| Year |
Citation |
Score |
| 2014 |
Li T, Yang Y, Canessa CM. A method for activation of endogenous acid-sensing ion channel 1a (ASIC1a) in the nervous system with high spatial and temporal precision. The Journal of Biological Chemistry. 289: 15441-8. PMID 24727474 DOI: 10.1074/Jbc.M114.550012 |
0.323 |
|
| 2012 |
Li T, Yang Y, Canessa CM. Impact of recovery from desensitization on acid-sensing ion channel-1a (ASIC1a) current and response to high frequency stimulation. The Journal of Biological Chemistry. 287: 40680-9. PMID 23048040 DOI: 10.1074/Jbc.M112.418400 |
0.334 |
|
| 2011 |
Li T, Yang Y, Canessa CM. Outlines of the pore in open and closed conformations describe the gating mechanism of ASIC1. Nature Communications. 2: 399. PMID 21772270 DOI: 10.1038/Ncomms1409 |
0.363 |
|
| 2011 |
Li T, Yang Y, Canessa CM. Asp433 in the closing gate of ASIC1 determines stability of the open state without changing properties of the selectivity filter or Ca2+ block. The Journal of General Physiology. 137: 289-97. PMID 21357733 DOI: 10.1085/Jgp.201010576 |
0.378 |
|
| 2011 |
Li T, Yang Y, Canessa C. D433 Does Not Determine Ion Selectivity in ASIC1 Biophysical Journal. 100: 25a. DOI: 10.1016/J.Bpj.2010.12.343 |
0.338 |
|
| 2010 |
Li T, Yang Y, Canessa CM. Asn415 in the beta11-beta12 linker decreases proton-dependent desensitization of ASIC1. The Journal of Biological Chemistry. 285: 31285-91. PMID 20675379 DOI: 10.1074/Jbc.M110.160382 |
0.347 |
|
| 2010 |
Li T, Yang Y, Canessa CM. Leu85 in the beta1-beta2 linker of ASIC1 slows activation and decreases the apparent proton affinity by stabilizing a closed conformation. The Journal of Biological Chemistry. 285: 22706-12. PMID 20479002 DOI: 10.1074/Jbc.M110.134114 |
0.369 |
|
| 2010 |
Li T, Yang Y, Canessa CM. Two residues in the extracellular domain convert a nonfunctional ASIC1 into a proton-activated channel. American Journal of Physiology. Cell Physiology. 299: C66-73. PMID 20427715 DOI: 10.1152/Ajpcell.00100.2010 |
0.37 |
|
| 2010 |
Li T, Canessa CM. The β1-β2 Linker in the Extracellular Domain of ASIC1 Determines Desensitization of ASIC1 Biophysical Journal. 98: 702a. DOI: 10.1016/J.Bpj.2009.12.3854 |
0.327 |
|
| 2009 |
Li T, Yang Y, Canessa CM. Interaction of the aromatics Tyr-72/Trp-288 in the interface of the extracellular and transmembrane domains is essential for proton gating of acid-sensing ion channels. The Journal of Biological Chemistry. 284: 4689-94. PMID 19074149 DOI: 10.1074/Jbc.M805302200 |
0.351 |
|
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