نتایج جستجو برای: scorpion toxin

تعداد نتایج: 53607  

2015
Karen Luna-Ramírez Verónica Quintero-Hernández Víctor Rivelino Juárez-González Lourival D. Possani Mandë Holford

Australian scorpion venoms have been poorly studied, probably because they do not pose an evident threat to humans. In addition, the continent has other medically important venomous animals capable of causing serious health problems. Urodacus yaschenkoi belongs to the most widely distributed family of Australian scorpions (Urodacidae) and it is found all over the continent, making it a useful m...

Journal: :Toxicon : official journal of the International Society on Toxinology 2011
B I García-Gómez F I V Coronas R Restano-Cassulini R R Rodríguez L D Possani

This communication describes the first general biochemical, molecular and functional characterization of the venom from the Cuban blue scorpion Rhopalurus junceus, which is often used as a natural product for anti-cancer therapy in Cuba. The soluble venom of this arachnid is not toxic to mice, injected intraperitoneally at doses up to 200 μg/20 g body weight, but it is deadly to insects at dose...

Scorpion venom is a rich source of toxins which have great potential to develop new therapeutic agents. Scorpion chloride channel toxins (ClTxs), such as Chlorotoxin selectively inhibit human Matrix Methaloproteinase-2 (hMMP-2). The inhibitors of hMMP-2 have potential use in cancer therapy. Three new ClTxs, meuCl14, meuCl15 and meuCl16, derived from the venom transcriptome of Iranian scorpion, ...

Journal: :Biochemistry 2001
K C Ellis T C Tenenholz H Jerng M Hayhurst C S Dudlak W F Gilly M P Blaustein D J Weber

A toxin from the scorpion Tityus serrulatus (TsTX-Kalpha) blocks native squid K(+) channels and their cloned counterpart, sqKv1A, at pH 8 ((native)K(d) approximately 20 nM; (sqKv1A)K(d) approximately 10 nM). In both cases, decreasing the pH below 7.0 significantly diminishes the TsTX-Kalpha effect (pK = 6.6). In the cloned squid channel, the pH dependence of the block is abolished by a single p...

2017
Shilong Yang Fan Yang Bei Zhang Bo Hyun Lee Bowen Li Lei Luo Jie Zheng Ren Lai

Venomous animals use peptide toxins for hunting and self-defense. To achieve these goals, toxins need to bind to their targets with high affinity due to the small amount that a single bite or sting can deliver. The scorpion toxin BmP01 is linked to sting-induced excruciating pain; however, the reported minimum concentrations for activating TRPV1 channel or inhibiting voltage-gated potassium (Kv...

Journal: :General physiology and biophysics 1985
L D Zaborovskaya B I Khodorov

Recently it has been established that y toxin of Tityus serrulatus scorpion venom has a very high affinity to Na channels and can be successfully used as a marker during their purification from excitable membranes (Barhanin et al. 1983 ; Grishin 1983). There has, however, been some controversy concerning the effects of the y toxin on properties of Na channels in different tissues. Thus, in neur...

Journal: :The Journal of biological chemistry 2012
Cathy Poillot Hicham Bichraoui Céline Tisseyre Eloi Bahemberae Nicolas Andreotti Jean-Marc Sabatier Michel Ronjat Michel De Waard

Maurocalcine is the first demonstrated example of an animal toxin peptide with efficient cell penetration properties. Although it is a highly competitive cell-penetrating peptide (CPP), its relatively large size of 33 amino acids and the presence of three internal disulfide bridges may hamper its development for in vitro and in vivo applications. Here, we demonstrate that several efficient CPPs...

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