Results 41 to 50 of about 6,074 (204)
Discrete cytosolic macromolecular BRAF complexes exhibit distinct activities and composition [PDF]
, 2017 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
Pharmaceuticals, 2013 A fundamental role of the Hsp90-Cdc37 chaperone system in mediating maturation of protein kinase clients and supporting kinase functional activity is essential for the integrity and viability of signaling pathways involved in cell cycle control and ...
Gennady Verkhivker +3 more
doaj +1 more source
Cells, 2020 Tumor cells exhibit therapeutic stress resistance-associated secretory phenotype involving extracellular vesicles (EVs) such as oncosomes and heat shock proteins (HSPs). Such a secretory phenotype occurs in response to cell stress and cancer therapeutics.
Takanori Eguchi +8 more
doaj +1 more source
Celastrol targets mitochondrial respiratory chain complex I to induce reactive oxygen species-dependent cytotoxicity in tumor cells [PDF]
, 2011 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
HECTD3 mediates an HSP90-dependent degradation pathway for protein kinase clients [PDF]
, 2017 Inhibition of the ATPase cycle of the HSP90 chaperone promotes ubiquitylation and proteasomal degradation of its client proteins, which include many oncogenic protein kinases.
Li, Zhaobo +4 more
core +6 more sources
HSP-90/kinase complexes are stabilized by the large PPIase FKB-6
Scientific Reports, 2021 Protein kinases are important regulators in cellular signal transduction. As one major type of Hsp90 client, protein kinases rely on the ATP-dependent molecular chaperone Hsp90, which maintains their structure and supports their activation.
Siyuan Sima +7 more
doaj +1 more source
Characterization of HSP90 isoforms in transformed bovine leukocytes infected with Theileria annulata [PDF]
, 2016 HSP90 chaperones are essential regulators of cellular function, as they ensure the appropriate conformation of multiple key client proteins. Four HSP90 isoforms were identified in the protozoan parasite Theileria annulata.
Calder, Ewen D.D. +8 more
core +2 more sources
Characterization of Celastrol to Inhibit Hsp90 and Cdc37 Interaction [PDF]
Journal of Biological Chemistry, 2009 The molecular chaperone heat shock protein 90 (Hsp90) is required for the stabilization and conformational maturation of various oncogenic proteins in cancer. The loading of protein kinases to Hsp90 is actively mediated by the cochaperone Cdc37. The crucial role of the Hsp90-Cdc37 complex has made it an exciting target for cancer treatment.
Tao, Zhang +5 more
openaire +2 more sources
Cdc37 and protein kinase folding
RSC Advances, 2007 Cdc37 is a molecular chaperone that collaborates with Hsp90 to fold protein kinases and other clients including transcription factors. Cdc37 function in protein kinase folding is dependent on direct interaction between the chaperone and the N-lobe of the kinase catalytic domain.
Robert Matts, Avrom J. Caplan
openaire +2 more sources
[Pemetrexed + Sorafenib] lethality is increased by inhibition of ERBB1/2/3-PI3K-NFκB compensatory survival signaling [PDF]
, 2016 In the completed phase I trial NCT01450384 combining the anti-folate pemetrexed and the multi-kinase inhibitor sorafenib it was observed that 20 of 33 patients had prolonged stable disease or tumor regression, with one complete response and multiple ...
Boone, David L. +9 more
core +1 more source