Results 31 to 40 of about 793,047 (255)

Scorpion Toxin, BmP01, Induces Pain by Targeting TRPV1 Channel

open access: yesToxins, 2015
The intense pain induced by scorpion sting is a frequent clinical manifestation. To date, there is no established protocol with significant efficacy to alleviate the pain induced by scorpion envenomation.
Md Abdul Hakim   +6 more
doaj   +1 more source

Quantification of the emetic toxin cereulide in food products by liquid chromatography-mass spectrometry using synthetic cereulide as a standard [PDF]

open access: yes, 2010
Bacillus cereus produces the emetic toxin cereulide, a cyclic dodecadepsipeptide that can act as a K+ ionophore, dissipating the transmembrane potential in mitochondria of eukaryotic cells.
de Veld, P.   +21 more
core   +1 more source

Peptide isolated from Cry1Ab16 toxin present in Bacillus thuringiensis: Synthesis and morphology data for layer-by-layer films studied by atomic force microscopy

open access: yesData in Brief, 2016
The peptide PcL342-354C was obtained from the Cry1Ab16 toxin present in Bacillus thuringiensis (“Computational Modeling Deduced Three Dimensional Structure of Cry1Ab16 Toxin from B. thuringiensis AC11” (Kashyap, 2012) [1]).
Alexandra Plácido   +5 more
doaj   +1 more source

The light chain of tetanus toxin inhibits calcium-dependent vasopressin release from permeabilized nerve endings [PDF]

open access: yes, 1992
The effects of tetanus toxin and its light and heavy chain subunits on vasopressin release were investigated in digitonin-permeabilized neurosecretory nerve terminals isolated from the neural lobe of the rat pituitary gland.
Weller, U.   +5 more
core   +1 more source

Comparative analysis of antimicrobial activities of valinomycin and cereulide, the Bacillus cereus emetic toxin [PDF]

open access: yes, 2011
Cereulide and valinomycin are highly similar cyclic dodecadepsipeptides with potassium ionophoric properties. Cereulide, produced by members of the Bacillus cereus group, is known mostly as emetic toxin, and no ecological function has been assigned.
Marcel H. Tempelaars   +5 more
core   +1 more source

Exploring the functional domain and the target of the tetanus toxin light chain in neurohypophysial terminals [PDF]

open access: yes, 1994
The tetanus toxin light chain blocks calcium induced vasopressin release from neurohypophysial nerve terminals. Here we show that histidine residue 233 within the putative zinc binding motif of the tetanus toxin light chain is essential for the ...
Weller, U.   +7 more
core   +1 more source

A novel RRGW derived peptide is a promising inhibitor of BoNT/A

open access: yesJournal of Enzyme Inhibition and Medicinal Chemistry, 2023
Clostridium botulinum neurotoxin type A (BoNT/A) is one of the most potent biotoxins ever known. Its entry into neurons could block vesicle exocytosis to abolish the release of neurotransmitters from nerve terminals, thus leading to muscle paralysis ...
Wantong Ma   +10 more
doaj   +1 more source

Clostridium perfringensepsilon toxin H149A mutant as a platform for receptor binding studies [PDF]

open access: yes, 2013
Clostridium perfringens epsilon toxin (Etx) is a pore-forming toxin responsible for a severe and rapidly fatal enterotoxemia of ruminants. The toxin is classified as a category B bioterrorism agent by the U.S.
Titball, R.W.   +21 more
core   +1 more source

Binding of κ-Conotoxin-PVIIA to Open and Closed Shaker K-Channels Are Differentially Affected by the Ionic Strength

open access: yesMarine Drugs, 2020
κ-Conotoxin-PVIIA (κ-PVIIA) is a potassium-channel blocking peptide from the venom of the fish-hunting snail, Conus purpurascens, which is essential for quick prey’s excitotoxic immobilization.
David Naranjo, Ignacio Díaz-Franulic
doaj   +1 more source

Identification of a peptide motif that potently inhibits two functionally distinct subunits of Shiga toxin

open access: yesCommunications Biology, 2021
Watanabe-Takahashi, Tamada, Senda et al. identify a tetravalent peptide that inhibits Shiga toxin (Stx), a major virulence factor of enterohemorrhagic Escherichia coli, by targeting its receptor-binding.
Miho Watanabe-Takahashi   +8 more
doaj   +1 more source

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