Novartis

About: Novartis is a company organization based out in Basel, Switzerland. It is known for research contribution in the topics: Alkyl & Population. The organization has 41930 authors who have published 50566 publications receiving 1978996 citations. The organization is also known as: Novartis International AG.

Insecticidal toxines, genes coding therefor, antibodies binding them, transgenic plant cells and plants expressing these toxines

Abstract: This invention relates to transgenic plants, plant cells and microorganisms which are transformed by use of recombinant DNA techniques in such a way that they are able to synthesise toxins, which act selectively on insects, from venomous animals, advantageously from representatives of the phylum Arthropoda, in particular from representatives of the class Arachnida (arachnids), especially from representatives of the order Scorpiones, and, in particular, from representatives of the class Chilopoda (centipedes). The invention also relates to genes which encode the said toxins, and to the use of these genes in order to confer on plants a genetically mediated resistance to insects and in order to control phytopathogenic insects. The invention also relates to a toxin from the venom of the scorpion Leiurus quinquestriatus hebraeus with the amino-acid sequence VRDAYIAKNY NCVYECFRDA YCNELCTKNG ASSGYCQWAG KYGNACWCYA LPDNVPIRVP GKCR. The invention furthermore relates to antibodies against said toxins and insecticidal agents which contain said toxins.

Negative regulation of cytochrome c‐mediated oligomerization of Apaf‐1 and activation of procaspase‐9 by heat shock protein 90

Abstract: The release of cytochrome c from mitochondria results in the formation of an Apaf-1–caspase-9 apoptosome and induces the apoptotic protease cascade by activation of procaspase-3. The present studies demonstrate that heat shock protein 90 (Hsp90) forms a cytosolic complex with Apaf-1 and thereby inhibits the formation of the active complex. Immunodepletion of Hsp90 depletes Apaf-1 and thereby inhibits cytochrome c-mediated activation of caspase-9. Addition of purified Apaf-1 to Hsp90-depleted cytosolic extracts restores cytochrome c-mediated activation of procaspase-9. We also show that Hsp90 inhibits cytochrome c-mediated oligomerization of Apaf-1 and thereby activation of procaspase-9. Furthermore, treatment of cells with diverse DNA-damaging agents dissociates the Hsp90–Apaf-1 complex and relieves the inhibition of procaspase-9 activation. These findings provide the first evidence for a negative cytosolic regulator of cytochrome c-dependent apoptosis and for involvement of a chaperone in the caspase cascade.