𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Phosphorylation, Glycosylation, and Transglutaminase Sites in Bovine Osteopontin

✍ Scribed by ESBEN S. SØRENSEN; TORBEN E. PETERSEN

Book ID
119872448
Publisher
John Wiley and Sons
Year
1995
Tongue
English
Weight
137 KB
Volume
760
Category
Article
ISSN
0890-6564

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

Posttranslational modifications of bovin
Posttranslational modifications of bovine osteopontin: Identification of twenty-eight phosphorylation and three O-glycosylation sites
✍ Esben S. Sørensen; Torben E. Petersen; Peter Højrup 📂 Article 📅 1995 🏛 Cold Spring Harbor Laboratory Press 🌐 English ⚖ 991 KB

## Abstract Osteopontin (OPN) is a multiphosphorylated glycoprotein found in bone and other normal and malignant tissues, as well as in the physiological fluids urine and milk. The present study demonstrates that bovine milk osteopontin is phosphorylated at 27 serine residues and 1 threonine residu

Identification of osteopontin phosphoryl
Identification of osteopontin phosphorylation sites involved in bone remodeling and inhibition of pathological calcification
✍ Fawzy A. Saad; Erdjan Salih; Melvin J. Glimcher 📂 Article 📅 2008 🏛 John Wiley and Sons 🌐 English ⚖ 98 KB

## Abstract Osteopontin is a noncollagenous, phosphorylated extracellular glycoprotein, expressed in mineralized and nonmineralized tissues, organs and body fluids. The protein contains an RGD tripeptide cell‐binding motif, and is subjected to a variety of posttranslational modifications that play