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The molecular basis of the specific anti‐influenza action of amantadine.
TLDR
The data reported here demonstrate that the basis of these actions is similar and resides in the virus‐coded M2 membrane protein, the product of a spliced transcript of RNA segment 7.
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Drug resistance in veterinary helminths.
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Characterisation of the binding of [3H]methyllycaconitine: a new radioligand for labelling α7-type neuronal nicotinic acetylcholine receptors
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Candidate anthelmintic resistance-associated gene expression and sequence polymorphisms in a triple-resistant field isolate of Haemonchus contortus.
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Genome Sequence of the Pea Aphid Acyrthosiphon pisum
The genome of the pea aphid shows remarkable levels of gene duplication and equally remarkable gene absences that shed light on aspects of aphid biology, most especially its symbiosis with Buchnera.
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Glutamate-gated chloride channels and the mode of action of the avermectin/milbemycin anthelmintics
TLDR
The known expression patterns of the GluCl explain most of the observed biological effects of treatment with the macrocyclic lactones, though the reason for the long-lasting inhibition of larval production in filarial species is still poorly understood.
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Molecular basis of resistance of influenza A viruses to amantadine.
TLDR
Mutations which confer resistance to amantadine are restricted to four amino acids within a hydrophobic sequence of M2 indicating that the primary target of drug action is the membrane-associated portion of this molecule.
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Recent advances in candidate-gene and whole-genome approaches to the discovery of anthelmintic resistance markers and the description of drug/receptor interactions
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Molecular detection of benzimidazole resistance in Haemonchus contortus using real-time PCR and pyrosequencing
TLDR
The concordance between real-time PCR and pyrosequencing results carried out in different laboratories indicated that these tools are suitable for the routine diagnosis of BZ-resistance in H. contortus.
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An autoradiographic study of the distribution of binding sites for the novel α7‐selective nicotinic radioligand [3H]‐methyllycaconitine in the mouse brain
TLDR
The utility of [3H]‐MLA for characterization of α7‐type nicotinic receptors in mammalian brain, and suggests that it labels a population identical to that defined by [125I]‐α‐bungarotoxin, is demonstrated.
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