@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}
}

@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}
}

@{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: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: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: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: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: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: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}
}