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Michael R. Kanost

Researcher at Kansas State University

Publications -  209
Citations -  20028

Michael R. Kanost is an academic researcher from Kansas State University. The author has contributed to research in topics: Manduca sexta & Hemolymph. The author has an hindex of 69, co-authored 202 publications receiving 18407 citations. Previous affiliations of Michael R. Kanost include Florida State University College of Arts and Sciences & University of Arizona.

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Insights into social insects from the genome of the honeybee Apis mellifera

George M. Weinstock, +228 more
- 26 Oct 2006 - 
TL;DR: The genome sequence of the honeybee Apis mellifera is reported, suggesting a novel African origin for the species A. melliferA and insights into whether Africanized bees spread throughout the New World via hybridization or displacement.
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Biological mediators of insect immunity

TL;DR: A component of insect immune responses to bacteria is the synthesis by fat body and hemocytes of a variety of antibacterial proteins and peptides, which are secreted into the hemolymph.
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Immune pathways and defence mechanisms in honey bees Apis mellifera

TL;DR: It is suggested that an implied reduction in immune flexibility in bees reflects either the strength of social barriers to disease, or a tendency for bees to be attacked by a limited set of highly coevolved pathogens.
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RNA interference in Lepidoptera: An overview of successful and unsuccessful studies and implications for experimental design

Olle Terenius, +78 more
TL;DR: Despite a large variation in the data, trends that are found are that RNAi is particularly successful in the family Saturniidae and in genes involved in immunity and that gene expression in epidermal tissues seems to be most difficult to silence.
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Innate immune responses of a lepidopteran insect, Manduca sexta

TL;DR: Current research is focused on the proteolytic activation of prophenoloxidase (proPO) – a reaction implicated in melanotic encapsulation, wound healing, and protein cross‐linking, and three proPO‐activating proteinases, each of which requires serine proteinase homologs as a cofactor for generating active phenol oxidase.