M
Michael J. Levine
Researcher at State University of New York System
Publications - 162
Citations - 10170
Michael J. Levine is an academic researcher from State University of New York System. The author has contributed to research in topics: Saliva & Mucin. The author has an hindex of 60, co-authored 161 publications receiving 9928 citations. Previous affiliations of Michael J. Levine include University at Buffalo & University of Minnesota.
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Role of salivary mucins in the protection of the oral cavity
TL;DR: Mucins are the principal organic constituents of mucus, the slimy visco-elastic material that coats all mucosal surfaces, and compelling evidence suggests that they play an integral role in non-immune protection of the oral cavity.
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Molecular cloning, sequence, and specificity of expression of the gene encoding the low molecular weight human salivary mucin (MUC7).
TL;DR: The isolation and characterization of overlapping cDNA clones which code for the MG2 protein core are described and a proposed name is proposed for this gene MUC7 in accordance with the mucin genes cloned to date named MUC1-MUC6.
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Periodontal Therapy in Humans: I. Microbiological and Clinical Effects of a Single Course of Periodontal Scaling and Root Planing, and of Adjunctive Tetracycline Therapy
TL;DR: The present results showed that maarked and long-lasting changes in the subgingival microflora associated withperiodontal disease could be achieved by a single course of periodontal treatment.
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Structure of human salivary alpha-amylase at 1.6 A resolution: implications for its role in the oral cavity.
TL;DR: The three-dimensional atomic structure of salivary amylase has been determined and it is found that the highly mobile glycine-rich loop 304-310 may act as a gateway for substrate binding and be involved in a 'trap-release' mechanism in the hydrolysis of substrates.
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Salivary statherin. Dependence on sequence, charge, hydrogen bonding potency, and helical conformation for adsorption to hydroxyapatite and inhibition of mineralization.
TL;DR: The structural domains of salivary statherin that are partly responsible for the protection and recalcification of tooth enamel were examined with respect to charge, sequence, hydrophobicity, hydrogen bonding potential, and conformation to indicate that the negative charge density, sequence (1-15), and helical conformation at the N-terminal region of st Heatherin are important for its surface interaction with HAP.