Immobilization of a phosphonated analog of matrix phosphoproteins within cross-linked collagen as a templating mechanism for biomimetic mineralization

L Gu, YK Kim, Y Liu, K Takahashi, S Arun, CE Wimmer… - Acta biomaterialia, 2011 - Elsevier
Immobilization of phosphoproteins on a collagen matrix is important for the induction of
intrafibrillar apatite mineralization. Unlike phosphate esters, polyphosphonic acid has no …
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[PDF][PDF] Immobilization of a phosphonated analog of matrix phosphoproteins within cross-linked collagen as a templating mechanism for biomimetic mineralization

L Gu, YK Kim, Y Liu, K Takahashi, S Arun… - Acta Biomater. Author …, 2012 - academia.edu
Immobilization of phosphoproteins on a collagen matrix is important for induction of
intrafibrillar apatite mineralization. Unlike phosphate esters, polyphosphonic acid has no …

Immobilization of a phosphonated analog of matrix phosphoproteins within cross-linked collagen as a templating mechanism for biomimetic mineralization

LS Gu, YK Kim, Y Liu, K Takahashi… - Acta …, 2011 - pubmed.ncbi.nlm.nih.gov
Immobilization of phosphoproteins on a collagen matrix is important for the induction of
intrafibrillar apatite mineralization. Unlike phosphate esters, polyphosphonic acid has no …

Immobilization of a phosphonated analog of matrix phosphoproteins within cross-linked collagen as a templating mechanism for biomimetic mineralization

LS Gu, YK Kim, Y Liu, K Takahashi… - Acta …, 2011 - okayama.elsevierpure.com
抄録 Immobilization of phosphoproteins on a collagen matrix is important for the induction of
intrafibrillar apatite mineralization. Unlike phosphate esters, polyphosphonic acid has no …
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[HTML][HTML] Immobilization of a phosphonated analog of matrix phosphoproteins within cross-linked collagen as a templating mechanism for biomimetic mineralization

L Gu, YK Kim, Y Liu, K Takahashi, S Arun… - Acta …, 2011 - ncbi.nlm.nih.gov
Immobilization of phosphoproteins on a collagen matrix is important for induction of
intrafibrillar apatite mineralization. Unlike phosphate esters, polyphosphonic acid has no …

Immobilization of a phosphonated analog of matrix phosphoproteins within cross-linked collagen as a templating mechanism for biomimetic mineralization

LS Gu, YK Kim, Y Liu, K Takahashi… - Acta …, 2011 - augusta.elsevierpure.com
Immobilization of phosphoproteins on a collagen matrix is important for the induction of
intrafibrillar apatite mineralization. Unlike phosphate esters, polyphosphonic acid has no …

Immobilization of a phosphonated analog of matrix phosphoproteins within cross-linked collagen as a templating mechanism for biomimetic mineralization

L Gu, YK Kim, Y Liu, K Takahashi, S Arun, CE Wimmer… - Acta Biomaterialia, 2011 - infona.pl
Immobilization of phosphoproteins on a collagen matrix is important for the induction of
intrafibrillar apatite mineralization. Unlike phosphate esters, polyphosphonic acid has no …

Immobilization of a phosphonated analog of matrix phosphoproteins within cross-linked collagen as a templating mechanism for biomimetic mineralization.

LS Gu, YK Kim, Y Liu, K Takahashi, S Arun… - Acta …, 2010 - europepmc.org
Immobilization of phosphoproteins on a collagen matrix is important for induction of
intrafibrillar apatite mineralization. Unlike phosphate esters, polyphosphonic acid has no …

Immobilization of a phosphonated analog of matrix phosphoproteins within cross-linked collagen as a templating mechanism for biomimetic mineralization

LS Gu, YK Kim, Y Liu, K Takahashi… - Acta …, 2011 - okayama.elsevierpure.com
Immobilization of phosphoproteins on a collagen matrix is important for the induction of
intrafibrillar apatite mineralization. Unlike phosphate esters, polyphosphonic acid has no …