TY  - JOUR
AU  - Panyi, György
AU  - Deutsch, C
TI  - Probing the cavity of the slow inactivated conformation of shaker potassium channels.
JF  - JOURNAL OF GENERAL PHYSIOLOGY
J2  - J GEN PHYSIOL
VL  - 129
PY  - 2007
IS  - 5
SP  - 403
EP  - 418
PG  - 16
SN  - 0022-1295
DO  - 10.1085/jgp.200709758
UR  - https://m2.mtmt.hu/api/publication/1321722
ID  - 1321722
N1  - GR: GM 069837/GM/NIGMS NIH HHS/United States
GR: NS 052665/NS/NINDS NIH HHS/United States
PMC: PMC2154382
OID: NLM: PMC2154382
AB  - 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.
LA  - English
DB  - MTMT
ER  - 

TY  - JOUR
AU  - Panyi, György
AU  - Deutsch, C
TI  - Cross talk between activation and slow inactivation gates of Shaker potassium channels.
JF  - JOURNAL OF GENERAL PHYSIOLOGY
J2  - J GEN PHYSIOL
VL  - 128
PY  - 2006
IS  - 5
SP  - 547
EP  - 559
PG  - 13
SN  - 0022-1295
DO  - 10.1085/jgp.200609644
UR  - https://m2.mtmt.hu/api/publication/1321724
ID  - 1321724
N1  - GR: GM 069837/GM/NIGMS NIH HHS/United States
GR: NS 052665/NS/NINDS NIH HHS/United States
PMC: PMC2151579
OID: NLM: PMC2151579
AB  - 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.
LA  - English
DB  - MTMT
ER  - 

TY  - JOUR
AU  - Panyi, György
AU  - Varga, Zoltán
AU  - Gaspar, R
TI  - Ion channels and lymphocyte activation
JF  - IMMUNOLOGY LETTERS
J2  - IMMUNOL LETT
VL  - 92
PY  - 2004
SP  - 55
EP  - 66
PG  - 12
SN  - 0165-2478
DO  - 10.1016/j.imlet.2003.11.020
UR  - https://m2.mtmt.hu/api/publication/105638
ID  - 105638
LA  - English
DB  - MTMT
ER  -