Michael Gregory Page
Dentist (Pediatric) | Pediatric Dentistry
2824 Ne Wasco St Suite 230 Portland OR, 97232About
Dr. Michael Page is a pediatric dentist practicing in Portland, OR. Dr. Page specializes in the oral health of children. Pediatric dentists tend to patients ranging in age from infancy to teenaged years. As a pediatric dentist, Dr. Page takes care of a childs teeth, gums and mouth. Children can face dental problems like tooth decay and gum disease without proper care. Pediatric dentists can provide dental examinations, give cleanings and treatments, repair cavitities and dental injuries like fractured or knocked-out teeth, diagnose oral conditions and more.
Provider Details
Expert Publications
Data provided by the National Library of Medicine- The structure and function of the 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase from Haemophilus influenzae.
- Multiple conformations of the acylenzyme formed in the hydrolysis of methicillin by Citrobacter freundii beta-lactamase: a time-resolved FTIR spectroscopic study.
- Restriction site-free insertion of PCR products directionally into vectors.
- Hydroxamic acid derivatives as potent peptide deformylase inhibitors and antibacterial agents.
- Crystal structure of the class D beta-lactamase OXA-10.
- Rapid identification of substrates for novel proteases using a combinatorial peptide library.
- In vitro and in vivo properties of Ro 63-9141, a novel broad-spectrum cephalosporin with activity against methicillin-resistant staphylococci.
- Peptide deformylase as an antibacterial drug target: assays for detection of its inhibition in Escherichia coli cell homogenates and intact cells.
- Peptide deformylase as an antibacterial drug target: target validation and resistance development.
- Effect of divalent metal cations on the dimerization of OXA-10 and -14 class D beta-lactamases from Pseudomonas aeruginosa.
- Membrane transport proteins: implications of sequence comparisons.
- Extended-spectrum beta-lactamases: structure and kinetic mechanism.
- Crystallization and preliminary X-ray characterization of maltoporin from Escherichia coli.
- Topographic labelling of pore-forming proteins from the outer membrane of Escherichia coli.
- Cloning, over-expression and the catalytic properties of the EcoP15 modification methylase from Escherichia coli.
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