Preview
Sign-in for full Details 
Sign-in free and Explore the Exciting World of BiomedExperts:
- Over 1.500.000 Profiles
- More than 1.800 Organizations worldwide
- State of the Art Network Visualizations
- Manage your own Profile
- Locate Experts in your Country/Region
- Locate Experts in your 1. and 2. Level Network
- Connect to Experts Worldwide
find experts for
Sign-in to see more
2002:
Sawa Masaaki; Kiyoi Takao; Kurokawa Kiriko; Kumihara Hiroshi; Yamamoto Minoru; Miyasaka Tomohiro; Ito Yasuko; Hirayama Ryoichi; Inoue Tomomi; Kirii Yasuyuki; Nishiwaki Eiji; Ohmoto Hiroshi; Maeda Yu; Ishibushi Etsuko; Inoue Yoshimasa; Yoshino Kohichiro; Kondo Hirosato
New type of metalloproteinase inhibitor: design and synthesis of new phosphonamide-based hydroxamic acids.
Journal of medicinal chemistry 2002;
45(
4):.
A series of phosphonamide-based hydroxamate derivatives were synthesized, and the inhibitory activities were evaluated against various metalloproteinases in order to clarify its selectivity profile. Among the four diastereomeric isomers resulting from the chirality at the C-3 and P atoms, the compound with a (R,R)-configuration both at the C-3 position and the phosphorus atom was found to be potently active, while the other diastereomeric isomers were almost inactive. A number of (R,R)-compounds synthesized here exhibited broad spectrum activities with nanomolar K(i) values against MMP-1, -3, -9, and TACE and also showed nanomolar IC(50) values against HB-EGF shedding in a cell-based inhibition assay. The modeling study using X-ray structure of MMP-3 suggested the possible binding mode of the phosphonamide-based inhibitors.
Sign in free and see...
Visualized networks:
See your personal network in
sophisticated graphical views
GeoTargeted Searches:
Locate experts around the world
and connect with global collaborators
Research Profiles:
See the visualized research activity
of experts around the globe
Sign-in to see more
