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J Pharm Anal 2020 Apr 13;10(2):157-163. Epub 2019 Dec 13.

Department of Chemistry and Biochemistry, South Dakota State University, Box 2202, Brookings, SD, 57007, USA.

The noxious effects from exposure to toxic inhalation hazards (TIHs, such as isocyanates, chlorine, etc.) are known to be triggered by the activation of transient receptor potential ankyrin 1 (TRPA1) ion channel. Antagonists of TRPA1 have shown near complete attenuation of the noxious effects from TIH exposure. Read More

Beilstein J Org Chem 2020 9;16:337-350. Epub 2020 Mar 9.

Laboratory of Organic, Bioorganic and Natural Product Chemistry, Molecular Biology and Genetics Department, Democritus University of Thrace, University Campus, Dragana, 68100, Alexandroupolis, Greece.

A number of -pyridinyl oxime carbamate derivatives were prepared upon the reaction of the corresponding oximes with isocyanates. These novel compounds reacted photochemically in the presence of supercoiled plasmid DNA. Structure-activity relationship (SAR) studies revealed that the substituent on the imine group was not affecting the extend of the DNA damage, whereas the substituent of the carbamate group was critical, with the halogenated derivatives to be able to cause extensive single and double stranded DNA cleavages, acting as "synthetic nucleases", independently of oxygen and pH. Read More

Proc Natl Acad Sci U S A 2019 12 3;116(51):26008-26019. Epub 2019 Dec 3.

Biochemical and Cellular Pharmacology, Genentech, Inc., South San Francisco, CA 94080;

The transient receptor potential ankyrin 1 (TRPA1) channel functions as an irritant sensor and is a therapeutic target for treating pain, itch, and respiratory diseases. As a ligand-gated channel, TRPA1 can be activated by electrophilic compounds such as allyl isothiocyanate (AITC) through covalent modification or activated by noncovalent agonists through ligand binding. However, how covalent modification leads to channel opening and, importantly, how noncovalent binding activates TRPA1 are not well-understood. Read More

Biosci Rep 2019 09 20;39(9). Epub 2019 Sep 20.

School of Biological Sciences, National Institute of Science Education and Research, HBNI, Bhubaneswar, Jatni, Khurda 752050, Odisha, India

Transient receptor potential channel subfamily A member 1 (TRPA1) is a non-selective cationic channel, identified initially as a cold sensory receptor. TRPA1 responds to diverse exogenous and endogenous stimuli associated with pain and inflammation. However, the information on the role of TRPA1 toward T-cell responses remains scanty. Read More

J Pharmacol Exp Ther 2017 09 15;362(3):368-377. Epub 2017 Jun 15.

Department of Integrative Physiology and Neuroscience, Washington State University, Pullman, Washington (D.K.F., F.J.S., J.E.M.L., J.H.P.); and Department of Neuroscience, The Scripps Research Institute, Jupiter, Florida (S.-w.W.).

The nonselective cation channel transient receptor potential ankryn subtype family 1 (TRPA1) is expressed in neurons of dorsal root ganglia and trigeminal ganglia and also in vagal afferent neurons that innervate the lungs and gastrointestinal tract. Many TRPA1 agonists are reactive electrophilic compounds that form covalent adducts with TRPA1. Allyl isothiocyanate (AITC), the common agonist used to identify TRPA1, contains an electrophilic group that covalently binds with cysteine residues of TRPA1 and confers a structural change on the channel. Read More