C-terminal phosphorylation of Hsp70 and Hsp90 regulates alternate binding to co-chaperones CHIP and HOP to determine cellular protein folding/degradation balances

The Hsp90 chaperone machinery: Conformational dynamics and regulation by co-chaperones

(2011) Jing Li et al.   BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH

Targeting HSP70: The second potentially druggable heat shock protein and molecular chaperone?

(2011) Marissa V. Powers et al.   CELL CYCLE

A Phase I Study of the Heat Shock Protein 90 Inhibitor Alvespimycin (17-DMAG) Given Intravenously to Patients with Advanced Solid Tumors

(2011) Simon Pacey et al.   CLINICAL CANCER RESEARCH

Conformational dynamics of the molecular chaperone Hsp90

(2011) Kristin A. Krukenberg et al.   QUARTERLY REVIEWS OF BIOPHYSICS

Balance between Folding and Degradation for Hsp90-Dependent Client Proteins: A Key Role for CHIP

(2010) Lenka Kundrat et al.   BIOCHEMISTRY

Gymnastics of Molecular Chaperones

(2010) Matthias P. Mayer   MOLECULAR CELL

Swe1Wee1-Dependent Tyrosine Phosphorylation of Hsp90 Regulates Distinct Facets of Chaperone Function

(2010) Mehdi Mollapour et al.   MOLECULAR CELL

HSP90 at the hub of protein homeostasis: emerging mechanistic insights

(2010) Mikko Taipale et al.   NATURE REVIEWS MOLECULAR CELL BIOLOGY

The Proteome in Balance

(2010) D. Hutt et al.   SCIENCE

Protein Kinase CK2 in Health and Disease

(2009) Y. Miyata   CELLULAR AND MOLECULAR LIFE SCIENCES

To fold or not to fold: modulation and consequences of Hsp90 inhibition

(2009) Laura B Peterson et al.   Future Medicinal Chemistry

The ubiquitin ligase CHIP acts as an upstream regulator of oncogenic pathways

(2009) Masashi Kajiro et al.   NATURE CELL BIOLOGY

Chaperone-dependent stabilization and degradation of p53 mutants

(2008) P Muller et al.   ONCOGENE