All Outputs (3)

New Insights Into Refractory Chronic Cough and Unexplained Chronic Cough: A 6-Year Ambispective Cohort Study (2023)
Journal Article
Zhang, M., Morice, A. H., Si, F., Zhang, L., Chen, Q., Wang, S., Zhu, Y., Xu, X., Yu, L., & Qiu, Z. (2023). New Insights Into Refractory Chronic Cough and Unexplained Chronic Cough: A 6-Year Ambispective Cohort Study. Allergy Asthma and Immunology Research, 15(6), 795-811. https://doi.org/10.4168/aair.2023.15.6.795

Purpose: Only limited studies have depicted the unique features and management of refractory chronic cough (RCC) and unexplained chronic cough (UCC). These led to the initiation of this study, which reported the demographic characteristics, manifesta... Read More about New Insights Into Refractory Chronic Cough and Unexplained Chronic Cough: A 6-Year Ambispective Cohort Study.

N-cinnamoylanthranilates as human TRPA1 modulators: Structure-activity relationships and channel binding sites (2019)
Journal Article
Chandrabalan, A., McPhillie, M. J., Morice, A. H., Boa, A. N., & Sadofsky, L. R. (2019). N-cinnamoylanthranilates as human TRPA1 modulators: Structure-activity relationships and channel binding sites. European Journal of Medicinal Chemistry, 170, 141-156. https://doi.org/10.1016/j.ejmech.2019.02.074

The transient receptor potential ankyrin 1 (TRPA1) channel is a non-selective cation channel, which detects noxious stimuli leading to pain, itch and cough. However, the mechanism(s) of channel modulation by many of the known, non-reactive modulators... Read More about N-cinnamoylanthranilates as human TRPA1 modulators: Structure-activity relationships and channel binding sites.

TRPA1 is activated by direct addition of cysteine residues to the N-hydroxysuccinyl esters of acrylic and cinnamic acids (2010)
Journal Article
Sadofsky, L. R., Boa, A. N., Maher, S. A., Birrell, M. A., Belvisi, M. G., & Morice, A. H. (2011). TRPA1 is activated by direct addition of cysteine residues to the N-hydroxysuccinyl esters of acrylic and cinnamic acids. Pharmacological research : the official journal of the Italian Pharmacological Society, 63(1), 30-36. https://doi.org/10.1016/j.phrs.2010.11.004

The nociceptor TRPA1 is thought to be activated through covalent modification of specific cysteine residues on the N terminal of the channel. The precise mechanism of covalent modification with unsaturated carbonyl-containing compounds is unclear, th... Read More about TRPA1 is activated by direct addition of cysteine residues to the N-hydroxysuccinyl esters of acrylic and cinnamic acids.