Author pages are created from data sourced from our academic publisher partnerships and public sources.
Share This Author
The toxicogenomic multiverse: convergent recruitment of proteins into animal venoms.
- B. Fry, K. Roelants, R. D. L. de la Vega
- BiologyAnnual review of genomics and human genetics
- 28 August 2009
A number of overarching structural, functional, and evolutionary generalities of the protein families from which these toxins have been frequently recruited are discussed and a revised and expanded working definition for venom is proposed.
The MinD Membrane Targeting Sequence Is a Transplantable Lipid-binding Helix*
- T. Szeto, S. Rowland, Cheryl Habrukowich, G. King
- BiologyJournal of Biological Chemistry
- 10 October 2003
It is shown that the MinD MTS is a transplantable lipid-binding motif that can effectively target heterologous proteins to the cell membrane and that the phospholipid preference of each MTS has been evolutionarily “tuned” to its specific role in different bacteria.
Membrane localization of MinD is mediated by a C-terminal motif that is conserved across eubacteria, archaea, and chloroplasts
- T. Szeto, S. Rowland, L. Rothfield, G. King
- BiologyProceedings of the National Academy of Sciences…
- 7 November 2002
It is shown that the extreme C-terminal region of MinD contains a highly conserved 8- to 12-residue sequence motif that is essential for membrane localization of the protein and provides evidence that this motif forms an amphipathic helix that most likely mediates a direct interaction between MinD and membrane phospholipids.
Mapping the MinE Site Involved in Interaction with the MinD Division Site Selection Protein of Escherichia coli
The site within MinE that is required for interaction with MinD was mapped by studying the effects of site-directed minE mutations on MinD-MinE interactions in yeast two-hybrids and three-hybrid experiments, confirming that the MinE N-terminal domain is responsible for the interaction of MinE with Min D.
Structural basis for the topological specificity function of MinE
The structure of the homodimeric topological specificity domain of Escherichia coli MinE is reported and it is shown that it forms a novel αβ sandwich.
Spider-venom peptides that target voltage-gated sodium channels: pharmacological tools and potential therapeutic leads.
Venoms as a platform for human drugs: translating toxins into therapeutics
- G. King
- Biology, ChemistryExpert opinion on biological therapy
- 6 October 2011
The current pipeline of venom-derived therapeutics is surveyed and the potential of peptide and protein drugs derived from venoms is critically examined, including an increasing industry focus on disulfide-rich venom peptides and the use of a broader array of molecular targets in order to develop venom-based therapeutics for treating a wider range of clinical conditions.
Spider-venom peptides: structure, pharmacology, and potential for control of insect pests.
This work critically review the potential of spider-venom peptides to control insect pests and highlight their advantages and disadvantages compared with conventional chemical insecticides.
The structure of a novel insecticidal neurotoxin, ω-atracotoxin-HV1, from the venom of an Australian funnel web spider
A family of potent insecticidal toxins has recently been isolated from the venom of Australian funnel web spiders. Among these is the 37-residue peptide ω-atracotoxin-HV1 (ω-ACTX-HV1) from Hadronyche…
ArachnoServer 2.0, an updated online resource for spider toxin sequences and structures
Key features of ArachnoServer include a molecular target ontology designed specifically for venom toxins, current and historic taxonomic information and a powerful advanced search interface.