Laszlo Csanady, Ph.D.
Affiliations: | 2000 | Rockefeller University, New York, NY, United States |
Area:
General Biophysics, Biochemistry, Neuroscience BiologyGoogle:
"Laszlo Csanady"Mean distance: 53433
Parents
Sign in to add mentor| David C. Gadsby | grad student | 2000 | Rockefeller | |
| (Structure-function studies on human epithelial cystic fibrosis chloride channels expressed in Xenopus laevis oocytes.) | ||||
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Publications
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| Bartók Á, Csanády L. (2024) TRPM2 - An adjustable thermostat. Cell Calcium. 118: 102850 |
| Simon MA, Iordanov I, Szollosi A, et al. (2023) Estimating the true stability of the prehydrolytic outward-facing state in an ABC protein. Elife. 12 |
| Csanády L. (2023) Blue flash sheds light on the roles of individual phosphoserines in CFTR channel activation. The Journal of General Physiology. 155 |
| Simon MA, Csanády L. (2023) Optimization of CFTR gating through the evolution of its extracellular loops. The Journal of General Physiology. 155 |
| Bartók Á, Csanády L. (2022) Dual amplification strategy turns TRPM2 channels into supersensitive central heat detectors. Proceedings of the National Academy of Sciences of the United States of America. 119: e2212378119 |
| Simon MA, Csanády L. (2021) Molecular pathology of the R117H cystic fibrosis mutation is explained by loss of a hydrogen bond. Elife. 10 |
| Csanády L. (2021) Degenerate but indispensable: How CFTR channel activity depends on the catalytically inactive ATP binding site. The Journal of Physiology. 599: 4523-4524 |
| Mihályi C, Iordanov I, Töröcsik B, et al. (2020) Simple binding of protein kinase A prior to phosphorylation allows CFTR anion channels to be opened by nucleotides. Proceedings of the National Academy of Sciences of the United States of America |
| Tóth B, Iordanov I, Csanády L. (2020) Selective profiling of N- and C-terminal nucleotide-binding sites in a TRPM2 channel. The Journal of General Physiology. 152 |
| Csanády L, Du J, Zubcevic L. (2020) Decision letter: Global alignment and assessment of TRP channel transmembrane domain structures to explore functional mechanisms Elife |