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BIIB021

Known as: BIIB-021 
National Institutes of Health

Papers overview

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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… 
2013
2013
Purpose: BIIB021 is the first oral, synthetic, non-geldanamycin–based HSP90 inhibitor that showed activity in preclinical models… 
2013
2013
Purpose: Kaposi sarcoma–associated herpes virus (KSHV)–associated primary effusion lymphomas (PEL) have extremely poor prognosis… 
Highly Cited
2009
Highly Cited
2009
Inhibition of heat shock protein 90 (Hsp90) results in the degradation of oncoproteins that drive malignant progression, inducing… 
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… 
Highly Cited
2009
Highly Cited
2009
Heat shock protein 90 (Hsp90) is a molecular chaperone that promotes the conformational maturation of numerous client proteins… 
Highly Cited
2009
Highly Cited
2009
17‐AAG, the first‐generation clinical Hsp90 inhibitor, exhibits promising antitumor activity in clinical studies, but is limited… 
2009
2009
Purpose: In Hodgkin's lymphoma, constitutive activation of NF-κB promotes tumor cell survival and proliferation. The molecular… 
Highly Cited
2009
Highly Cited
2009
Heat shock protein 90 (HSP90) inhibitors, such as 17-allylamino-17-demethoxygeldanamycin (17-AAG, tanespimycin), which is… 
2008
2008
2503 Background: BIIB021 is an oral fully synthetic Hsp90 inhibitor that is being developed for both solid and hematologic tumors…