RINGs of good and evil: RING finger ubiquitin ligases at the crossroads of tumour suppression and oncogenesis
S Lipkowitz, AM Weissman - Nature Reviews Cancer, 2011 - nature.com
The ubiquitin-proteasome system has numerous crucial roles in physiology and
pathophysiology. Fundamental to the specificity of this system are ubiquitin-protein ligases …
pathophysiology. Fundamental to the specificity of this system are ubiquitin-protein ligases …
Drug discovery in the ubiquitin–proteasome system
G Nalepa, M Rolfe, JW Harper - Nature reviews Drug discovery, 2006 - nature.com
Regulated protein turnover via the ubiquitin–proteasome system (UPS) underlies a wide
variety of signalling pathways, from cell-cycle control and transcription to development …
variety of signalling pathways, from cell-cycle control and transcription to development …
CHIP-Hsc70 complex ubiquitinates phosphorylated tau and enhances cell survival
The microtubule-binding protein tau has been implicated in the neurofibrillary pathology of
Alzheimer's disease. Within affected cells, ubiquitinated and hyperphosphorylated tau …
Alzheimer's disease. Within affected cells, ubiquitinated and hyperphosphorylated tau …
High HSP90 expression is associated with decreased survival in breast cancer
The heat shock protein HSP90 chaperones proteins implicated in breast cancer
progression, including Her2/neu. HSP90-targeting agents are in clinical trials for breast …
progression, including Her2/neu. HSP90-targeting agents are in clinical trials for breast …
Heat shock proteins in the regulation of apoptosis: new strategies in tumor therapy: a comprehensive review
AS Sreedhar, P Csermely - Pharmacology & therapeutics, 2004 - Elsevier
Heat shock proteins (Hsp) form the most ancient defense system in all living organisms on
earth. These proteins act as molecular chaperones by helping in the refolding of misfolded …
earth. These proteins act as molecular chaperones by helping in the refolding of misfolded …
The Hsp90 molecular chaperone: an open and shut case for treatment
The molecular chaperone Hsp90 (90 kDa heat-shock protein) is a remarkably versatile
protein involved in the stress response and in normal homoeostatic control mechanisms. It …
protein involved in the stress response and in normal homoeostatic control mechanisms. It …
Chaperoned ubiquitylation—crystal structures of the CHIP U box E3 ubiquitin ligase and a CHIP-Ubc13-Uev1a complex
CHIP is a dimeric U box E3 ubiquitin ligase that binds Hsp90 and/or Hsp70 via its TPR-
domain, facilitating ubiquitylation of chaperone bound client proteins. We have determined …
domain, facilitating ubiquitylation of chaperone bound client proteins. We have determined …
DNAJA1 controls the fate of misfolded mutant p53 through the mevalonate pathway
Stabilization of mutant p53 (mutp53) in tumours greatly contributes to malignant progression.
However, little is known about the underlying mechanisms and therapeutic approaches to …
However, little is known about the underlying mechanisms and therapeutic approaches to …
Targeting Hsp90/Hsp70-based protein quality control for treatment of adult onset neurodegenerative diseases
WB Pratt, JE Gestwicki, Y Osawa… - Annual review of …, 2015 - annualreviews.org
Currently available therapies for adult onset neurodegenerative diseases provide
symptomatic relief but do not modify disease progression. Here we explore a new …
symptomatic relief but do not modify disease progression. Here we explore a new …
Discovery of (2, 4-Dihydroxy-5-isopropylphenyl)-[5-(4-methylpiperazin-1-ylmethyl)-1, 3-dihydroisoindol-2-yl] methanone (AT13387), a Novel Inhibitor of the Molecular …
AJ Woodhead, H Angove, MG Carr… - Journal of medicinal …, 2010 - ACS Publications
Inhibitors of the molecular chaperone heat shock protein 90 (Hsp90) are currently
generating significant interest in clinical development as potential treatments for cancer. In a …
generating significant interest in clinical development as potential treatments for cancer. In a …