نتایج جستجو برای: spider venoms

تعداد نتایج: 14870  

2014
Björn M. von Reumont Alexander Blanke Sandy Richter Fernando Alvarez Christoph Bleidorn Ronald A. Jenner

Animal venoms have evolved many times. Venomous species are especially common in three of the four main groups of arthropods (Chelicerata, Myriapoda, and Hexapoda), which together represent tens of thousands of species of venomous spiders, scorpions, centipedes, and hymenopterans. Surprisingly, despite their great diversity of body plans, there is no unambiguous evidence that any crustacean is ...

2013
Daniel M. Lajoie Pamela A. Zobel-Thropp Vlad K. Kumirov Vahe Bandarian Greta J. Binford Matthew H. J. Cordes

Venoms of brown spiders in the genus Loxosceles contain phospholipase D enzyme toxins that can cause severe dermonecrosis and even death in humans. These toxins cleave the substrates sphingomyelin and lysophosphatidylcholine in mammalian tissues, releasing the choline head group. The other products of substrate cleavage have previously been reported to be monoester phospholipids, which would re...

2014
Pamela A Zobel-Thropp Emily Z Thomas Cynthia L David Linda A Breci Greta J Binford

Spider venoms are complex cocktails rich in peptides, proteins and organic molecules that collectively act to immobilize prey. Venoms of the primitive hunting spider, Plectreurys tristis, have numerous neurotoxic peptides called "plectoxins" (PLTX), a unique acylpolyamine called bis(agmatine)oxalamide, and larger unidentified protein components. These spiders also have unconventional multi-lobe...

2017
Silmara R Sousa Joshua S Wingerd Andreas Brust Christopher Bladen Lotten Ragnarsson Volker Herzig Jennifer R Deuis Sebastien Dutertre Irina Vetter Gerald W Zamponi Glenn F King Paul F Alewood Richard J Lewis

Spider venoms are rich sources of peptidic ion channel modulators with important therapeutical potential. We screened a panel of 60 spider venoms to find modulators of ion channels involved in pain transmission. We isolated, synthesized and pharmacologically characterized Cd1a, a novel peptide from the venom of the spider Ceratogyrus darlingi. Cd1a reversibly paralysed sheep blowflies (PD50 of ...

Journal: :Protein and peptide letters 2009
Lucilene D dos Santos Nathalia B Dias José Roberto A S Pinto Mario S Palma

Loxosceles intermedia spider venom was subjected to proteomic analysis through a MudPIT shot-gun approach to identify the protein composition. Were identified 39 proteins which seem to responsible by the lesion of different types of tissues, to some physiopathological actions and by the prevention of structural damage to the toxin structures.

2016
Yongjun Wang Ling Wang Huali Yang Haoliang Xiao Athar Farooq Zhonghua Liu Min Hu Xiaoliu Shi

Antimicrobial peptides have been accepted as excellent candidates for developing novel antibiotics against drug-resistant bacteria. Recent studies indicate that spider venoms are the source for the identification of novel antimicrobial peptides. In the present study, we isolated and characterized an antibacterial peptide named lycosin-II from the venom of the spider Lycosa singoriensis. It cont...

2003
W. D. Branton L. Kolton Y. N. Jan L. Y. Jan Howard Hughes

Studies of presynaptic events in synaptic transmission may be facilitated through the use of specific ligands for functional components of the transmitter release mechanism and through the use of genetics. For this purpose, neurotoxins that affect neuromuscular transmission in Drosophila have been identified and purified from Plecfreurys spider venom (PLTX). One class of toxins causes irreversi...

2014
Jessica E. Garb

Venoms are chemically complex secretions typically comprising numerous proteins and peptides with varied physiological activities. Functional characterization of venom proteins has important biomedical applications, including the identification of drug leads or probes for cellular receptors. Spiders are the most species rich clade of venomous organisms, but the venoms of only a few species are ...

Journal: :Proceedings of the National Academy of Sciences 1984

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