Targeting multiple signal transduction pathways through inhibition of Hsp90
H Zhang, F Burrows - Journal of molecular medicine, 2004 - Springer
The multichaperone heat shock protein (Hsp) 90 complex mediates the maturation and
stability of a variety of proteins, many of which are crucial in oncogenesis, including …
stability of a variety of proteins, many of which are crucial in oncogenesis, including …
Heat-shock protein 90 inhibitors as novel cancer chemotherapeutic agents
L Neckers, K Neckers - Expert opinion on emerging drugs, 2002 - Taylor & Francis
Heat-shock protein 90 (Hsp90) is a molecular chaperone whose association is required for
the stability and function of multiple mutated, chimeric and overexpressed signalling proteins …
the stability and function of multiple mutated, chimeric and overexpressed signalling proteins …
Hsp90 inhibitors as novel cancer chemotherapeutic agents
L Neckers - Trends in molecular medicine, 2002 - cell.com
Abstract Heat shock protein 90 (Hsp90) is a molecular chaperone whose association is
required for the stability and function of multiple mutated, chimeric and over-expressed …
required for the stability and function of multiple mutated, chimeric and over-expressed …
Therapeutic and diagnostic implications of Hsp90 activation
A Kamal, MF Boehm, FJ Burrows - Trends in molecular medicine, 2004 - cell.com
The molecular chaperone heat-shock protein 90 (Hsp90) is involved in the stabilization and
conformational maturation of many signaling proteins that are deregulated in cancers …
conformational maturation of many signaling proteins that are deregulated in cancers …
Hsp90 activation and cell cycle regulation
F Burrows, H Zhang, A Kamal - Cell cycle, 2004 - Taylor & Francis
The widely-expressed molecular chaperone heat shock protein 90 (Hsp90) regulates
several important cellular processes via its' repertoire of 'client'proteins. Signal transduction …
several important cellular processes via its' repertoire of 'client'proteins. Signal transduction …
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 …
molecular target for cancer therapy. It operates as part of a multichaperone complex and is …
Altered Hsp90 function in cancer: a unique therapeutic opportunity
R Bagatell, L Whitesell - Molecular cancer therapeutics, 2004 - AACR
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 …
protein homeostasis within cells. In performing this function, they guide the folding …
Heat-shock protein 90 inhibitors as novel cancer chemotherapeutics–an update
L Neckers, K Neckers - Expert opinion on emerging drugs, 2005 - Taylor & Francis
Heat-shock protein 90 (Hsp90) is a molecular chaperone whose association is required for
stability and function of a growing number of signalling proteins that have been implicated in …
stability and function of a growing number of signalling proteins that have been implicated in …
Chaperoning oncogenes: Hsp90 as a target of geldanamycin
L Neckers - Molecular chaperones in health and disease, 2006 - Springer
Abstract Heat shock protein 90 (Hsp90) is a molecular chaperone required for the stability
and function of a number of conditionally activated and/or expressed signaling proteins, as …
and function of a number of conditionally activated and/or expressed signaling proteins, as …
Hsp90: a novel target for cancer therapy
Hsp90 is a molecular chaperone required for the stress-survival response, protein refolding,
and the conformational maturation of a variety of signaling proteins. Natural products that …
and the conformational maturation of a variety of signaling proteins. Natural products that …