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Martin S. Williamson

Researcher at Rothamsted Research

Publications -  165
Citations -  15089

Martin S. Williamson is an academic researcher from Rothamsted Research. The author has contributed to research in topics: Knockdown resistance & Pyrethroid. The author has an hindex of 59, co-authored 164 publications receiving 12974 citations. Previous affiliations of Martin S. Williamson include University of Hertfordshire & The Hertz Corporation.

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Genome Sequence of the Pea Aphid Acyrthosiphon pisum

Stephen Richards, +223 more
- 01 Jan 2010 - 
TL;DR: 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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Molecular characterization of pyrethroid knockdown resistance (kdr) in the major malaria vector Anopheles gambiae s. s.

TL;DR: This work demonstrates that a modification of the voltage‐gated sodium channel protein recently shown to be associated with mutations of the para‐type sodium channel gene is present in certain strains of pyrethroid resistant A. gambiae, and describes a PCR‐based diagnostic test allowing its detection in the genome of single mosquitoes.
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The global status of insect resistance to neonicotinoid insecticides

TL;DR: Despite the current scale of resistance, neonicotinoids remain a major component of many pest control programmes, and resistance management strategies, based on mode of action rotation, are of crucial importance in preventing resistance becoming more widespread.
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The evolution of insecticide resistance in the peach–potato aphid, Myzus persicae

TL;DR: The peach potato aphid, Myzus persicae, is a globally distributed crop pest with a host range of over 400 species including many economically important crop plants as discussed by the authors.
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DDT, pyrethrins, pyrethroids and insect sodium channels.

TL;DR: Some of the work (done at Rothamsted Research and elsewhere) that has led to the identification of specific residues on the sodium channel that may constitute the DDT and pyrethroid binding sites are reviewed.