The carbodiimide product of diafenthiuron reacts covalently with two mitochondrial proteins, the F0-proteolipid and porin, and inhibits mitochondrial ATPase in vitro

Author:

Ruder Franz J.,Kayser Hartmut

Publisher

Elsevier BV

Subject

Health, Toxicology and Mutagenesis,Agronomy and Crop Science,General Medicine

Reference42 articles.

1. The effect of chemodynamic parameters on pesticide performance;Steinemann;Aspects Appl. Biol,1989

2. The thiourea insecticide/acaricide diafenthiuron has a novel mode of action: Inhibition of mitochondrial respiration by its carbodiimide product;Ruder;Pestic. Biochem. Physiol,1991

3. Toxicological studies of the thiourea diafenthiuron in diamond back moths (Lepidoptera: yponomeutidae), two-spotted spider mites (Acari: tetranychidea), and bulb mites (Acari: acaridiae);Kadir;J. Econ. Entomol,1991

4. N,N′-dicyclohexylcarbodiimide binds specifically to a single glutamyl residue of the proteolipid subunit of the mitochondrial adenosinetriphosphatases from Neurospora crassa and Saccharomyces cerevisiae;Sebald,1980

5. On the structure and genetics of the proteolipid subunit of the ATP synthase complex;Sebald;Curr. Top. Bioenerg,1981

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