Targeted transcriptional upregulation of SENP1 by CRISPR activation enhances deSUMOylation pathways to elicit antinociception in the spinal nerve ligation model of neuropathic pain. [PDF]
Gomez K +9 more
europepmc +1 more source
The Human Lens Fiber Cytoskeletome Reveals Neuronal Signatures and the Presence of Chaperonins, Proteasome, Signaling, and Redox Regulators. [PDF]
Maddala R +3 more
europepmc +1 more source
Evaluation of an indirect Na<sub>V</sub>1.7 inhibitor as adjunctive analgesic in burn-related neuropathic pain in a cat. [PDF]
Chiavaccini L +5 more
europepmc +1 more source
Intranasal CRMP2-Ubc9 inhibitor regulates Na V 1.7 to alleviate trigeminal neuropathic pain. [PDF]
Loya-Lopez SI +11 more
europepmc +1 more source
The Duality of Cdk5: A Master Regulator in Neurodevelopment and a Hijacked Oncogene in Cancer. [PDF]
Nishimura YV, Kawauchi T.
europepmc +1 more source
Decoding orofacial pain: a translational review of mechanisms and novel therapies. [PDF]
Kang Y, Fu Y, Jian K, Liu J, Shao L.
europepmc +1 more source
Chemical shift perturbation mapping of the Ubc9-CRMP2 interface identifies a pocket in CRMP2 amenable for allosteric modulation of Nav1.7 channels [PDF]
Drug discovery campaigns directly targeting the voltage-gated sodium channel NaV1.7, a highly prized target in chronic pain, have not yet been clinically successful. In a differentiated approach, we demonstrated allosteric control of trafficking and activity of NaV1.7 by prevention of SUMOylation of collapsin response mediator protein 2 (CRMP2). Spinal
Liberty Francois-Moutal +2 more
exaly +4 more sources
Phosphorylated CRMP2 Regulates Spinal Nociceptive Neurotransmission [PDF]
The collapsin response mediator protein 2 (CRMP2) has emerged as a central node in assembling nociceptive signaling complexes involving voltage-gated ion channels. Concerted actions of post-translational modifications, phosphorylation and SUMOylation, of CRMP2 contribute to regulation of pathological pain states.
Aubin Moutal +2 more
exaly +3 more sources
CRMP2 Protein SUMOylation Modulates NaV1.7 Channel Trafficking [PDF]
Voltage-gated sodium channel (NaV) trafficking is incompletely understood. Post-translational modifications of NaVs and/or auxiliary subunits and protein-protein interactions have been posited as NaV-trafficking mechanisms. Here, we tested if modification of the axonal collapsin response mediator protein 2 (CRMP2) by a small ubiquitin-like modifier ...
Erik T Dustrude +2 more
exaly +3 more sources

