نتایج جستجو برای: scorpion toxin

تعداد نتایج: 53607  

2014
Zhijian Cao Zhiyong Di Yingliang Wu Wenxin Li

Scorpions are one of the most ancient groups of terrestrial animals. They have maintained a steady morphology over more than 400 million years of evolution. Their venom arsenals for capturing prey and defending against predators may play a critical role in their ancient and conservative appearance. In the current review, we present the scorpion fauna of China: 53 species covering five families ...

Journal: :Science 2013
Ashlee H Rowe Yucheng Xiao Matthew P Rowe Theodore R Cummins Harold H Zakon

Painful venoms are used to deter predators. Pain itself, however, can signal damage and thus serves an important adaptive function. Evolution to reduce general pain responses, although valuable for preying on venomous species, is rare, likely because it comes with the risk of reduced response to tissue damage. Bark scorpions capitalize on the protective pain pathway of predators by inflicting i...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2011
Jennifer J Smith Justine M Hill Michelle J Little Graham M Nicholson Glenn F King Paul F Alewood

The three-disulfide inhibitor cystine knot (ICK) motif is a fold common to venom peptides from spiders, scorpions, and aquatic cone snails. Over a decade ago it was proposed that the ICK motif is an elaboration of an ancestral two-disulfide fold coined the disulfide-directed β-hairpin (DDH). Here we report the isolation, characterization, and structure of a novel toxin [U(1)-liotoxin-Lw1a (U(1)...

Journal: :BMB reports 2010
Rong Zhang Yong Cui Xi Zhang Zhuo Yang Yongshan Zhao Yongbo Song Chunfu Wu Jinghai Zhang

The existence of glycine residues in long-chain scorpion toxins has been well documented. However, their role as analgesics has not been evaluated. To address this issue, we investigated the functional role of glycines in the C-terminal end of Chinese-scorpion toxin from Buthus martensii Karsch (BmK AGP-SYPU2) using site-directed mutagenesis and analgesic activity assays. Recombinant BmK AGP-SY...

Journal: :Science 1998
R MacKinnon S L Cohen A Kuo A Lee B T Chait

Toxins from scorpion venom interact with potassium channels. Resin-attached, mutant K+ channels from Streptomyces lividans were used to screen venom from Leiurus quinquestriatus hebraeus, and the toxins that interacted with the channel were rapidly identified by mass spectrometry. One of the toxins, agitoxin2, was further studied by mutagenesis and radioligand binding. The results show that a p...

Journal: :Protein and peptide letters 2005
Chong Li Wei Liu Frank Bossmans Rong-Huan Zhu Jan Tytgat Da-Cheng Wang

The cDNA of BmK IT-AP, an excitatory insect toxin from the scorpion Buthus martensi Karsch that has an analgesic effect on mammalian cells, was expressed in E. coli in the form of an inclusion body. Following denaturation and reduction, the recombinant protein was renatured and purified by liquid chromatography. The authenticity of the recombinant product was confirmed by bioassay and its elect...

Journal: :General physiology and biophysics 1990
G N Mozhayeva A P Naumov Kuryshev YuA E D Nosyreva

Currents through sodium channels of neuroblastoma cells were measured using patch technique in outside-out configuration. Scorpion toxin (ScTX) produced 3 to 4 fold prolongation of mean open time and increased number of reopenings. The mean open times showed slow fluctuations around some average values. The distribution of channel open times for ScTX-modified channels required more than one exp...

Journal: :Peptides 2013
Elisabeth F. Schwartz Adam Bartok Carlos Alberto Schwartz Ferenc Papp Froylan Gómez-Lagunas Gyorgy Panyi Lourival D. Possani

Opisthacanthus cayaporum belongs to the Liochelidae family, and the scorpions from this genus occur in southern Africa, Central America and South America and, therefore, can be considered a true Gondwana heritage. In this communication, the isolation, primary structure characterization, and K⁺-channel blocking activity of new peptide from this scorpion venom are reported. OcyKTx2 is a 34 amino ...

2014
Karina Furlani Zoccal Claudia da Silva Bitencourt Francisco Wanderley Garcia Paula-Silva Carlos Artério Sorgi Karla de Castro Figueiredo Bordon Eliane Candiani Arantes Lúcia Helena Faccioli

Scorpion sting-induced human envenomation provokes an intense inflammatory reaction. However, the mechanisms behind the recognition of scorpion venom and the induction of mediator release in mammalian cells are unknown. We demonstrated that TLR2, TLR4 and CD14 receptors sense Tityus serrulatus venom (TsV) and its major component, toxin 1 (Ts1), to mediate cytokine and lipid mediator production....

Journal: :Journal of molecular biology 2004
Rong-Jin Guan Ye Xiang Xiao-Lin He Chun-Guang Wang Miao Wang Ying Zhang Eric J Sundberg Da-Cheng Wang

Non-proline cis peptide bonds have been observed in numerous protein crystal structures even though the energetic barrier to this conformation is significant and no non-prolyl-cis/trans-isomerase has been identified to date. While some external factors, such as metal binding or co-factor interaction, have been identified that appear to induce cis/trans isomerization of non-proline peptide bonds...

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