Expressed in the Yeast Saccharomyces cerevisiae, Human ERK5 Is a Client of the Hsp90 Chaperone That Complements Loss of the Slt2p (Mpk1p) Cell Integrity Stress-Activated Protein Kinase

Ítems similars

• A Two-Hybrid Screen of the Yeast Proteome for Hsp90 Interactors Uncovers a Novel Hsp90 Chaperone Requirement in the Activity of a Stress-Activated Mitogen-Activated Protein Kinase, Slt2p (Mpk1p)
  per: Millson, Stefan H., et al.
  Publicat: (2005)
• In the Yeast Heat Shock Response, Hsf1-Directed Induction of Hsp90 Facilitates the Activation of the Slt2 (Mpk1) Mitogen-Activated Protein Kinase Required for Cell Integrity
  per: Truman, Andrew W., et al.
  Publicat: (2007)
• Investigating the protein-protein interactions of the yeast Hsp90 chaperone system by two-hybrid analysis: potential uses and limitations of this approach
  per: Millson, Stefan H., et al.
  Publicat: (2004)
• Threonine 22 phosphorylation attenuates Hsp90 interaction with co-chaperones and affects its chaperone activity
  per: Mollapour, Mehdi, et al.
  Publicat: (2011)
• Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex
  per: Ali, Maruf M. U., et al.
  Publicat: (2006)