snx-2112 and Ovarian-Neoplasms

snx-2112 has been researched along with Ovarian-Neoplasms* in 1 studies

Other Studies

1 other study(ies) available for snx-2112 and Ovarian-Neoplasms

Article	Year
Discovery of NMS-E973 as novel, selective and potent inhibitor of heat shock protein 90 (Hsp90). Bioorganic & medicinal chemistry, 2013, Nov-15, Volume: 21, Issue:22 Novel small molecule inhibitors of heat shock protein 90 (Hsp90) were discovered with the help of a fragment based drug discovery approach (FBDD) and subsequent optimization with a combination of structure guided design, parallel synthesis and application of medicinal chemistry principles. These efforts led to the identification of compound 18 (NMS-E973), which displayed significant efficacy in a human ovarian A2780 xenograft tumor model, with a mechanism of action confirmed in vivo by typical modulation of known Hsp90 client proteins, and with a favorable pharmacokinetic and safety profile. Topics: Animals; Antineoplastic Agents; Binding Sites; Biomarkers, Tumor; Catalytic Domain; Cell Line, Tumor; Cell Survival; Crystallography, X-Ray; Drug Design; Drug Evaluation, Preclinical; Female; HSP90 Heat-Shock Proteins; Humans; Isoxazoles; Mice; Mice, Inbred BALB C; Mice, Nude; Ovarian Neoplasms; Protein Binding; Structure-Activity Relationship; Transplantation, Heterologous	2013

Article

Year

Discovery of NMS-E973 as novel, selective and potent inhibitor of heat shock protein 90 (Hsp90).

Bioorganic & medicinal chemistry, 2013, Nov-15, Volume: 21, Issue:22

Novel small molecule inhibitors of heat shock protein 90 (Hsp90) were discovered with the help of a fragment based drug discovery approach (FBDD) and subsequent optimization with a combination of structure guided design, parallel synthesis and application of medicinal chemistry principles. These efforts led to the identification of compound 18 (NMS-E973), which displayed significant efficacy in a human ovarian A2780 xenograft tumor model, with a mechanism of action confirmed in vivo by typical modulation of known Hsp90 client proteins, and with a favorable pharmacokinetic and safety profile.

Topics: Animals; Antineoplastic Agents; Binding Sites; Biomarkers, Tumor; Catalytic Domain; Cell Line, Tumor; Cell Survival; Crystallography, X-Ray; Drug Design; Drug Evaluation, Preclinical; Female; HSP90 Heat-Shock Proteins; Humans; Isoxazoles; Mice; Mice, Inbred BALB C; Mice, Nude; Ovarian Neoplasms; Protein Binding; Structure-Activity Relationship; Transplantation, Heterologous

2013