Results 61 to 70 of about 6,022 (190)

Characterization of Celastrol to Inhibit Hsp90 and Cdc37 Interaction [PDF]

open access: yesJournal 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

Differential maturation and chaperone dependence of the paralogous protein kinases DYRK1A and DYRK1B

open access: yesScientific Reports, 2022
The HSP90/CDC37 chaperone system not only assists the maturation of many protein kinases but also maintains their structural integrity after folding.
Marco Papenfuss   +6 more
doaj   +1 more source

Antiangiogenic compounds: well-established drugs versus emerging natural molecules [PDF]

open access: yes, 2018
Angiogenesis is the natural and physiologic process of growing blood vessels from pre-existing ones. Pathological angiogenesis occurs when the precise balance of all the molecular pathways that regulate angiogenesis is disrupted, and this process is a ...
Abreu, Rui M.V.   +4 more
core   +1 more source

Role of p50/CDC37 in Hepadnavirus Assembly and Replication [PDF]

open access: yesJournal of Biological Chemistry, 2002
The cellular chaperone Hsp90 has been shown to associate with the reverse transcriptase (RT) of the duck hepatitis B virus and is required for RT functions. However, the molecular basis for the specific interaction between the RT and Hsp90 remains unknown.
Xingtai, Wang   +2 more
openaire   +2 more sources

Regulation of CDK4 [PDF]

open access: yes, 2006
Cyclin-dependent kinase (CDK)4 is a master integrator that couples mitogenic and antimitogenic extracellular signals with the cell cycle. It is also crucial for many oncogenic transformation processes.
Laurence Bockstaele   +4 more
core   +2 more sources

Cdc37 Promotes the Stability of Protein Kinases Cdc28 and Cak1 [PDF]

open access: yesMolecular and Cellular Biology, 2000
In the budding yeast Saccharomyces cerevisiae, Cdc37 is required for the productive formation of Cdc28-cyclin complexes. The cdc37-1 mutant arrests at Start with low levels of Cdc28 protein, which is predominantly unphosphorylated at Thr169, fails to bind cyclin, and has little protein kinase activity.
A, Farrell, D O, Morgan
openaire   +2 more sources

Systematic Analysis Reveals Elongation Factor 2 and α-Enolase as Novel Interaction Partners of AKT2. [PDF]

open access: yesPLoS ONE, 2013
AKT2 is one of the three isoforms of the protein kinase AKT being involved in the modulation of cellular metabolism. Since protein-protein interactions are one possibility to convey specificity in signal transduction, we performed AKT2-protein ...
Katharina Bottermann   +4 more
doaj   +1 more source

Identification of co-chaperone Cdc37 in Penaeus monodon: coordination with Hsp90 can reduce cadmium stress-induced lipid peroxidation

open access: yesEcotoxicology and Environmental Safety, 2021
Cell division cycle 37 (Cdc37) is an important cytoplasmic phosphoprotein, which usually functions as a complex with heat shock protein 90 (Hsp90), to effectively reduce the damage caused by heavy metals, such as cadmium (Cd), in aquatic animals.
Chao Zhao   +5 more
doaj   +1 more source

Transcriptional Response to Acute Thermal Exposure in Juvenile Chinook Salmon Determined by RNAseq. [PDF]

open access: yes, 2015
Thermal exposure is a serious and growing challenge facing fish species worldwide. Chinook salmon (Oncorhynchus tshawytscha) living in the southern portion of their native range are particularly likely to encounter warmer water due to a confluence of ...
Baerwald, Melinda R   +6 more
core  

Characterization of HSP90 isoforms in transformed bovine leukocytes infected with Theileria annulata [PDF]

open access: yes, 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

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