Area of research
Physiology · Cellular and Molecular Neuroscience
Research interest
Research focused on Dorsal root ganglion and Sodium channel, with related work in NAV1, Pharmacology, Nociception. Notable publications include 'Structural Insights Into TDP-43 and Effects of Post-translational Modifications', 'A membrane-delimited N-myristoylated CRMP2 peptide aptamer inhibits CaV2.2 trafficking and reverses inflammatory and postoperative pain behaviors', and 'CRISPR/Cas9 editing of Nf1 gene identifies CRMP2 as a therapeutic target in neurofibromatosis type 1-related pain that is reversed by (S)-Lacosamide'.
Nociceptors are functionally male or female: from mouse to monkey to man
Identification and targeting of a unique Na <sub>V</sub> 1.7 domain driving chronic pain
Heat shock protein Grp78/BiP/HspA5 binds directly to TDP-43 and mitigates toxicity associated with disease pathology
Selective targeting of NaV1.7 via inhibition of the CRMP2-Ubc9 interaction reduces pain in rodents
<i>In Silico</i> Targeting of the Long Noncoding RNA MALAT1
Direct targeting of TDP-43, from small molecules to biologics: the therapeutic landscape
An Allosteric Modulator of RNA Binding Targeting the N-Terminal Domain of TDP-43 Yields Neuroprotective Properties
Structural Insights Into TDP-43 and Effects of Post-translational Modifications
Small Molecule Targeting TDP-43’s RNA Recognition Motifs Reduces Locomotor Defects in a <i>Drosophila</i> Model of Amyotrophic Lateral Sclerosis (ALS)
The Natural Flavonoid Naringenin Elicits Analgesia through Inhibition of NaV1.8 Voltage-Gated Sodium Channels
Targeting the CaVα–CaVβ interaction yields an antagonist of the N-type CaV2.2 channel with broad antinociceptive efficacy
Inhibition of the Ubc9 E2 SUMO-conjugating enzyme–CRMP2 interaction decreases NaV1.7 currents and reverses experimental neuropathic pain
CRISPR/Cas9 editing of Nf1 gene identifies CRMP2 as a therapeutic target in neurofibromatosis type 1-related pain that is reversed by (S)-Lacosamide
Homology‐guided mutational analysis reveals the functional requirements for antinociceptive specificity of collapsin response mediator protein 2‐derived peptides
A single structurally conserved SUMOylation site in CRMP2 controls NaV1.7 function
A membrane-delimited N-myristoylated CRMP2 peptide aptamer inhibits CaV2.2 trafficking and reverses inflammatory and postoperative pain behaviors
(S)-Lacosamide Binding to Collapsin Response Mediator Protein 2 (CRMP2) Regulates CaV2.2 Activity by Subverting Its Phosphorylation by Cdk5