Anti-Hsp90 therapy in autoimmune and inflammatory diseases: a review of preclinical studies.
Gdańsk, Poland. In Cell Stress Chaperones, Feb 2016
UNASSIGNED: Heat shock protein 90 (Hsp90), a 90-kDa molecular chaperone, is responsible for biological activities of key signaling molecules (clients) such as protein kinases, ubiquitin ligases, steroid receptors, cell cycle regulators, and transcription factors regulating various cellular processes, including growth, survival, differentiation, and apoptosis.
Green Turtles (Chelonia mydas) Have Novel Asymmetrical Antibodies.
Honolulu, United States. In J Immunol, Jan 2016
Using immunoassays with isotype-specific mAbs, in this study we show that green turtles (Chelonia mydas) have a 5.7S 120-kDa IgY comprising two equally sized H/L chains with truncated Fc and a 7S 200-kDa IgY comprised of two differently sized H chains bound to L chains and apparently often noncovalently associated with an antigenically related 90-kDa moiety.
Regulation of NF-κB signalling cascade by immunophilins.
Buenos Aires, Argentina. In Curr Mol Pharmacol, 2014
It was first discovered that TPR-domain immunophilins such as FKBP51 and FKBP52 play a cardinal role, usually in an antagonistic fashion, in the regulation of several members of the steroid receptor family via its interaction with the heat-shock protein of 90-kDa, Hsp90.