Results 1 to 10 of about 260,045 (204)

Pharmacokinetics of Toxin-Derived Peptide Drugs [PDF]

open access: yesToxins, 2018
Toxins and venoms produced by different organisms contain peptides that have evolved to have highly selective and potent pharmacological effects on specific targets for protection and predation.
David Stepensky
doaj   +5 more sources

Water Thermodynamics of Peptide Toxin Binding Sites on Ion Channels [PDF]

open access: yesToxins, 2020
Peptide toxins isolated from venomous creatures, long prized as research tools due to their innate potency for ion channels, are emerging as drugs as well.
Binita Shah   +3 more
doaj   +2 more sources

Antibacterial and Anti-Inflammatory Effects of Novel Peptide Toxin from the Spider Pardosa astrigera [PDF]

open access: yesAntibiotics, 2020
The prevalence of antibiotic-resistant bacteria has become an immediate threat to public health. Antimicrobial peptides are attracting attention as a new source of antibiotics due to their ability to prevent drug-resistances with fewer side effects ...
Min Kyoung Shin   +8 more
doaj   +2 more sources

PhcrTx2, a New Crab-Paralyzing Peptide Toxin from the Sea Anemone Phymanthus crucifer [PDF]

open access: yesToxins, 2018
Sea anemones produce proteinaceous toxins for predation and defense, including peptide toxins that act on a large variety of ion channels of pharmacological and biomedical interest. Phymanthus crucifer is commonly found in the Caribbean Sea; however, the
Armando Alexei Rodríguez   +12 more
doaj   +2 more sources

Mycoplasma pneumoniae CARDS toxin elicits a functional IgE response in Balb/c mice. [PDF]

open access: yesPLoS ONE, 2017
Mycoplasma pneumoniae is strongly associated with new onset asthma and asthma exacerbations. Until recently, the molecular mechanisms utilized by M. pneumoniae to influence asthma symptoms were unknown.
Jorge L Medina   +3 more
doaj   +1 more source

Expression, Purification and Refolding of a Human NaV1.7 Voltage Sensing Domain with Native-like Toxin Binding Properties

open access: yesToxins, 2021
The voltage-gated sodium channel NaV1.7 is an important target for drug development due to its role in pain perception. Recombinant expression of full-length channels and their use for biophysical characterization of interactions with potential drug ...
Ryan V. Schroder   +4 more
doaj   +1 more source

Protective Effect of Peptide Calcium Channel Blocker Omega-Hexatoxin-Hv1a on Epithelial Cell during Ischemia–Reperfusion Injury

open access: yesPharmaceuticals, 2023
Ischemia–reperfusion injury (IRI) is a common phenomenon that develops both from natural causes and during major operations. Many intracellular processes mediated by calcium ions are involved in the development of IRI. Currently, chemical calcium channel
Elena Iurova   +8 more
doaj   +1 more source

A new theraphosid spider toxin causes early insect cell death by necrosis when expressed in vitro during recombinant baculovirus infection. [PDF]

open access: yesPLoS ONE, 2013
Baculoviruses are the most studied insect viruses in the world and are used for biological control of agricultural and forest insect pests. They are also used as versatile vectors for expression of heterologous proteins.
Daniel Mendes Pereira Ardisson-Araújo   +4 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

A novel Kv1.1 potassium channel blocking toxin from the venom of Palamneus gravimanus (Indian black scorpion)

open access: yesJournal of Venomous Animals and Toxins including Tropical Diseases, 2005
A peptide toxin was isolated from the venom of Palamneus gravimanus, the Indian black scorpion, to block human Kv1.1 channels expressed in Xenopus laevis oocytes.
S. S. More   +4 more
doaj   +1 more source

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