Results 151 to 160 of about 260,045 (204)

Enhanced Effectiveness of Onabotulinum Toxin A in Combination With Definisse KP1 Eye Contour Cream for Upper Face Rejuvenation: A Case Series. [PDF]

J Cosmet Dermatol
Proietti I, Manni M.
europepmc   +1 more source

RTP004 Peptide Binds to Botulinum Neurotoxin, Increases Cell Surface Binding, and Enhances Cellular SNAP-25 Cleavage. [PDF]

Toxins (Basel)
Batista AF, Singh R, Lee F, Zhuo S, Leonoudakis D, Gallagher CJ.   +5 more
europepmc   +1 more source

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Peptide Toxins Targeting KV Channels

2021
A number of peptide toxins isolated from animals target potassium ion (K+) channels. Many of them are particularly known to inhibit voltage-gated K+ (KV) channels and are mainly classified into pore-blocking toxins or gating-modifier toxins. Pore-blocking toxins directly bind to the ion permeation pores of KV channels, thereby physically occluding them.
Kazuki, Matsumura, Mariko, Yokogawa, Masanori, Osawa   +2 more
openaire   +2 more sources

Neuroprotection and peptide toxins

Brain Research Reviews, 2004
Neurodegeneration induced by excitatory neurotransmitter glutamate is considered to be of particular relevance in several types of acute and chronic neurological impairments ranging from cerebral ischaemia to neuropathological conditions such as motor neuron disease, Alzheimer's, Parkinson's disease and epilepsy.
Wudayagiri, Rajendra, Arunmozhiarasi, Armugam, Kandiah, Jeyaseelan   +2 more
openaire   +2 more sources

Pharmacologically active spider peptide toxins

Cellular and Molecular Life Sciences (CMLS), 2003
Advances in mass spectrometry and peptide biochemistry coupled to modern methods in electrophysiology have permitted the isolation and identification of numerous novel peptide toxins from animal venoms in recent years. These advances have also opened up the field of spider venom research, previously unexplored due to methodological limitations.
G, Corzo, P, Escoubas
openaire   +2 more sources

Engineering Cyclic Peptide Toxins

2012
Peptide-based toxins have attracted much attention in recent years for their exciting potential applications in drug design and development. This interest has arisen because toxins are highly potent and selectively target a range of physiologically important receptors.
Clark, Richard J., Craik, David J.
openaire   +3 more sources

Synthetic peptide antigens of tetanus toxin

Molecular Immunology, 1994
In this study the immunochemical structure of the heavy chain polypeptide from tetanus toxin was studied. Numerous antigenic determinants were identified by probing a set of overlapping peptides derived from the amino acid sequence of tetanus toxin with polyclonal anti-toxoid antibody preparations.
P M, Fischer, M E, Howden
openaire   +2 more sources

NMR of Peptide Toxins

2009
This article gives an overview of the use of NMR to determine the structures of peptide-based toxins, with ‘toxin’ loosely defined as a peptide that has a harmful effect on any organism. We focus on peptides up to
Rosengren, K. Johan, Daly, N. L., Craik, D. J.   +2 more
openaire   +2 more sources

Peptide antagonists of superantigen toxins

Molecular Diversity, 2004
Superantigens produced by Staphylococcus aureus and Streptococcus pyogenes are among the most lethal of toxins. Toxins in this large family trigger an excessive cellular immune response leading to toxic shock. Superantigens are secreted by the bacteria as diverse natural mixtures, a complexity that demands development of broad-spectrum countermeasures.
openaire   +2 more sources

Rapid analysis of peptide toxins in cyanobacteria

Journal of Chromatography A, 1988
A quick and easy-to-perform method for routine analysis of cyanobacterial (blue-green algal) peptide toxins is proposed. The toxins are analysed by means of high-performance liquid chromatography using a recently developed internal surface reversed-phase column.
J A, Meriluoto, J E, Eriksson
openaire   +2 more sources