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BIIB021

Known as: BIIB-021 
 
National Institutes of Health

Papers overview

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2016
2016
  • W. He, X. Ye, +5 authors W. Qian
  • International journal of oncology
  • 2016
  • Corpus ID: 19753131
Development of drug resistance due to BCR-ABL point mutations and the persistence of leukemia initiating cells has become a major… Expand
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2016
2016
The effec.t of BIIB021, a novel heat shock protein 90 (hsp90) inhibitor, on survival of thyroid carcinoma cells has not been… Expand
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Highly Cited
2013
Highly Cited
2013
BACKGROUND HSP90 inhibition leads to proteosomal degradation of activated KIT and has in vitro activity against gastrointestinal… Expand
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2013
2013
Purpose: BIIB021 is the first oral, synthetic, non-geldanamycin–based HSP90 inhibitor that showed activity in preclinical models… Expand
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Highly Cited
2010
Highly Cited
2010
Heat shock protein 90 (Hsp90) is a molecular chaperone that promotes the conformational maturation of numerous client proteins… Expand
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Highly Cited
2010
Highly Cited
2010
17‐AAG, the first‐generation clinical Hsp90 inhibitor, exhibits promising antitumor activity in clinical studies, but is limited… Expand
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Highly Cited
2009
Highly Cited
2009
Inhibition of heat shock protein 90 (Hsp90) results in the degradation of oncoproteins that drive malignant progression, inducing… Expand
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Highly Cited
2009
Highly Cited
2009
Purpose: We designed and synthesized CUDC-305, an HSP90 inhibitor of the novel imidazopyridine class. Here, we report its unique… Expand
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2009
2009
Purpose: In Hodgkin's lymphoma, constitutive activation of NF-κB promotes tumor cell survival and proliferation. The molecular… Expand
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2008
2008
2503 Background: BIIB021 is an oral fully synthetic Hsp90 inhibitor that is being developed for both solid and hematologic tumors… Expand
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