RNA interference and receptors

@article{rosenthal_l-canavanine_1989,

title = {L-canavanine incorporation into vitellogenin and macromolecular conformation},

author = {G A Rosenthal and Jean-Marc Reichhart and Jules A Hoffmann},

issn = {0021-9258},

year  = {1989},

date = {1989-01-01},

journal = {J. Biol. Chem.},

volume = {264},

number = {23},

pages = {13693--13696},

abstract = {L-Canavanine is a potentially deleterious arginine antimetabolite whose toxicity is expressed in canavanine-sensitive organisms ranging from viruses to humans. Canavanine, a substrate for arginyl-tRNA synthetase, is incorporated into nascent polypeptide chains in place of arginine. This substitution results in the production of structurally aberrant, canavanyl proteins. Chemical, physical, and immunological studies of native and canavanine-containing vitellogenin obtained from female migratory locusts (Locusta migratoria migratorioides (Orthoptera] provide the first experimental evidence that canavanine can disrupt the tertiary and/or quaternary structure that yields the three-dimensional conformation unique to the protein. These findings enhance our understanding of the biochemical basis for canavanine's antimetabolic and potent insecticidal properties.},

keywords = {Animals, Antibodies, Canavanine, fluorescence, Grasshoppers, hoffmann, M3i, Monoclonal, Protein Conformation, reichhart, Spectrometry, Vitellogenins},

pubstate = {published},

tppubtype = {article}

}

@article{lagueux_ecdysteroids_1981,

title = {Ecdysteroids are bound to vitellin in newly laid eggs of Locusta},

author = {Marie Lagueux and P Harry and Jules A Hoffmann},

issn = {0303-7207},

year  = {1981},

date = {1981-12-01},

journal = {Mol. Cell. Endocrinol.},

volume = {24},

number = {3},

pages = {325--338},

abstract = {The follicle cells of vitellogenic ovaries of Locusta migratoria have been reported to synthesize impressive amounts of ecdysteroids which accumulate inside the oöcytes where they persist during egg-laying; these ecdysteroids are conjugated to more than 95%, and it is believed that their hydrolysis in the egg is the source of the peaks of free ecdysone observed in early embryonic development. The present paper shows that, in the eggs, the ecdysteroid conjugates are bound to a 520 000-dalton macromolecule which shares several characteristics with the major yolk protein vitellin and is precipitated by an anti-vitellin antibody. The physiological relevance of the binding of ovarian ecdysteroid conjugates is discussed in respect to the transfer of maternal ecdysteroids to the embryo.},

keywords = {Animals, Chromatography, Ecdysteroids, Female, Grasshoppers, High Pressure Liquid, hoffmann, Invertebrate Hormones, Lipoproteins, M3i, Molecular Weight, Ovum, Peptide Hydrolases, Radioimmunoassay, Vitellogenins},

pubstate = {published},

tppubtype = {article}

}