Protein kinase CK2 is widely expressed in follicular, Burkitt and diffuse large B-cell lymphomas and propels malignant B-cell growth. [PDF]
, 2015 Serine-threonine kinase CK2 is highly expressed and pivotal for survival and proliferation in multiple myeloma, chronic lymphocytic leukemia and mantle cell lymphoma.
Agostinelli, C +9 more
core +1 more source
Computational and Structural Biotechnology Journal, 2023 Heat shock protein 90 (Hsp90) and cell division cycle 37 (Cdc37) work together as a molecular chaperone complex to regulate the activity of a multitude of client protein kinases.
Surya Sukumaran +7 more
doaj +1 more source
Mapping differential interactomes by affinity purification coupled with data independent mass spectrometry acquisition [PDF]
, 2013 Characterizing changes in protein-protein interactions associated with sequence variants (e.g. disease-associated mutations or splice forms) or following exposure to drugs, growth factors or hormones is critical to understanding how protein complexes are
AC Gingras +55 more
core +5 more sources
Activity of the Heat Shock Protein 90 Inhibitor Ganetespib in Melanoma [PDF]
, 2013 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
Cell surface Cdc37 participates in extracellular HSP90 mediated cancer cell invasion.
PLoS ONE, 2012 Cdc37 is a 50 kDa molecular chaperone which targets intrinsically unstable protein kinases to the molecular chaperone HSP90. It is also an over-expressed oncoprotein that mediates carcinogenesis and maintenance of the malignant phenotype by stabilizing ...
Avraam El Hamidieh +2 more
doaj +1 more source
Journal of Extracellular Vesicles, 2020 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
Elaiophylin Is a Potent Hsp90/ Cdc37 Protein Interface Inhibitor with K-Ras Nanocluster Selectivity
Biomolecules, 2021 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
Targeting the Hsp90-Cdc37-client protein interaction to disrupt Hsp90 chaperone machinery
Journal of Hematology & Oncology, 2018 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
Molecular Cochaperones: Tumor Growth and Cancer Treatment [PDF]
, 2014 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
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]
PLoS ONE, 2017 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