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An overview of toxins and genes from the venom of the Asian scorpion Buthus martensi Karsch.
Structural features and molecular evolution of Bowman-Birk protease inhibitors and their potential application.
The canonical nine-residue loop of BBIs/STFI-1 provides an ideal template for drug design of specific inhibitors to target their respective proteases, focusing on the conserved disulfide bridges.
Exploration of the functional site of a scorpion alpha-like toxin by site-directed mutagenesis.
Light is shed on the nature and roles of the residues possibly involved in the biological activity of a scorpion alpha-like toxin and the comparison of BmK M1 with Aah2 and Lqh(alpha)IT showed that the specific orientation of the C-terminus mediated by the reverse turn might be relevant to the preference of alpha-toxin subgroups for phylogenetically distinct yet closely related receptor sites.
Isolation and nucleotide sequence determination of a gene encoding a heat-stable enterotoxin of Escherichia coli.
A Novel Conotoxin from Conus betulinus, κ-BtX, Unique in Cysteine Pattern and in Function as a Specific BK Channel Modulator*
Electrophysiological experiments show that κ-BtX is a novel specific biotoxin against BK channels and its cDNA was cloned and sequenced, and it is concluded thatκ- BtX has no effect on single channel conductance, but increases the open probability of BK channel.
Characterization of novel M‐superfamily conotoxins with new disulfide linkage
The disulfide analyses of two M‐1 conotoxins, mr3e and tx3a, revealed that they possess a new disulfides bond arrangement which is different from those of the M‐4 branch and M‐2 branch, which is the first report of three different patterns of disulfIDE connectivity in conotoxin with the same cysteine framework.
Biological characteristics of dengue virus and potential targets for drug design.
A brief summary of the biological characteristics of d Dengue virus and associated flaviviruses is presented, and the progress on studies of vaccines and drugs based on potential targets of the dengue virus are outlined.
The Ternary Structure of the Double-headed Arrowhead Protease Inhibitor API-A Complexed with Two Trypsins Reveals a Novel Reactive Site Conformation*
- R. Bao, Cong-Zhao Zhou, Chunhui Jiang, Sheng-Xiang Lin, C. Chi, Yuxing Chen
- ChemistryThe Journal of Biological Chemistry
- 28 July 2009
Analysis of the two binding interfaces sheds light on atomic details of the inhibitor specificity and also promises potential improvements in enzyme activity by engineering of the reactive sites.
From the identification of gene organization of alpha conotoxins to the cloning of novel toxins.
- Duoduo Yuan, Yuhong Han, Chun-guang Wang, C. Chi
- BiologyToxicon : official journal of the International…
Based on the comparison of these cDNA and gene sequences, a hypothesis of the alpha conotoxin evolution was proposed and it was suggested that the mutation rate in exon I (encoding the signal peptide and a part of pro-region) is much lower than that inExon II (encoded the other part ofPropeptide, the mature peptides and 3' untranslational region).
Conotoxin αD-GeXXA utilizes a novel strategy to antagonize nicotinic acetylcholine receptors
It is suggested that αD-GeXXA cooperatively binds to two inter-subunit interfaces on the top surface of nAChR, thus allosterically disturbing the opening of the receptor, and provides a valuable basis for the rational design of new nA ChR-targeting compounds.