@article{MTMT:1321722,
	title = {Probing the cavity of the slow inactivated conformation of shaker potassium channels.},
	url = {https://m2.mtmt.hu/api/publication/1321722},
	author = {Panyi, György and Deutsch, C},
	doi = {10.1085/jgp.200709758},
	journal-iso = {J GEN PHYSIOL},
	journal = {JOURNAL OF GENERAL PHYSIOLOGY},
	volume = {129},
	unique-id = {1321722},
	issn = {0022-1295},
	abstract = {Slow inactivation involves a local rearrangement of the outer mouth of voltage-gated potassium channels, but nothing is known regarding rearrangements in the cavity between the activation gate and the selectivity filter. We now report that the cavity undergoes a conformational change in the slow-inactivated state. This change is manifest as altered accessibility of residues facing the aqueous cavity and as a marked decrease in the affinity of tetraethylammonium for its internal binding site. These findings have implications for global alterations of the channel during slow inactivation and putative coupling between activation and slow-inactivation gates.},
	year = {2007},
	eissn = {1540-7748},
	pages = {403-418},
	orcid-numbers = {Panyi, György/0000-0001-6227-3301}
}

@article{MTMT:1321724,
	title = {Cross talk between activation and slow inactivation gates of Shaker potassium channels.},
	url = {https://m2.mtmt.hu/api/publication/1321724},
	author = {Panyi, György and Deutsch, C},
	doi = {10.1085/jgp.200609644},
	journal-iso = {J GEN PHYSIOL},
	journal = {JOURNAL OF GENERAL PHYSIOLOGY},
	volume = {128},
	unique-id = {1321724},
	issn = {0022-1295},
	abstract = {This study addresses the energetic coupling between the activation and slow inactivation gates of Shaker potassium channels. To track the status of the activation gate in inactivated channels that are nonconducting, we used two functional assays: the accessibility of a cysteine residue engineered into the protein lining the pore cavity (V474C) and the liberation by depolarization of a Cs(+) ion trapped behind the closed activation gate. We determined that the rate of activation gate movement depends on the state of the inactivation gate. A closed inactivation gate favors faster opening and slower closing of the activation gate. We also show that hyperpolarization closes the activation gate long before a channel recovers from inactivation. Because activation and slow inactivation are ubiquitous gating processes in potassium channels, the cross talk between them is likely to be a fundamental factor in controlling ion flux across membranes.},
	year = {2006},
	eissn = {1540-7748},
	pages = {547-559},
	orcid-numbers = {Panyi, György/0000-0001-6227-3301}
}

@article{MTMT:105638,
	title = {Ion channels and lymphocyte activation},
	url = {https://m2.mtmt.hu/api/publication/105638},
	author = {Panyi, György and Varga, Zoltán and Gaspar, R},
	doi = {10.1016/j.imlet.2003.11.020},
	journal-iso = {IMMUNOL LETT},
	journal = {IMMUNOLOGY LETTERS},
	volume = {92},
	unique-id = {105638},
	issn = {0165-2478},
	year = {2004},
	eissn = {1879-0542},
	pages = {55-66},
	orcid-numbers = {Panyi, György/0000-0001-6227-3301}
}