## Abstract __The molecular chaperone Hsp90 is responsible for activation and stabilization of several oncoproteins in cancer cells, and has emerged as an important target in cancer treatment because of this pivotal role. In recent years, interests have arisen around structureβbased design of small
Inhibition of HSP90 with Pochoximes: SAR and Structure-Based Insights
β Scribed by Sofia Barluenga; Jean-Gonzague Fontaine; Cuihua Wang; Kais Aouadi; Ruihong Chen; Kristin Beebe; Len Neckers; Nicolas Winssinger
- Publisher
- John Wiley and Sons
- Year
- 2009
- Tongue
- English
- Weight
- 640 KB
- Volume
- 10
- Category
- Article
- ISSN
- 1439-4227
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
## Abstract ChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 200 leading journals. To access a ChemInform Abstract of an article which was published elsewhere, please select a βFull Textβ option. The original article is trackable v
A high-resolution structure of Escherichia coli aspartate transcarbamoylase has been determined to 2.1 Γ ; resolution in the presence of the bisubstrate analog N-phosphonacetyl-L-aspartate (PALA). The structure was refined to a free R-factor of 23.4% and a working R-factor of 20.3%. The PALA molecule
Protein Structure-Based Design, Synthesis, and Biological Evaluation of 5-Thia-2,6-diamino-4(3H)-oxopyrimidines: Potent Inhibitors of Glycinamide Ribonucleotide Transformylase with Potent Cell Growth Inhibition. -A novel series of inhibitors such as (I) and (II) are prepared and designed using the X