نتایج جستجو برای: toxin peptides

تعداد نتایج: 128988  

Journal: :The Biochemical journal 1997
J D Ashcom B G Stiles

The venoms of predatory marine cone snails, Conus species, contain numerous peptides and proteins with remarkably diverse pharmacological properties. One group of peptides are the alpha-conotoxins, which consist of 13-19 amino acids constrained by two disulphide bonds. A biologically active fluorescein derivative of Conus geographus alpha-conotoxin GI (FGI) was used in novel solution-phase-bind...

2001
MIKAEL JOLKKONEN

Jolkkonen, M., 1996. Muscarinic Toxins from Dendroaspis (Mamba) Venom: Peptides Selective for Subtypes of Muscarinic Acetylcholine Receptors. Acta Univ. Ups., Comprehensive Summaries of Uppsala Dissertations from the Faculty of Science and Technology 183. 52 pp. Uppsala. ISBN 91-554-3675-7 Snake venoms from various mamba species contain peptides which bind to the muscarinic but not to the nicot...

Journal: :Biochemistry 1993
E Gazit Y Shai

The Bacillus thuringiensis var. israelensis (Bti) cytolytic toxin is hypothesized to exert its toxic activity via pore formation in the cell membrane as a result of the aggregation of several monomers. To gain insight into the toxin's mode of action, 2 putative hydrophobic 22 amino acid peptides were synthesized and characterized spectroscopically and functionally. One peptide corresponded to t...

Journal: :Journal of Investigative Dermatology 2022

Our group has challenged the concept that S. epidermidis (SE) is only a beneficial commensal microbe by showing when skin colonization of SE increases, it promotes inflammation through production protease EcpA. Analysis genome revealed encodes 4 genes homologous to α-type phenol soluble modulin (PSM) toxic peptide made aureus (SA), thus suggesting another mechanism which can harm skin. Principl...

Journal: :Toxicon : official journal of the International Society on Toxinology 2011
Darin R Rokyta Kenneth P Wray Alan R Lemmon Emily Moriarty Lemmon S Brian Caudle

Despite causing considerable human mortality and morbidity, animal toxins represent a valuable source of pharmacologically active macromolecules, a unique system for studying molecular adaptation, and a powerful framework for examining structure-function relationships in proteins. Snake venoms are particularly useful in the latter regard as they consist primarily of a moderate number of protein...

Journal: :The Journal of biological chemistry 2001
I Gómez D I Oltean S S Gill A Bravo M Soberón

In susceptible lepidopteran insects, aminopeptidase N and cadherin-like proteins are the putative receptors for Bacillus thuringiensis (Bt) toxins. Using phage display, we identified a key epitope that is involved in toxin-receptor interaction. Three different scFv molecules that bind Cry1Ab toxin were obtained, and these scFv proteins have different amino acid sequences in the complementary de...

Journal: :The Journal of biological chemistry 2009
Nareen Abboud Magdia De Jesus Antonio Nakouzi Radames J B Cordero Mario Pujato András Fiser Johanna Rivera Arturo Casadevall

Protective antigen (PA), the binding subunit of anthrax toxin, is the major component in the current anthrax vaccine, but the fine antigenic structure of PA is not well defined. To identify linear neutralizing epitopes of PA, 145 overlapping peptides covering the entire sequence of the protein were synthesized. Six monoclonal antibodies (mAbs) and antisera from mice specific for PA were tested ...

2018
Stephan Holger Drukewitz Nico Fuhrmann Eivind A B Undheim Alexander Blanke Julien Giribaldi Rosanna Mary Guillaume Laconde Sébastien Dutertre Björn Marcus von Reumont

Predatory robber flies (Diptera, Asilidae) have been suspected to be venomous due to their ability to overpower well-defended prey. However, details of their venom composition and toxin arsenal remained unknown. Here, we provide a detailed characterization of the venom system of robber flies through the application of comparative transcriptomics, proteomics and functional morphology. Our result...

Journal: :The Journal of neuroscience : the official journal of the Society for Neuroscience 1999
Q Q Sun N Dale

5-HT produces voltage-independent inhibition of the N-, P/Q-, and T-type Ca2+ currents in sensory neurons of Xenopus larvae by acting on 5-HT1A and 5-HT1D receptors. We have explored the underlying mechanisms further and found that the inhibition of high voltage-activated (HVA) currents by 5-HT is mediated by a pertussis toxin-sensitive G-protein that activates a diffusible second messenger. Al...

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