Results 81 to 90 of about 3,374 (156)

Key structural determinants in the agonist binding loops of human β2 and β4 nicotinic acetylcholine receptor subunits contribute to α3β4 subtype selectivity of α-conotoxins

open access: yes, 2016
α-Conotoxins represent a large group of pharmacologically active peptides that antagonize nicotinic acetylcholine receptors (nAChRs). The α3β4 nAChR, a predominant subtype in the peripheral nervous system, has been implicated in various ...
Han Shen Tae (19586293)   +4 more
core  

Protein engineering strategies to optimise recombinant product synthesis and accumulation in Nicotiana benthamiana

open access: yesPlant Biotechnology Journal, Volume 24, Issue 1, Page 31-43, January 2026.
Summary In plant molecular farming, recombinant products include traditional protein targets, such as antibodies, antigens, and enzymes, but also increasingly refers to high‐value peptides, and small molecules produced by heterologous enzymatic pathways.
Maxim D. Harding, Frank Sainsbury
wiley   +1 more source

NMR structures of conotoxins [PDF]

open access: yes, 1996
journal articleThis review discusses the methodology, structural details, and biological implications regarding NMR structures of conotoxins. NMR and molecular modeling techniques have improved to the point that three-dimensional structures of conotoxins
Mitchell, Scott S.; Shon, Ki Joon   +1 more
core  

Physico-chemical characterization and synthesis of neuronally active alpha-conotoxins

open access: yes, 2004
The high speciFIcity of alpha-conotoxins for different neuronal nicotinic acetylcholine receptors makes them important probes for dissecting receptor subtype selectivity. New sequences continue to expand the diversity and utility of the pool of available
Loughnan, M. L., Alewood, P. F.
core   +1 more source

Predicting Structural Details of the Sodium Channel Pore Basing on Animal Toxin Studies

open access: yesFrontiers in Pharmacology, 2018
Eukaryotic voltage-gated sodium channels play key roles in physiology and are targets for many toxins and medically important drugs. Physiology, pharmacology, and general architecture of the channels has long been the subject of intensive research in ...
Denis B. Tikhonov   +2 more
doaj   +1 more source

Conotoxins That Could Provide Analgesia through Voltage Gated Sodium Channel Inhibition

open access: yesToxins, 2015
Chronic pain creates a large socio-economic burden around the world. It is physically and mentally debilitating, and many suffers are unresponsive to current therapeutics.
Nehan R. Munasinghe   +1 more
doaj   +1 more source

Venom Diversity and Evolution in the Most Divergent Cone Snail Genus Profundiconus

open access: yesToxins, 2019
Profundiconus is the most divergent cone snail genus and its unique phylogenetic position, sister to the rest of the family Conidae, makes it a key taxon for examining venom evolution and diversity. Venom gland and foot transcriptomes of Profundiconus cf.
Giulia Fassio   +8 more
doaj   +1 more source

T-superfamily of conotoxins [PDF]

open access: yes, 1999
journal articleWe report the discovery and initial characterization of the T-superfamily of conotoxins. Eight different T-superfamily peptides from five Conus species were identified; they share a consensus signal sequence, and a conserved ...
Walker, Craig S.; Steel, Douglas; Jacobsen, Richard B.; Lirazan, Marcelina B.; Cruz, Lourdes J.; Hooper, David; Shetty, Reshma; DelaCruz, Richard C.; Nielsen, Jacob S.; Zhou, Li Ming; Bandyopadhyay, Pradip; Craig, A. Grey   +1 more
core  

Structure/activity relationship of alpha-conotoxins targeting GABAB receptor

open access: yes, 2011
Conotoxins are small disulfide rich peptides derived from the venom of Cone snails. They target different receptors in the nervous system with high selectivity and potency making them valuable as drug leads or drug themselves.
Køller, Katrine Sperstad
core  

Comparison of Teretoxin Tv1 and known M superfamily Conotoxins.

open access: yes, 2014
Comparison of Teretoxin Tv1 and known M superfamily Conotoxins.
Victoria Russell (446089)   +9 more
core   +1 more source

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