Area of research
Physiology · Molecular Biology
Research interest
Research interests include Biology, Neuropathic pain, Sodium channel, Medicine, Voltage-dependent calcium channel, and Neuropilin 1.
C2230, a preferential use- and state-dependent CaV2.2 channel blocker, mitigates pain behaviors across multiple pain models
Identification and targeting of a unique Na <sub>V</sub> 1.7 domain driving chronic pain
A peptidomimetic modulator of the Ca <sub>V</sub> 2.2 N-type calcium channel for chronic pain
Breast cancer therapies reduce risk of Alzheimer’s disease and promote estrogenic pathways and action in brain
Targeting the vascular endothelial growth factor A/neuropilin 1 axis for relief of neuropathic pain
The natural product argentatin C attenuates postoperative pain via inhibition of voltage‐gated sodium and T‐type voltage‐gated calcium channels
Selective targeting of NaV1.7 via inhibition of the CRMP2-Ubc9 interaction reduces pain in rodents
Novel Compounds Targeting Neuropilin Receptor 1 with Potential To Interfere with SARS-CoV-2 Virus Entry
Antihypertensive drug treatment and susceptibility to SARS-CoV-2 infection in human PSC-derived cardiomyocytes and primary endothelial cells
SARS-CoV-2 spike protein co-opts VEGF-A/neuropilin-1 receptor signaling to induce analgesia
The role of cyclin-dependent kinase 5 in neuropathic pain
Druggability of CRMP2 for Neurodegenerative Diseases
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
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
(S)-Lacosamide Binding to Collapsin Response Mediator Protein 2 (CRMP2) Regulates CaV2.2 Activity by Subverting Its Phosphorylation by Cdk5