Graham M. Nicholson

ORCID: 0000-0002-4277-4296
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About
Contact & Profiles
Research Areas
  • Ion channel regulation and function
  • Venomous Animal Envenomation and Studies
  • Insect and Pesticide Research
  • Nicotinic Acetylcholine Receptors Study
  • Neurobiology and Insect Physiology Research
  • Neuroscience and Neuropharmacology Research
  • Insect and Arachnid Ecology and Behavior
  • Antimicrobial Peptides and Activities
  • Biochemical and Structural Characterization
  • Insect Resistance and Genetics
  • Marine Toxins and Detection Methods
  • Healthcare and Venom Research
  • Neuroscience and Neural Engineering
  • Epilepsy research and treatment
  • Beetle Biology and Toxicology Studies
  • Cardiac electrophysiology and arrhythmias
  • Neuroscience of respiration and sleep
  • Rabies epidemiology and control
  • Toxin Mechanisms and Immunotoxins
  • Pain Mechanisms and Treatments
  • Insect Pest Control Strategies
  • Transcranial Magnetic Stimulation Studies
  • Cholinesterase and Neurodegenerative Diseases
  • Redox biology and oxidative stress
  • Muscle activation and electromyography studies

University of Technology Sydney
2011-2020

Lewis & Clark College
2010

The University of Queensland
2003

Université d'Angers
2001

Department of Medical Sciences
2001

New South Wales Department of Health
2000

The University of Sydney
1983-1999

University of Virginia
1999

Georgia Institute of Technology
1997

University of Tübingen
1995

ArachnoServer ( www.arachnoserver.org ) is a manually curated database providing information on the sequence, structure and biological activity of protein toxins from spider venoms. These proteins are interest to wide range biologists due their diverse applications in medicine, neuroscience, pharmacology, drug discovery agriculture. currently manages 1078 sequences, 759 nucleic acid sequences 56 structures. Key features include molecular target ontology designed specifically for venom...

10.1093/nar/gkq1058 article EN cc-by-nc Nucleic Acids Research 2010-10-29

Spiders are one of the most successful venomous animals, with more than 48,000 described species. Most spider venoms dominated by cysteine-rich peptides a diverse range pharmacological activities. Some contain thousands unique peptides, but little is known about mechanisms used to generate such complex chemical arsenals. We an integrated transcriptomic, proteomic, and structural biology approach demonstrate that lethal Australian funnel-web produces 33 superfamilies venom proteins....

10.1073/pnas.1914536117 article EN Proceedings of the National Academy of Sciences 2020-05-12

Ciguatoxins are cyclic polyether toxins, derived from marine dinoflagellates, which responsible for the symptoms of ciguatera poisoning. Ingestion tropical and subtropical fin fish contaminated by ciguatoxins results in an illness characterised neurological, cardiovascular gastrointestinal disorders. The pharmacology is their ability to cause persistent activation voltage-gated sodium channels, increase neuronal excitability neurotransmitter release, impair synaptic vesicle recycling, cell...

10.3390/md403082 article EN cc-by Marine Drugs 2006-04-06

The three-disulfide inhibitor cystine knot (ICK) motif is a fold common to venom peptides from spiders, scorpions, and aquatic cone snails. Over decade ago it was proposed that the ICK an elaboration of ancestral two-disulfide coined disulfide-directed β-hairpin (DDH). Here we report isolation, characterization, structure novel toxin [U 1 -liotoxin-Lw1a (U -LITX-Lw1a)] scorpion Liocheles waigiensis first example native peptide adopts DDH fold. U -LITX-Lw1a not only represents discovery...

10.1073/pnas.1103501108 article EN Proceedings of the National Academy of Sciences 2011-06-13

Pacific ciguatoxin-1 (P-CTX-1), is a highly lipophilic cyclic polyether molecule originating from the marine dinoflagellate Gambierdiscus toxicus. Its effects were investigated on sodium channel subtypes present in acutely dissociated rat dorsal root ganglion neurons, using whole-cell patch clamp techniques. Concentrations of P-CTX-1 ranging 0.2 to 20 nM had no effect kinetics tetrodotoxin-sensitive (TTX-S) or tetrodotoxin-resistant (TTX-R) activation and inactivation, however,...

10.1016/s0022-3565(24)37963-7 article EN Journal of Pharmacology and Experimental Therapeutics 1999-01-01

We have isolated a novel family of insect-selective neurotoxins that appear to be the most potent blockers insect voltage-gated calcium channels reported date. These toxins display exceptional phylogenetic specificity, with at least 10,000-fold preference for <i>versus</i> vertebrate channels. The structure one reveals highly structured, disulfide-rich core and structurally disordered C-terminal extension is essential channel blocking activity. Weak structural/functional homology...

10.1074/jbc.m105206200 article EN cc-by Journal of Biological Chemistry 2001-10-01
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