𝔖 Bobbio Scriptorium
✦   LIBER   ✦

The Structures of the Thrombospondin-1 N-Terminal Domain and Its Complex with a Synthetic Pentameric Heparin

✍ Scribed by Kemin Tan; Mark Duquette; Jin-huan Liu; Rongguang Zhang; Andrzej Joachimiak; Jia-huai Wang; Jack Lawler


Book ID
113918563
Publisher
Elsevier Science
Year
2006
Tongue
English
Weight
828 KB
Volume
14
Category
Article
ISSN
0969-2126

No coin nor oath required. For personal study only.


πŸ“œ SIMILAR VOLUMES


Decorin inhibits cell attachment to thro
✍ Blandine Merle; Luc Malaval; Jack Lawler; Pierre Delmas; Philippe Clezardin πŸ“‚ Article πŸ“… 1997 πŸ› John Wiley and Sons 🌐 English βš– 131 KB πŸ‘ 1 views

Skin decorin (DCN) is an antiadhesive dermatan sulfate-rich proteoglycan that interacts with thrombospondin-1 (TSP) and inhibits fibroblast adhesion to TSP [WinnemΓΆller et al., 1992]. Molecular mechanisms by which DCN interacts with TSP and inhibits cell adhesion to TSP are unknown. In the present s

The structure of the BIR3 domain of cIAP
✍ Kulathila, Raviraj ;Vash, Brian ;Sage, David ;Cornell-Kennon, Susan ;Wright, Kir πŸ“‚ Article πŸ“… 2008 πŸ› International Union of Crystallography 🌐 English βš– 989 KB

The inhibitor of apoptosis protein (IAP) family of molecules inhibit apoptosis through the suppression of caspase activity. It is known that the XIAP protein regulates both caspase-3 and caspase-9 through direct protein-protein interactions. Specifically, the BIR3 domain of XIAP binds to caspase-9 v