TRP channel activation by reversible covalent modification

By Andrew Hinman, H. Chuang, D. Bautista, D. Julius. Proceedings of the National Academy of Sciences of the United States of America, 2006

879 citations recorded by the source corpus.

Subfields: Biochemistry, Plant Science, Sensory Systems

View Paper: https://www.semanticscholar.org/paper/50483cea5f8c65feb9565c5fd6a7ecab8ee16b1c

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Biochemistry

1. D. Julius
2. A. Dinkova-Kostova

In Plant Science

1. Ardem Patapoutian

In Sensory Systems

1. D. Julius
2. Ardem Patapoutian
3. Clifford J. Woolf
4. S. Bevan
5. D. Andersson
6. C. Gentry
7. Sian Moss
8. S. Tate

Citations in the corpus

• TRP channels and pain. (2013, background): “…the ankyrin-rich domain to the transmembrane core; mutation of all three residues renders the channel insensitive to activation by isothiocyanates, except at very high (>100 μM) concentrations, where modification of a nearby lysine elicits small and persistent responses (Hinman et al. 2006).”
• Transient receptor potential channels: targeting pain at the source (2009, background): “Such pungent compounds are all electrophiles that activate TRPA1 through covalent modification of reactive amino acids such as cysteine”
• Transient Receptor Potential A1 Is a Sensory Receptor for Multiple Products of Oxidative Stress (2008, positive): “Site directed mutagenesis studies have shown that allyl isothiocyanate (AITC), cinnamaldehyde and acrolein activate TRPA1 by covalently reacting with cysteine residues in the cytoplasmic N terminus of the channel (Hinman et al., 2006; Macpherson et al., 2007a).”
• TRP Channels (2012, neutral): “1) (146a, 252a).”
• Cellular and Molecular Mechanisms of Pain (2009, neutral): “For example, allyl isothiocyanate (from wasabi) or allicin (from garlic) are membrane permeable electrophiles that activate TRPA1 by covalently modifying cysteine residues within the amino-terminal cytoplasmic domain of the channel (Hinman et al., 2006; Macpherson et al., 2007).”
• Oxidative Stress in Cancer (2020, background): “Within human TRPA1, Cys-414, Cys-421, Cys-621, Cys-641, and Cys-665 contribute to regulation of the channel by electrophiles (Hinman et al., 2006; Macpherson et al., 2007).”