Noncollagenous phosphoproteins that interact with type I collagen are thought to nucleate
the mineral phase to collagen network of mineralized tissues. Previously, we found that …

Noncollagenous phosphoproteins that interact with type I collagen are thought to nucleate
the mineral phase to the collagen fibril network of mineralized tissues. We previously …

Immobilization of phosphoproteins on a collagen matrix is important for the induction of
intrafibrillar apatite mineralization. Unlike phosphate esters, polyphosphonic acid has no …

Although “chaperone molecules” rich in negatively charged residues (ie, glutamic and
aspartic acid) are known to play important roles in the biomineralization process, the precise …

Collagen is the critical organic component of bone matrix, which is the template for bone
biomineralization. Phosphorylation modification of collagen plays an important role in the …

Non-collagenous phosphoproteins that interact with a type-I collagen are thought to
nucleate bone mineral into collagen networks of mineralized tissues. Previously …

Decalcified samples of chicken bone containing phosphoproteins of varying concentrations
were used to assess the effect of phosphoproteins and of protein-bound Ser (P) and Thr (P) …

Bone is a composite material in which collagen fibrils form a scaffold for a highly organized
arrangement of uniaxially oriented apatite crystals,. In the periodic 67 nm cross-striated …

Osteopontin is a phosphorylated sialoprotein containing a conserved sequence of
contiguous aspartic acid residues. This protein is expressed at high levels in mineralized …

Phosphoproteins (PP) covalently bound to a collagenous matrix have been reported to
promote its mineralization in vitro. It was the aim of the present study to determine whether …