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The Hsp90 Co-Chaperones Cdc37 and Sti1 Interact Physically and Genetically
Biological Chemistry, 2002Cdc37 associates with the heat-shock protein 90 (Hsp90) molecular chaperone as one of several auxiliary proteins that are collectively referred to as Hsp90 co-chaperones. Cdc37 has been proposed to be a specificity factor for Hsp90, directing it notably towards kinases.
Abbas-Terki, Toufik +3 more
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A role for Cdc37 in EGFRvIII biogenesis
2013The mutant epidermal growth factor receptor, EGFRvIII, is associated with tumour aggressiveness and drug resistance in glioblastoma. Our lab has shown that the molecular chaperone Hsp90 interacts with nascent EGFRvIII, and that EGFRvIII expression and function is dependent upon Hsp90 activity.
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Exposure of protein kinase motifs that trigger binding of Hsp90 and Cdc37
Biochemical and Biophysical Research Communications, 2005Hsp90 and its co-chaperone Cdc37 are required for the activity of numerous eukaryotic protein kinases. c-Jun N-terminal kinases (JNKs) appear to be Hsp90-independent kinases, as their activity is unaffected by Hsp90 inhibition. It is currently unknown why some protein kinases are Hsp90- and Cdc37-dependent for their function, while others are not ...
Thomas, Prince, Robert L, Matts
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Role of Cdc37 in Protein Kinase Folding
2007As nascent chains emerge from the ribosome, they interact with molecular chaperone proteins that prevent aggregation and promote protein folding. Chaperones such as Hsp70 and Hsp40 function together to protect nascent chains while still ribosome bound, and function with little if any specificity for the unfolded polypeptide.
Atin K. Mandal +2 more
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