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Salivary and pellicle proteome: A datamining analysis
by
Schweigel, Hardy
, Schwendicke, Falk
, Wicht, Michael
in
631/114/2164
/ 692/4017
/ Animals
/ Data Mining
/ Dental Enamel Proteins - metabolism
/ Dental pellicle
/ Dental Pellicle - metabolism
/ Enzymatic activity
/ Humanities and Social Sciences
/ Humans
/ multidisciplinary
/ Pellicle
/ pH effects
/ Protein structure
/ Proteins
/ Proteome - metabolism
/ Proteomes
/ Salivary Proteins and Peptides - metabolism
/ Science
/ Structure-function relationships
2016
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Salivary and pellicle proteome: A datamining analysis
by
Schweigel, Hardy
, Schwendicke, Falk
, Wicht, Michael
in
631/114/2164
/ 692/4017
/ Animals
/ Data Mining
/ Dental Enamel Proteins - metabolism
/ Dental pellicle
/ Dental Pellicle - metabolism
/ Enzymatic activity
/ Humanities and Social Sciences
/ Humans
/ multidisciplinary
/ Pellicle
/ pH effects
/ Protein structure
/ Proteins
/ Proteome - metabolism
/ Proteomes
/ Salivary Proteins and Peptides - metabolism
/ Science
/ Structure-function relationships
2016
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Salivary and pellicle proteome: A datamining analysis
by
Schweigel, Hardy
, Schwendicke, Falk
, Wicht, Michael
in
631/114/2164
/ 692/4017
/ Animals
/ Data Mining
/ Dental Enamel Proteins - metabolism
/ Dental pellicle
/ Dental Pellicle - metabolism
/ Enzymatic activity
/ Humanities and Social Sciences
/ Humans
/ multidisciplinary
/ Pellicle
/ pH effects
/ Protein structure
/ Proteins
/ Proteome - metabolism
/ Proteomes
/ Salivary Proteins and Peptides - metabolism
/ Science
/ Structure-function relationships
2016
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Journal Article
Salivary and pellicle proteome: A datamining analysis
2016
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Overview
We aimed to comprehensively compare two compartmented oral proteomes, the salivary and the dental pellicle proteome. Systematic review and datamining was used to obtain the physico-chemical, structural, functional and interactional properties of 1,515 salivary and 60 identified pellicle proteins. Salivary and pellicle proteins did not differ significantly in their aliphatic index, hydrophaty, instability index, or isoelectric point. Pellicle proteins were significantly more charged at low and high pH and were significantly smaller (10–20 kDa) than salivary proteins. Protein structure and solvent accessible molecular surface did not differ significantly. Proteins of the pellicle were more phosphorylated and glycosylated than salivary proteins. Ion binding and enzymatic activities also differed significantly. Protein-protein-ligand interaction networks relied on few key proteins. The identified differences between salivary and pellicle proteins could guide proteome compartmentalization and result in specialized functionality. Key proteins could be potential targets for diagnostic or therapeutic application.
Publisher
Nature Publishing Group UK,Nature Publishing Group
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