alpha M-Conotoxin MIIIJ Blocks Nicotinic Acetylcholine Receptors at Neuromuscular Junctions of Frog and Fish

Autor: Layla Azam, J. Michael McIntosh, Henrik O'Brien, Helena Safavi-Hemami, Baldomero M. Olivera, Matthew J Rybin, Doju Yoshikami, Iris Bea L Ramiro

Publikováno v: Rybin, M J, O'Brien, H, Ramiro, I B L, Azam, L, McIntosh, J M, Olivera, B M, Safavi-Hemami, H & Yoshikami, D 2020, ' alpha M-Conotoxin MIIIJ Blocks Nicotinic Acetylcholine Receptors at Neuromuscular Junctions of Frog and Fish ', Toxins, vol. 12, no. 3, 197 . https://doi.org/10.3390/toxins12030197
Toxins, Vol 12, Iss 3, p 197 (2020)
Toxins
Volume 12
Issue 3

We report the discovery and functional characterization of &alpha
M-Conotoxin MIIIJ, a peptide from the venom of the fish-hunting cone snail Conus magus. Injections of &alpha
M-MIIIJ induced paralysis in goldfish (Carassius auratus) but not

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9323ae1ad9ca9df52c1819854485d148
https://curis.ku.dk/ws/files/247214469/OA_M_Conotoxin_MIIIJ_Blocks_Nicotinic_Acetylcholine.pdf

Probing the Redox States of Sodium Channel Cysteines at the Binding Site of μO§-Conotoxin GVIIJ

Autor: Grzegorz Bulaj, Doju Yoshikami, Baldomero M. Olivera, Joanna Gajewiak, Min Min Zhang, Layla Azam

Publikováno v: Biochemistry. 54:3911-3920

μO§-Conotoxin GVIIJ is a 35-amino acid peptide that readily blocks six of eight tested NaV1 subunit isoforms of voltage-gated sodium channels. μO§-GVIIJ is unusual in having an S-cysteinylated cysteine (at residue 24). A proposed reaction scheme

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::38d02d27003382cf6b76bee1ea2d3c5a
https://doi.org/10.1021/acs.biochem.5b00390

A disulfide tether stabilizes the block of sodium channels by the conotoxin μO§-GVIIJ

Autor: Grzegorz Bulaj, Pradip K. Bandyopadhyay, Yi Liu, Shrinivasan Raghuraman, Baldomero M. Olivera, Layla Azam, Natali A. Minassian, Marshall Bern, Beatrix Ueberheide, Rebecca Hagan, H. Mimi Zhou, Brad R. Green, Julita S. Imperial, Doju Yoshikami, Alan D. Wickenden, Aleksandra Walewska, Joanna Gajewiak, Min Min Zhang, Mack Flinspach

Publikováno v: Proceedings of the National Academy of Sciences. 111:2758-2763

A cone snail venom peptide, μO§-conotoxin GVIIJ from Conus geographus, has a unique posttranslational modification, S-cysteinylated cysteine, which makes possible formation of a covalent tether of peptide to its target Na channels at a distinct lig

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e16aa93a382b2f4eabc990179cc3ecc5
https://doi.org/10.1073/pnas.1324189111

Co-expression of NaVβ subunits alters the kinetics of inhibition of voltage-gated sodium channels by pore-blocking μ-conotoxins

Autor: Doju Yoshikami, Baldomero M. Olivera, Jean Rivier, Joanna Gajewiak, Grzegorz Bulaj, Layla Azam, Michael J. Wilson, Min Min Zhang

Publikováno v: British Journal of Pharmacology. 168:1597-1610

Background and Purpose Voltage-gated sodium channels (VGSCs) are assembled from two classes of subunits, a pore-bearing α-subunit (NaV1) and one or two accessory β-subunits (NaVβs). Neurons in mammals can express one or more of seven isoforms of N

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::95dcb57c3b37ec5b3fb96785c7225000
https://doi.org/10.1111/bph.12051

μ-Conotoxins that differentially block sodium channels Na V 1.1 through 1.8 identify those responsible for action potentials in sciatic nerve

Autor: Min Min Zhang, Layla Azam, Baldomero M. Olivera, Michael J. Wilson, Joanna Gajewiak, Doju Yoshikami, Grzegorz Bulaj

Publikováno v: Proceedings of the National Academy of Sciences. 108:10302-10307

Voltage-gated sodium channels (VGSCs) are important for action potentials. There are seven major isoforms of the pore-forming and gate-bearing α-subunit (Na V 1) of VGSCs in mammalian neurons, and a given neuron can express more than one isoform. Fi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::651a93ccb661cd6dfb42785e257f45c9
https://doi.org/10.1073/pnas.1107027108