Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Conus ventricosus

ABSTRACT: Lautoconus ventricosus genome sequencing and assembly

PROVIDER: PRJNA678883 | ENA |

REPOSITORIES: ENA

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
		Other
	SRR13757741_1.fastq.gz	Fastqsanger.gz
	SRR13757741_2.fastq.gz	Fastqsanger.gz
	SRR13740844_1.fastq.gz	Fastqsanger.gz
	SRR13740844_2.fastq.gz	Fastqsanger.gz

Items per page:

1 - 5 of 11

Similar Datasets

Conus ventricosus

Project description:Conus ventricosus overview

| PRJNA982225 | ENA

Conus ventricosus

Project description:Conus ventricosus low coverage genome raw sequence reads

| PRJNA856832 | ENA

Araneus ventricosus

Project description:Araneus ventricosus draft genome

| PRJDB7092 | ENA

Ophion ventricosus

Project description:Ophion ventricosus overview

| PRJNA1073659 | ENA

Araneus ventricosus

Project description:Araneus ventricosus overview

| PRJNA553601 | ENA

Araneus ventricosus

Project description:Araneus ventricosus Transcriptome or Gene expression

| PRJNA636258 | ENA

Argopecten ventricosus

Project description:Modulatory effect of Homeopathic complexes on the microbiota associated with TGI Catarina Scallop (Argopecten ventricosus = circularis)

| PRJNA341370 | ENA

α-Conotoxin VnIB from Conus ventricosus is a potent and selective antagonist of α6β4* nicotinic acetylcholine receptors.

Project description:α6-containing (α6*) nicotinic acetylcholine receptors (nAChRs) are expressed throughout the periphery and the central nervous system and constitute putative therapeutic targets in pain, addiction and movement disorders. The α6β2* nAChRs are relatively well studied, in part due to the availability of target specific α-conotoxins (α-Ctxs). In contrast, all native α-Ctxs identified that potently block α6β4 nAChRs exhibit higher potencies for the closely related α6β2β3 and/or α3β4 subtypes. In this study, we have identified a novel peptide from Conus ventricosus with pronounced selectivity for the α6β4 nAChR. The peptide-encoding gene was cloned from genomic DNA and the predicted mature peptide, α-Ctx VnIB, was synthesized. The functional properties of VnIB were characterized at rat and human nAChRs expressed in Xenopus oocytes by two-electrode voltage clamp electrophysiology. VnIB potently inhibited ACh-evoked currents at rα6β4 and rα6/α3β4 nAChRs, displayed ∼20-fold and ∼250-fold lower potencies at rα3β4 and rα6/α3β2β3 receptors, respectively, and exhibited negligible effects at eight other nAChR subtypes. Interestingly, even higher degrees of selectivity were observed for hα6/α3β4 over hα6/α3β2β3 and hα3β4 receptors. Finally, VnIB displayed fast binding kinetics at rα6/α3β4 (on-rate t½ = 0.87 min-1, off-rate t½ = 2.7 min-1). The overall preference of VnIB for β4* over β2* nAChRs is similar to the selectivity profiles of other 4/6 α-Ctxs. However, in contrast to previously identified native α-Ctxs targeting α6* nAChRs, VnIB displays pronounced selectivity for α6β4 nAChRs over both α3β4 and α6β2β3 receptors. VnIB thus represents a novel molecular probe for elucidating the physiological role and therapeutic properties of α6β4* nAChRs.

| S-EPMC6693646 | biostudies-literature

Conus consors

Project description:Conus consors Genome sequencing and assembly

| PRJNA267645 | ENA

Conus tribblei

Project description:Conus tribblei Genome sequencing and assembly

| PRJNA285711 | ENA