Activity of the Heat Shock Protein 90 Inhibitor Ganetespib in Melanoma [PDF]
Heat shock protein 90 (HSP90) is involved in the regulation of diverse biological processes such as cell signaling, proliferation and survival, and has been recently recognized as a potential target for cancer therapy.
Hodi, Frank Stephen +2 more
core +10 more sources
Celastrol targets mitochondrial respiratory chain complex I to induce reactive oxygen species-dependent cytotoxicity in tumor cells [PDF]
Background Celastrol is an active ingredient of the traditional Chinese medicinal plant Tripterygium Wilfordii, which exhibits significant antitumor activity in different cancer models in vitro and in vivo; however, the lack of information on the target ...
Guozhu Chen +8 more
core +2 more sources
Elaiophylin Is a Potent Hsp90/ Cdc37 Protein Interface Inhibitor with K-Ras Nanocluster Selectivity
The natural product elaiophylin is a macrodiolide with a broad range of biological activities. However, no direct target of elaiophylin in eukaryotes has been described so far, which hinders a systematic explanation of its astonishing activity range.
Farid A. Siddiqui +3 more
doaj +1 more source
Discrete cytosolic macromolecular BRAF complexes exhibit distinct activities and composition [PDF]
As a central element within the RAS/ERK pathway, the serine/threonine kinase BRAF plays a key role in development and homeostasis and represents the most frequently mutated kinase in tumors.
Brummer, Tilman +8 more
core +1 more source
Evidence has been accumulating to indicate that extracellular vesicles (EVs), including exosomes, released by cancer cells can foster tumour progression.
Kisho Ono +16 more
doaj +1 more source
Physical Interaction of Mammalian CDC37 with CDK4 [PDF]
CDC37 was originally identified as a Start gene in budding yeast and has been shown to be required for association of CDC28 with cyclins. The exact functional mechanism by which CDC37 promotes this association, however, remains unknown. CDK4 is a cyclin D-dependent kinase that controls progression through G1 of the mammalian cell cycle.
K, Dai, R, Kobayashi, D, Beach
openaire +2 more sources
Molecular Cochaperones: Tumor Growth and Cancer Treatment [PDF]
Molecular chaperones play important roles in all cellular organisms by maintaining the proteome in an optimally folded state. They appear to be at a premium in cancer cells whose evolution along the malignant pathways requires the fostering of cohorts of
Calderwood, Stuart K.
core +1 more source
Assembly mechanism of early Hsp90-Cdc37-kinase complexes
Molecular chaperones have an essential role for the maintenance of a balanced protein homeostasis. Here, we investigate how protein kinases are recruited and loaded to the Hsp90-Cdc37 complex, the first step during Hsp90-mediated chaperoning that leads to enhanced client kinase stability and activation.
Dimitra Keramisanou +4 more
openaire +2 more sources
Targeting the Hsp90-Cdc37-client protein interaction to disrupt Hsp90 chaperone machinery
Heat shock protein 90 (Hsp90) is a critical molecular chaperone protein that regulates the folding, maturation, and stability of a wide variety of proteins.
Ting Li +3 more
doaj +1 more source
Atomistic simulations and network-based modeling of the Hsp90-Cdc37 chaperone binding with Cdk4 client protein: A mechanism of chaperoning kinase clients by exploiting weak spots of intrinsically dynamic kinase domains. [PDF]
A fundamental role of the Hsp90 and Cdc37 chaperones in mediating conformational development and activation of diverse protein kinase clients is essential in signal transduction. There has been increasing evidence that the Hsp90-Cdc37 system executes its
Josh Czemeres +2 more
doaj +1 more source

