Publications by authors named "R Furter"

Objective: This study examined recent trends of preventive dental care utilization among Americans aged 50 and above, focusing on variations across racial and ethnic groups including Whites, Blacks, Hispanics, American Indians/Alaska Natives, and Asians.

Methods: Self-reported information on oral health behaviors was collected from 644,635 participants in the Behavioral Risk Factor Surveillance System between 1999 and 2008.

Results: Despite a significant upward trend of frequency of dental cleaning from 1999 to 2008 (OR = 1.

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Artificial proteins can be engineered to exhibit interesting solid state, liquid crystal or interfacial properties and may ultimately serve as important alternatives to conventional polymeric materials. The utility of protein-based materials is limited, however, by the availability of just the 20 amino acids that are normally recognized and utilized by biological systems; many desirable functional groups cannot be incorporated directly into proteins by biosynthetic means. In this study, we incorporate para-bromophenylalanine (p-Br-phe) into a model target protein, mouse dihydrofolate reductase (DHFR), by using a bacterial phenylalanyl-tRNA synthetase (PheRS) variant with relaxed substrate specificity.

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Site-directed incorporation of the amino acid analogue p-fluoro-phenylalanine (p-F-Phe) was achieved in Escherichia coli. A yeast suppressor tRNA(Phe)amber/phenylalanyl-tRNA synthetase pair was expressed in an analogue-resistant E. coli strain to direct analogue incorporation at a programmed amber stop codon in the DHFR marker protein.

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Michaelis- and dissociation constants of sarcomeric mitochondrial creatine kinase (Mi(b)-CK) in solution were determined by enzyme assay and compared to those of cytosolic MM-CK under identical conditions at pH 7.4 and 25 degrees C. Saturation transfer 31P-NMR was used to determine the steady state fluxes mediated by Mi-CK and MM-CK in solution.

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Creatine kinase (CK) has been postulated to consist of two flexibly hinged domains. A previously demonstrated protease-sensitive site in M-CK (Morris & Jackson, 1991) has directed our attempts to dissect mitochondrial CK (Mi-CK) into two protein fragments encompassing amino acids [1-167] and [168-380]. When expressed separately in Escherichia coli, the two fragments yielded large amounts of insoluble inclusion bodies, from which the respective polypeptides could be purified by a simple two-step procedure.

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