Turnitin
降AI改写
早检测系统
早降重系统
Turnitin-UK版
万方检测-期刊版
维普编辑部版
Grammarly检测
Paperpass检测
checkpass检测
PaperYY检测
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 …
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 …
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 …
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 …
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 …
protein homeostasis within cells. In performing this function, they guide the folding …
Anticancer inhibitors of Hsp90 function: beyond the usual suspects
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 …
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
Permeability edema is a life-threatening complication accompanying acute lung injury (ALI),
severe pneumonia and the acute respiratory distress syndrome (ARDS), which can be …
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 …
molecular target for cancer therapy. It operates as part of a multichaperone complex and is …
Hsp90: the vulnerable chaperone
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 …
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 …
dimerization, and contains the MEEVD motif essential for interaction with tetratricopeptide …