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COLD SPRING HARBOR PERSPECTIVES IN BIOLOGY, ISSN 1943-0264, 09/2019, Volume 11, Issue 9, p. 1
Journal Article
Trends in Biochemical Sciences, ISSN 0968-0004, 02/2015, Volume 40, Issue 2, pp. 117 - 125
The conserved Hsp90 chaperone is an ATP-controlled machine that assists the folding and controls the stability of select proteins. Emerging data explain how... 
protein–protein interactions | protein folding | molecular chaperones | Alzheimer disease | heat shock proteins | intrinsically disordered proteins | HSP72 Heat-Shock Proteins | Molecular Chaperones | HSP90 Heat-Shock Proteins | Humans | Intrinsically Disordered Proteins | Protein Binding | Substrate Specificity | Ligands | Alzheimer Disease | Protein Folding | Protein Interaction Maps | Heat shock proteins | Molecular chaperones | Intrinsically disordered proteins | Protein folding | Protein-protein interactions | X-RAY SOLUTION | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | STRUCTURAL-ANALYSIS | ESCHERICHIA-COLI HSP90 | POSTTRANSLATIONAL MODIFICATIONS | protein-protein interactions | HEAT-SHOCK-PROTEIN | GLUCOCORTICOID-RECEPTOR | SUBSTRATE-BINDING | N-TERMINAL DOMAIN | MOLECULAR CHAPERONE | Protein Binding - genetics | Molecular Chaperones - metabolism | Molecular Chaperones - genetics | HSP72 Heat-Shock Proteins - metabolism | Molecular Chaperones - chemistry | HSP72 Heat-Shock Proteins - chemistry | Alzheimer Disease - pathology | HSP72 Heat-Shock Proteins - genetics | Protein Interaction Maps - genetics | Intrinsically Disordered Proteins - chemistry | Alzheimer Disease - metabolism | HSP90 Heat-Shock Proteins - chemistry | HSP90 Heat-Shock Proteins - metabolism | HSP90 Heat-Shock Proteins - genetics | Alzheimer Disease - genetics | Intrinsically Disordered Proteins - metabolism | Proteins | Protein binding
Journal Article
Trends in Biochemical Sciences, ISSN 0968-0004, 02/2015, Volume 40, Issue 2, p. 117
  The conserved Hsp90 chaperone is an ATP-controlled machine that assists the folding and controls the stability of select proteins. Emerging data explain how... 
Proteins | Protein folding | Binding sites | Adenosine triphosphatase
Journal Article
Journal Article
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 1/2011, Volume 108, Issue 2, pp. 580 - 585
Journal Article
F1000Research, ISSN 2046-1402, 2019, Volume 8, p. 1840
Since its discovery more than 25 years ago, great progress has been made in our understanding of the unfolded protein response (UPR), a homeostatic mechanism... 
Journal Article
BBA - Molecular Cell Research, ISSN 0167-4889, 03/2012, Volume 1823, Issue 3, pp. 636 - 647
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 01/2011, Volume 108, Issue 2, p. 580
The molecular chaperone Hsp90 is a protein folding machine that is conserved from bacteria to man. Human, cytosolic Hsp90 is dedicated to folding of chiefly... 
Signal transduction | Molecules | Nuclear magnetic resonance--NMR | Heat shock proteins | Mass spectrometry | Adenosine triphosphatase | Binding sites
Journal Article
The Journal of Nutritional Biochemistry, ISSN 0955-2863, 12/2012, Volume 23, Issue 12, pp. 1617 - 1626
Sulforaphane [1-isothiocyanato-4-(methyl-sulfinyl) butane)], an isothiocyanate derived from cruciferous vegetables, has been shown to possess potent... 
Hsp90 | NMR | Sulforaphane | Pancreatic cancer | p50Cdc37 | P50 | sulforaphane | pancreatic cancer
Journal Article