR's non-canonical ATP-binding site support little interface separation during gating},
	url = {https://m2.mtmt.hu/api/publication/1690126},
	author = {Szöllősi, András and Muallem, DR and Csanády, László and Vergani, P},
	doi = {10.1085/jgp.201110608},
	journal-iso = {J GEN PHYSIOL},
	journal = {JOURNAL OF GENERAL PHYSIOLOGY},
	volume = {137},
	unique-id = {1690126},
	issn = {0022-1295},
	year = {2011},
	eissn = {1540-7748},
	pages = {549-562},
	orcid-numbers = {Szöllősi, András/0000-0002-5570-4609; 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:1493080,
	title = {Degenerate ABC composite site is stably glued together by trapped ATP},
	url = {https://m2.mtmt.hu/api/publication/1493080},
	author = {Csanády, László},
	doi = {10.1085/jgp.201010443},
	journal-iso = {J GEN PHYSIOL},
	journal = {JOURNAL OF GENERAL PHYSIOLOGY},
	volume = {135},
	unique-id = {1493080},
	issn = {0022-1295},
	year = {2010},
	eissn = {1540-7748},
	pages = {395-398},
	orcid-numbers = {Csanády, László/0000-0002-6547-5889}
}

@article{MTMT:1493079,
	title = {Permeating proton found guilty in compromising TRPM2 channel activity},
	url = {https://m2.mtmt.hu/api/publication/1493079},
	author = {Csanády, László},
	doi = {10.1113/jphysiol.2010.190223},
	journal-iso = {J PHYSIOL-LONDON},
	journal = {JOURNAL OF PHYSIOLOGY-LONDON},
	volume = {588},
	unique-id = {1493079},
	issn = {0022-3751},
	year = {2010},
	eissn = {1469-7793},
	pages = {1661-1662},
	orcid-numbers = {Csanády, László/0000-0002-6547-5889}
}

@article{MTMT:1493077,
	title = {Involvement of F1296 and N1303 of CFTR in induced-fit conformational change in response to ATP binding at NBD2},
	url = {https://m2.mtmt.hu/api/publication/1493077},
	author = {Szöllősi, András and Vergani, P and Csanády, László},
	doi = {10.1085/jgp.201010434},
	journal-iso = {J GEN PHYSIOL},
	journal = {JOURNAL OF GENERAL PHYSIOLOGY},
	volume = {136},
	unique-id = {1493077},
	issn = {0022-1295},
	year = {2010},
	eissn = {1540-7748},
	pages = {407-423},
	orcid-numbers = {Szöllősi, András/0000-0002-5570-4609; 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:1234613,
	title = {A novel kinetic assay of mitochondrial ATP-ADP exchange rate mediated by the ANT},
	url = {https://m2.mtmt.hu/api/publication/1234613},
	author = {Chinopoulos, Christos and Sisa-Vajda, Szilvia and Csanády, László and Mándi, Miklós and Mathe, K and Ádám, Veronika},
	doi = {10.1016/j.bpj.2008.12.3915},
	journal-iso = {BIOPHYS J},
	journal = {BIOPHYSICAL JOURNAL},
	volume = {96},
	unique-id = {1234613},
	issn = {0006-3495},
	abstract = {A novel method exploiting the differential affinity of ADP and ATP to Mg(2+) was 
		developed to measure mitochondrial ADP-ATP exchange rate. The rate of ATP
		appearing in the medium after addition of ADP to energized mitochondria, is
		calculated from the measured rate of change in free extramitochondrial [Mg(2+)]
		reported by the membrane-impermeable 5K(+) salt of the Mg(2+)-sensitive
		fluorescent indicator, Magnesium Green, using standard binding equations. The
		assay is designed such that the adenine nucleotide translocase (ANT) is the sole 
		mediator of changes in [Mg(2+)] in the extramitochondrial volume, as a result of 
		ADP-ATP exchange. We also provide data on the dependence of ATP efflux rate
		within the 6.8-7.8 matrix pH range as a function of membrane potential. Finally, 
		by comparing the ATP-ADP steady-state exchange rate to the amount of the ANT in
		rat brain synaptic, brain nonsynaptic, heart and liver mitochondria, we provide
		molecular turnover numbers for the known ANT isotypes.},
	year = {2009},
	eissn = {1542-0086},
	pages = {2490-2504},
	orcid-numbers = {Chinopoulos, Christos/0000-0003-0183-4149; Csanády, László/0000-0002-6547-5889; Ádám, Veronika/0000-0002-8350-8701}
}

@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: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:1493084,
	title = {Sulfonylurea receptors type 1 and 2A randomly assemble to form heteromeric K-ATP channels of mixed subunit composition},
	url = {https://m2.mtmt.hu/api/publication/1493084},
	author = {Chan, KW and Wheeler, A and Csanády, László},
	doi = {10.1085/jgp.200709894},
	journal-iso = {J GEN PHYSIOL},
	journal = {JOURNAL OF GENERAL PHYSIOLOGY},
	volume = {131},
	unique-id = {1493084},
	issn = {0022-1295},
	year = {2008},
	eissn = {1540-7748},
	pages = {43-58},
	orcid-numbers = {Csanády, László/0000-0002-6547-5889}
}

@article{MTMT:1493083,
	title = {The twain shall meet: channels, transporters and things between - Meeting on Membrane Transport in Flux: The Ambiguous Interface between Channels and Pumps},
	url = {https://m2.mtmt.hu/api/publication/1493083},
	author = {Csanády, László and Mindell, JA},
	doi = {10.1038/embor.2008.172},
	journal-iso = {EMBO REP},
	journal = {EMBO REPORTS},
	volume = {9},
	unique-id = {1493083},
	issn = {1469-221X},
	year = {2008},
	eissn = {1469-3178},
	pages = {960-965},
	orcid-numbers = {Csanády, László/0000-0002-6547-5889}
}

@article{MTMT:1493087,
	title = {Statistical evaluation of ion-channel gating models based on distributions of log-likelihood ratios},
	url = {https://m2.mtmt.hu/api/publication/1493087},
	author = {Csanády, László},
	doi = {10.1529/biophysj.105.075135},
	journal-iso = {BIOPHYS J},
	journal = {BIOPHYSICAL JOURNAL},
	volume = {90},
	unique-id = {1493087},
	issn = {0006-3495},
	year = {2006},
	eissn = {1542-0086},
	pages = {3523-3545},
	orcid-numbers = {Csanády, László/0000-0002-6547-5889}
}

@article{MTMT:1493085,
	title = {Thermodynamics of CFTR channel gating: A spreading conformational change initiates an irreversible gating cycle},
	url = {https://m2.mtmt.hu/api/publication/1493085},
	author = {Csanády, László and Nairn, AC and Gadsby, DC},
	doi = {10.1085/jgp.200609558},
	journal-iso = {J GEN PHYSIOL},
	journal = {JOURNAL OF GENERAL PHYSIOLOGY},
	volume = {128},
	unique-id = {1493085},
	issn = {0022-1295},
	year = {2006},
	eissn = {1540-7748},
	pages = {523-533},
	orcid-numbers = {Csanády, László/0000-0002-6547-5889}
}

@article{MTMT:1493086,
	title = {The N-terminal transmembrane domain (TMD0) and a cytosolic linker (L0) of sulphonylurea receptor define the unique intrinsic gating of K-ATP channels},
	url = {https://m2.mtmt.hu/api/publication/1493086},
	author = {Fang, K and Csanády, László and Chan, KW},
	doi = {10.1113/jphysiol.2006.112748},
	journal-iso = {J PHYSIOL-LONDON},
	journal = {JOURNAL OF PHYSIOLOGY-LONDON},
	volume = {576},
	unique-id = {1493086},
	issn = {0022-3751},
	year = {2006},
	eissn = {1469-7793},
	pages = {379-389},
	orcid-numbers = {Csanády, László/0000-0002-6547-5889}
}

@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}
}

@article{MTMT:1493090,
	title = {Functional roles of nonconserved structural segments in CFTR's NH2-terminal nucleotide binding domain},
	url = {https://m2.mtmt.hu/api/publication/1493090},
	author = {Csanády, László and Chan, KW and Nairn, AC and Gadsby, DC},
	doi = {10.1085/jgp.200409174},
	journal-iso = {J GEN PHYSIOL},
	journal = {JOURNAL OF GENERAL PHYSIOLOGY},
	volume = {125},
	unique-id = {1493090},
	issn = {0022-1295},
	year = {2005},
	eissn = {1540-7748},
	pages = {43-55},
	orcid-numbers = {Csanády, László/0000-0002-6547-5889}
}

@article{MTMT:1493089,
	title = {Preferential phosphorylation of R-domain serine 768 dampens activation of CFTR channels by PKA},
	url = {https://m2.mtmt.hu/api/publication/1493089},
	author = {Csanády, László and Seto-Young, D and Chan, KW and Cenciarelli, C and Angel, BB and Qin, J and McLachlin, DT and Krutchinsky, AN and Chait, BT and Nairn, AC and Gadsby, DC},
	doi = {10.1085/jgp.200409076},
	journal-iso = {J GEN PHYSIOL},
	journal = {JOURNAL OF GENERAL PHYSIOLOGY},
	volume = {125},
	unique-id = {1493089},
	issn = {0022-1295},
	year = {2005},
	eissn = {1540-7748},
	pages = {171-186},
	orcid-numbers = {Csanády, László/0000-0002-6547-5889}
}

@article{MTMT:1030898,
	title = {Antagonistic regulation of native Ca2+- and ATP-sensitive cation channels in brain capillaries by nucleotides and decavanadate},
	url = {https://m2.mtmt.hu/api/publication/1030898},
	author = {Csanády, László and Ádám, Veronika},
	doi = {10.1085/jgp.200309008},
	journal-iso = {J GEN PHYSIOL},
	journal = {JOURNAL OF GENERAL PHYSIOLOGY},
	volume = {123},
	unique-id = {1030898},
	issn = {0022-1295},
	year = {2004},
	eissn = {1540-7748},
	pages = {743-757},
	orcid-numbers = {Csanády, László/0000-0002-6547-5889; Ádám, Veronika/0000-0002-8350-8701}
}

@article{MTMT:1030904,
	title = {Ca2+- and voltage-dependent gating of Ca2+- and ATP-sensitive cationic channels in brain capillary endothelium},
	url = {https://m2.mtmt.hu/api/publication/1030904},
	author = {Csanády, László and Ádám, Veronika},
	doi = {10.1016/S0006-3495(03)74476-2},
	journal-iso = {BIOPHYS J},
	journal = {BIOPHYSICAL JOURNAL},
	volume = {85},
	unique-id = {1030904},
	issn = {0006-3495},
	year = {2003},
	eissn = {1542-0086},
	pages = {313-327},
	orcid-numbers = {Csanády, László/0000-0002-6547-5889; Ádám, Veronika/0000-0002-8350-8701}
}

@article{MTMT:1493091,
	title = {Severed molecules functionally define the boundaries of the cystic fibrosis transmembrane conductance regulator's NH2-terminal nucleotide binding domain},
	url = {https://m2.mtmt.hu/api/publication/1493091},
	author = {Chan, KW and Csanády, László and Seto-Young, D and Nairn, AC and Gadsby, DC},
	doi = {10.1085/jgp.116.2.163},
	journal-iso = {J GEN PHYSIOL},
	journal = {JOURNAL OF GENERAL PHYSIOLOGY},
	volume = {116},
	unique-id = {1493091},
	issn = {0022-1295},
	year = {2000},
	eissn = {1540-7748},
	pages = {163-180},
	orcid-numbers = {Csanády, László/0000-0002-6547-5889}
}

@article{MTMT:1493767,
	title = {Severed channels probe regulation of gating of cystic fibrosis transmembrane conductance regulator by its cytoplasmic domains},
	url = {https://m2.mtmt.hu/api/publication/1493767},
	author = {Csanády, László and Chan, KW and Seto-Young, D and Kopsco, DC and Nairn, AC and Gadsby, DC},
	doi = {10.1085/jgp.116.3.477},
	journal-iso = {J GEN PHYSIOL},
	journal = {JOURNAL OF GENERAL PHYSIOLOGY},
	volume = {116},
	unique-id = {1493767},
	issn = {0022-1295},
	year = {2000},
	eissn = {1540-7748},
	pages = {477-500},
	orcid-numbers = {Csanády, László/0000-0002-6547-5889}
}

@article{MTMT:1493092,
	title = {Rapid kinetic analysis of multichannel records by a simultaneous fit to all dwell-time histograms},
	url = {https://m2.mtmt.hu/api/publication/1493092},
	author = {Csanády, László},
	doi = {10.1016/S0006-3495(00)76636-7},
	journal-iso = {BIOPHYS J},
	journal = {BIOPHYSICAL JOURNAL},
	volume = {78},
	unique-id = {1493092},
	issn = {0006-3495},
	year = {2000},
	eissn = {1542-0086},
	pages = {785-799},
	orcid-numbers = {Csanády, László/0000-0002-6547-5889}
}

@article{MTMT:1493093,
	title = {CFTR channel gating: Incremental progress in irreversible steps},
	url = {https://m2.mtmt.hu/api/publication/1493093},
	author = {Csanády, László and Gadsby, DC},
	doi = {10.1085/jgp.114.1.49},
	journal-iso = {J GEN PHYSIOL},
	journal = {JOURNAL OF GENERAL PHYSIOLOGY},
	volume = {114},
	unique-id = {1493093},
	issn = {0022-1295},
	year = {1999},
	eissn = {1540-7748},
	pages = {49-53},
	orcid-numbers = {Csanády, László/0000-0002-6547-5889}
}