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ER 

ER 

200 M TRYPTOPHOL. 30 M DIM. 200  M I3C. DMSO. ER . HSP90.

By aderes
(104 views)


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HSP90 Screening

HSP90 Screening

Heat shock proteins (HSP90s) belong to a family of molecular chaperones that are rapid and abundantly induced by stresses. HSP90 plays an important role in stabilizing denatured proteins that have become misfolded or unfolded as a result of cellular stress and by aiding in their re-folding.

By wendywilson (10 views)

Heat Shock Proteins, Hsp90 Inhibitors, and Protein Degradation

Heat Shock Proteins, Hsp90 Inhibitors, and Protein Degradation

Heat Shock Proteins, Hsp90 Inhibitors, and Protein Degradation. By: Vince Centioni Paper: “A high affinity conformation of Hsp90 confers tumour selectivity on Hsp90 inhibitors”. I. Background A. Protein Degradation.

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Steroid-sparing Therapy After Hsp90 Inhibitor Clinical Study

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Hsp90-binding Immunophilins Link p53 to Dynein During p53 Transport to Nucleus

Hsp90-binding Immunophilins Link p53 to Dynein During p53 Transport to Nucleus

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C D C D C D

C D C D C D

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TARGETING HSP90 IN IM-RESISTANT GIST: KIT DEGRADATION AS A BROADLY RELEVANT SALVAGE STRATEGY

TARGETING HSP90 IN IM-RESISTANT GIST: KIT DEGRADATION AS A BROADLY RELEVANT SALVAGE STRATEGY

CTOS – Boca Raton, November 21 st , 2005. TARGETING HSP90 IN IM-RESISTANT GIST: KIT DEGRADATION AS A BROADLY RELEVANT SALVAGE STRATEGY. Sebastian Bauer 1,2 , Lynn Yu 1 , George Demetri 3 , Jonathan Fletcher 1 1 Brigham & Women's Hospital, Harvard Medical School, Boston, MA, USA

By kiefer (125 views)

Protein folding in the cell: The Hsp90 Chaperone Machine Stefan Rüdiger Utrecht, 26 February 2009

Protein folding in the cell: The Hsp90 Chaperone Machine Stefan Rüdiger Utrecht, 26 February 2009

Master Biomolecular Sciences 2008/2009 Master course “Membrane Biogenesis, Protein Folding and Sorting”. Protein folding in the cell: The Hsp90 Chaperone Machine Stefan Rüdiger Utrecht, 26 February 2009. R099. Protein folding and unfolding. Protein unfolding.

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