Results 21 to 30 of about 183,535 (259)

Isolation and cDNA cloning of four peptide toxins from the sea anemone Heteractis aurora [PDF]

open access: yesJournal of Venomous Animals and Toxins including Tropical Diseases
Background: Sea anemones are well known to contain multiple peptide toxins. However, of more than 1100 species of sea anemones distributed worldwide, only a little over 50 have been studied for peptide toxins.
Tomohiro Homma   +3 more
doaj   +1 more source

Structure-Based Prototype Peptides Targeting the Pseudomonas aeruginosa Type VI Secretion System Effector as a Novel Antibacterial Strategy

open access: yesFrontiers in Cellular and Infection Microbiology, 2017
The type VI secretion system (T6SS) secretes numerous toxins for bacteria-bacteria competition. TplE is a newly identified trans-kingdom toxin secreted by the T6SS in Pseudomonas aeruginosa, while TplEi neutralizes the toxic effect of TplE to protect ...
Xiaopan Gao   +4 more
doaj   +1 more source

Structure of the voltage-gated potassium channel KV1.3: Insights into the inactivated conformation and binding to therapeutic leads

open access: yesChannels, 2023
The voltage-gated potassium channel KV1.3 is an important therapeutic target for the treatment of autoimmune and neuroinflammatory diseases. The recent structures of KV1.3, Shaker-IR (wild-type and inactivating W434F mutant) and an inactivating mutant of
K. George Chandy   +2 more
doaj   +1 more source

Peptide Toxins in Solitary Wasp Venoms [PDF]

open access: yesToxins, 2016
Solitary wasps paralyze insects or spiders with stinging venom and feed the paralyzed preys to their larva. Accordingly, the venoms should contain a variety of constituents acting on nervous systems. However, only a few solitary wasp venoms have been chemically studied despite thousands of species inhabiting the planet.
Katsuhiro Konno   +2 more
openaire   +3 more sources

Assembling an arsenal, the scorpion way

open access: yesBMC Evolutionary Biology, 2008
Background For survival, scorpions depend on a wide array of short neurotoxic polypeptides. The venoms of scorpions from the most studied group, the Buthida, are a rich source of small, 23–78 amino acid-long peptides, well packed by either three or four ...
Mishmar Dan   +3 more
doaj   +1 more source

Toxins and antimicrobial peptides: interactions with membranes [PDF]

open access: yesSPIE Proceedings, 2009
The innate immunity to pathogenic invasion of organisms in the plant and animal kingdoms relies upon cationic antimicrobial peptides (AMPs) as the first line of defense. In addition to these natural peptide antibiotics, similar cationic peptides, such as the bee venom toxin melittin, act as nonspecific toxins. Molecular details of AMP and peptide toxin
Diana E, Schlamadinger   +2 more
openaire   +2 more sources

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

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

Cyclotides: Disulfide-rich peptide toxins in plants [PDF]

open access: yesToxicon, 2019
Cyclotides are a plant-derived family of peptides that comprise approximately 30 amino acid residues, a cyclic backbone and a cystine knot. Due to their unique structure, cyclotides are exceptionally stable to heat or proteolytic degradation and are tolerant to amino acid substitutions in their backbone loops between conserved cysteine residues.
Yen-Hua Huang   +2 more
openaire   +5 more sources

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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