LASZLO CSANADY

Summary

Affiliation: Semmelweis University
Country: Hungary

Publications

  1. pmc Involvement of F1296 and N1303 of CFTR in induced-fit conformational change in response to ATP binding at NBD2
    Andras Szollosi
    Department of Medical Biochemistry, Semmelweis University, Budapest, Hungary
    J Gen Physiol 136:407-23. 2010
  2. pmc Application of rate-equilibrium free energy relationship analysis to nonequilibrium ion channel gating mechanisms
    LASZLO CSANADY
    Department of Medical Biochemistry, Semmelweis University, Budapest, Hungary
    J Gen Physiol 134:129-36. 2009
  3. doi request reprint Electrophysiological, biochemical, and bioinformatic methods for studying CFTR channel gating and its regulation
    LASZLO CSANADY
    Department of Medical Biochemistry, Semmelweis University, Budapest, Hungary
    Methods Mol Biol 741:443-69. 2011
  4. pmc Four Ca2+ ions activate TRPM2 channels by binding in deep crevices near the pore but intracellularly of the gate
    LASZLO CSANADY
    Department of Medical Biochemistry, Semmelweis University, Budapest, Hungary
    J Gen Physiol 133:189-203. 2009
  5. pmc Strict coupling between CFTR's catalytic cycle and gating of its Cl- ion pore revealed by distributions of open channel burst durations
    LASZLO CSANADY
    Department of Medical Biochemistry, Semmelweis University, Budapest H 1094, Hungary
    Proc Natl Acad Sci U S A 107:1241-6. 2010
  6. pmc Thermodynamics of CFTR channel gating: a spreading conformational change initiates an irreversible gating cycle
    LASZLO CSANADY
    Department of Medical Biochemistry, Semmelweis University, 1088 Budapest, Hungary
    J Gen Physiol 128:523-33. 2006
  7. pmc Preferential phosphorylation of R-domain Serine 768 dampens activation of CFTR channels by PKA
    LASZLO CSANADY
    Department of Medical Biochemistry, Semmelweis University, Budapest, Germany
    J Gen Physiol 125:171-86. 2005
  8. pmc Functional roles of nonconserved structural segments in CFTR's NH2-terminal nucleotide binding domain
    LASZLO CSANADY
    Department of Medical Biochemistry, Semmelweis University, 1088 Budapest, Hungary
    J Gen Physiol 125:43-55. 2005
  9. pmc Mutant cycles at CFTR's non-canonical ATP-binding site support little interface separation during gating
    Andras Szollosi
    Department of Medical Biochemistry, Semmelweis University, Budapest, Hungary
    J Gen Physiol 137:549-62. 2011
  10. pmc Conformational changes in the catalytically inactive nucleotide-binding site of CFTR
    LASZLO CSANADY
    Department of Medical Biochemistry, Semmelweis University, Budapest H 1094, Hungary
    J Gen Physiol 142:61-73. 2013

Detail Information

Publications19

  1. pmc Involvement of F1296 and N1303 of CFTR in induced-fit conformational change in response to ATP binding at NBD2
    Andras Szollosi
    Department of Medical Biochemistry, Semmelweis University, Budapest, Hungary
    J Gen Physiol 136:407-23. 2010
    ....
  2. pmc Application of rate-equilibrium free energy relationship analysis to nonequilibrium ion channel gating mechanisms
    LASZLO CSANADY
    Department of Medical Biochemistry, Semmelweis University, Budapest, Hungary
    J Gen Physiol 134:129-36. 2009
    ..Additionally, REFER analysis provides limited information about the transition-state structures for gating schemes that are known to be nonequilibrium cycles...
  3. doi request reprint Electrophysiological, biochemical, and bioinformatic methods for studying CFTR channel gating and its regulation
    LASZLO CSANADY
    Department of Medical Biochemistry, Semmelweis University, Budapest, Hungary
    Methods Mol Biol 741:443-69. 2011
    ....
  4. pmc Four Ca2+ ions activate TRPM2 channels by binding in deep crevices near the pore but intracellularly of the gate
    LASZLO CSANADY
    Department of Medical Biochemistry, Semmelweis University, Budapest, Hungary
    J Gen Physiol 133:189-203. 2009
    ..Our results suggest that in intact cells that contain micromolar ADPR a single brief puff of Ca(2+) likely triggers prolonged, self-sustained TRPM2 activity...
  5. pmc Strict coupling between CFTR's catalytic cycle and gating of its Cl- ion pore revealed by distributions of open channel burst durations
    LASZLO CSANADY
    Department of Medical Biochemistry, Semmelweis University, Budapest H 1094, Hungary
    Proc Natl Acad Sci U S A 107:1241-6. 2010
    ....
  6. pmc Thermodynamics of CFTR channel gating: a spreading conformational change initiates an irreversible gating cycle
    LASZLO CSANADY
    Department of Medical Biochemistry, Semmelweis University, 1088 Budapest, Hungary
    J Gen Physiol 128:523-33. 2006
    ....
  7. pmc Preferential phosphorylation of R-domain Serine 768 dampens activation of CFTR channels by PKA
    LASZLO CSANADY
    Department of Medical Biochemistry, Semmelweis University, Budapest, Germany
    J Gen Physiol 125:171-86. 2005
    ..The observed reduced sensitivity to activation by [PKA] imparted by Ser 768 might serve to ensure activation of WT CFTR by strong stimuli while dampening responses to weak signals...
  8. pmc Functional roles of nonconserved structural segments in CFTR's NH2-terminal nucleotide binding domain
    LASZLO CSANADY
    Department of Medical Biochemistry, Semmelweis University, 1088 Budapest, Hungary
    J Gen Physiol 125:43-55. 2005
    ..In contrast, 633+668 channel function was indistinguishable from WT at both macroscopic and microscopic levels. We conclude that neither nonconserved segment is an essential element of PKA- or nucleotide-dependent regulation...
  9. pmc Mutant cycles at CFTR's non-canonical ATP-binding site support little interface separation during gating
    Andras Szollosi
    Department of Medical Biochemistry, Semmelweis University, Budapest, Hungary
    J Gen Physiol 137:549-62. 2011
    ..These results provide independent support for a gating model in which ATP-bound composite site 1 remains closed throughout the gating cycle...
  10. pmc Conformational changes in the catalytically inactive nucleotide-binding site of CFTR
    LASZLO CSANADY
    Department of Medical Biochemistry, Semmelweis University, Budapest H 1094, Hungary
    J Gen Physiol 142:61-73. 2013
    ....
  11. pmc Pore collapse underlies irreversible inactivation of TRPM2 cation channel currents
    Balazs Toth
    Department of Medical Biochemistry, Semmelweis University, Budapest H 1094, Hungary
    Proc Natl Acad Sci U S A 109:13440-5. 2012
    ..The noninactivating TRPM2 variant will be invaluable for gating studies...
  12. pmc Ca(2+)- and voltage-dependent gating of Ca(2+)- and ATP-sensitive cationic channels in brain capillary endothelium
    LASZLO CSANADY
    Department of Medical Biochemistry, Semmelweis University, Budapest, Hungary
    Biophys J 85:313-27. 2003
    ..We conclude that the biophysical properties of gating of this channel are remarkably similar to those of large-conductance Ca(2+)-activated K(+) channels...
  13. pmc Antagonistic regulation of native Ca2+- and ATP-sensitive cation channels in brain capillaries by nucleotides and decavanadate
    LASZLO CSANADY
    Department of Medical Biochemistry, Semmelweis University, and Neurochemical Group of the Hungarian Academy of Sciences, Budapest, Hungary
    J Gen Physiol 123:743-57. 2004
    ..Decavanadate now provides a valuable tool for studying native CA-NSC channels and for screening cloned channels...
  14. pmc Identification of direct and indirect effectors of the transient receptor potential melastatin 2 (TRPM2) cation channel
    Balazs Toth
    Department of Medical Biochemistry, Semmelweis University, Budapest H 1094, Hungary
    J Biol Chem 285:30091-102. 2010
    ..H(2)O(2), cADPR, and NAADP did not enhance activation by ADPR. Considering intracellular concentrations of these compounds, none of them are likely to directly affect the TRPM2 channel protein in a physiological context...
  15. pmc A novel kinetic assay of mitochondrial ATP-ADP exchange rate mediated by the ANT
    Christos Chinopoulos
    Department of Medical Biochemistry, Semmelweis University, Neurobiochemical Group, Hungarian Academy of Sciences, Szentagothai Knowledge Center, Budapest, Hungary
    Biophys J 96:2490-504. 2009
    ..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...
  16. pmc Statistical evaluation of ion-channel gating models based on distributions of log-likelihood ratios
    LASZLO CSANADY
    Department of Medical Biochemistry, Semmelweis University, and Neurochemical Group of the Hungarian Academy of Sciences, Budapest, Hungary
    Biophys J 90:3523-45. 2006
    ..These observations are explained by the distributions of DeltaLL when Xi or Xi(R) is true...
  17. doi request reprint Mitoxantrone is expelled by the ABCG2 multidrug transporter directly from the plasma membrane
    Laszlo Homolya
    Membrane Biology Research Group, Semmelweis University, Hungarian Academy of Sciences, DiĆ³szegi u 64, H 1113 Budapest, Hungary
    Biochim Biophys Acta 1808:154-63. 2011
    ..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...
  18. pmc Catalyst-like modulation of transition states for CFTR channel opening and closing: new stimulation strategy exploits nonequilibrium gating
    LASZLO CSANADY
    Department of Medical Biochemistry and 2 MTA SE Ion Channel Research Group, Semmelweis University, Budapest H 1094, Hungary
    J Gen Physiol 143:269-87. 2014
    ..Our results highlight how for CFTR, because of its unique cyclic mechanism, gating transition states determine Po and offer strategic targets for potentiator compounds to achieve maximal efficacy. ..