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.
cMyBP-C as a promiscuous substrate: phosphorylation by non-PKA kinases and its potential significance.
London, United Kingdom. In J Muscle Res Cell Motil, 2012
Although much of the work to date on phospho-regulation of cMyBP-C has focused on the role of protein kinase A (PKA, also known as cAMP-dependent protein kinase), recent evidence suggests that a number of non-PKA serine/threonine kinases, such as Ca(2+)/calmodulin-dependent protein kinase II, protein kinase C, protein kinase D and the 90-kDa ribosomal S6 kinase are also capable of targeting this key regulatory sarcomeric protein.