HSP90 and the chaperoning of cancer

L Whitesell, SL Lindquist - Nature Reviews Cancer, 2005 - nature.com
Standing watch over the proteome, molecular chaperones are an ancient and evolutionarily
conserved class of proteins that guide the normal folding, intracellular disposition and …

Regulation and function of the human HSP90AA1 gene

AD Zuehlke, K Beebe, L Neckers, T Prince - Gene, 2015 - Elsevier
Heat shock protein 90α (Hsp90α), encoded by the HSP90AA1 gene, is the stress inducible
isoform of the molecular chaperone Hsp90. Hsp90α is regulated differently and has different …

Molecular actions of glucocorticoids in cartilage and bone during health, disease, and steroid therapy

K Hartmann, M Koenen, S Schauer… - Physiological …, 2016 - journals.physiology.org
Cartilage and bone are severely affected by glucocorticoids (GCs), steroid hormones that
are frequently used to treat inflammatory diseases. Major complications associated with long …

Novobiocin and additional inhibitors of the Hsp90 C-terminal nucleotide-binding pocket

A Donnelly, BSJ Blagg - Current medicinal chemistry, 2008 - benthamdirect.com
The 90 kDa heat shock proteins (Hsp90), which are integrally involved in cell signaling,
proliferation, and survival, are ubiquitously expressed in cells. Many proteins in tumor cells …

Altered Hsp90 function in cancer: a unique therapeutic opportunity

R Bagatell, L Whitesell - Molecular cancer therapeutics, 2004 - aacrjournals.org
Molecular chaperones or so-called heat shock proteins serve as central integrators of
protein homeostasis within cells. In performing this function, they guide the folding …

Anticancer inhibitors of Hsp90 function: beyond the usual suspects

G Garg, A Khandelwal, BSJ Blagg - Advances in cancer research, 2016 - Elsevier
The 90-kDa heat-shock protein (Hsp90) is a molecular chaperone responsible for the
stability and function of a wide variety of client proteins that are critical for cell growth and …

Regulators of endothelial and epithelial barrier integrity and function in acute lung injury

R Lucas, AD Verin, SM Black, JD Catravas - Biochemical pharmacology, 2009 - Elsevier
Permeability edema is a life-threatening complication accompanying acute lung injury (ALI),
severe pneumonia and the acute respiratory distress syndrome (ARDS), which can be …

Inhibitors of the HSP90 molecular chaperone: current status

S Sharp, P Workman - Advances in cancer research, 2006 - Elsevier
The molecular chaperone heat shock protein 90 (HSP90) has emerged as an exciting
molecular target for cancer therapy. It operates as part of a multichaperone complex and is …

Hsp90: the vulnerable chaperone

G Chiosis, M Vilenchik, J Kim, D Solit - Drug discovery today, 2004 - Elsevier
The molecular chaperone Hsp90 has emerged as an important target in cancer treatment
because of its roles in maintaining transformation and regulating the function of proteins …

Modulation of chaperone function and cochaperone interaction by novobiocin in the C-terminal domain of Hsp90: evidence that coumarin antibiotics disrupt Hsp90 …

RK Allan, D Mok, BK Ward, T Ratajczak - Journal of Biological Chemistry, 2006 - jbc.org
The C-terminal domain of Hsp90 displays independent chaperone activity, mediates
dimerization, and contains the MEEVD motif essential for interaction with tetratricopeptide …