Results 51 to 60 of about 6,074 (204)
Interaction between Cdc37 and Cdk4 in human cells [PDF]
Using the yeast two-hybrid system we have identified novel potential Cdk4 interacting proteins. Here we described the interaction of Cdk4 with a human homologue of the yeast Drosophila CDC37 gene products. Cdc37 protein specifically interacts with Cdk4 and Cdk6, but not with Cdc2, Cdk2, Cdk3, Cdk5 and any of a number of cyclins tested.
L, Lamphere +7 more
openaire +2 more sources
The mammalian ULK1 complex and autophagy initiation [PDF]
Autophagy is a vital lysosomal degradation pathway that serves as a quality control mechanism. It rids the cell of damaged, toxic or excess cellular components, which if left to persist could be detrimental to the cell.
Bach +87 more
core +2 more sources
Role of p50/CDC37 in Hepadnavirus Assembly and Replication [PDF]
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
A Thermodynamic-Based Interpretation of Protein Expression Heterogeneity in Different Glioblastoma Multiforme Tumors Identifies Tumor-Specific Unbalanced Processes [PDF]
We describe a thermodynamic-motivated, information theoretic analysis of proteomic data collected from a series of 8 glioblastoma multiforme (GBM) tumors. GBMs are considered here as prototypes of heterogeneous cancers.
Heath, James R. +4 more
core +3 more sources
Cdc37 goes beyond Hsp90 and kinases
Cdc37 is a relatively poorly conserved and yet essential molecular chaperone. It has long been thought to function primarily as an accessory factor for Hsp90, notably directing Hsp90 to kinases as substrates. More recent discoveries challenge this simplistic view.
MacLean, Morag, Picard, Didier
openaire +5 more sources
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
Gene-expression changes in cerium chloride-induced injury of mouse hippocampus. [PDF]
Cerium is widely used in many aspects of modern society, including agriculture, industry and medicine. It has been demonstrated to enter the ecological environment, is then transferred to humans through food chains, and causes toxic actions in several ...
Zhe Cheng +15 more
doaj +1 more source
Role and Regulation of Myeloid Zinc Finger Protein 1 in Cancer [PDF]
Myeloid zinc finger 1 (MZF1) belongs to the SCAN-Zinc Finger (SCAN-ZF) transcription factor family that has recently been implicated in a number of types of cancer.
Anders +58 more
core +1 more source
Cdc37 as a Co-chaperone to Hsp90 [PDF]
The co-chaperone p50/Cdc37 is an important partner for Hsp90, assisting in molecular chaperone activities, particularly with regard to the regulation of protein kinases. The Hsp90/Cdc37complex controls the folding of a large proportion of protein kinases and thus stands at the hub of a multitude of intracellular signaling networks.
openaire +2 more sources
Interactions between Hsp90, its co-chaperone Cdc37 and kinases have been biochemically studied for over three decades and have been shown to be functionally important in organisms from yeast to humans.
Kliment Verba, David Agard
doaj +1 more source

