Salivary statherin. Dependence on sequence, charge, hydrogen bonding potency, and helical conformation for adsorption to hydroxyapatite and inhibition of mineralization.-Reference-Cited by-同舟云学术

Salivary statherin. Dependence on sequence, charge, hydrogen bonding potency, and helical conformation for adsorption to hydroxyapatite and inhibition of mineralization.

Published:1992-03 Issue:9 Volume:267 Page:5968-5976
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Raj P.A.,Johnsson M,Levine M.J.,Nancollas G.H.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference51 articles.

1. Inhibition of apatite crystal growth by the amino-terminal segment of human salivary acidic proline-rich proteins

2. The nature of the hydroxyapatite-binding site in salivary acidic proline-rich proteins

3. The location and nature of calcium-binding sites in salivary acidic proline-rich phosphoproteins.

4. Side chain-backbone hydrogen bonding contributes to helix stability in peptides derived from an α-helical region of carboxypeptidase A

5. Statherin: A major boundary lubricant of human saliva

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