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The implementation of a new paradigm for caries management is necessary for the profession to respond effectively to changing population health needs. The FDI Global Caries Initiative (GCI) is a 10 year programme aimed at developing and implementing a new paradigm for caries management, one that would contribute to a common vision of health. The article(More)
Although antibodies are highly specific, cross-reactions are frequently observed. To understand the molecular basis of this phenomenon, we studied the anti-hen egg lysozyme (HEL) monoclonal antibody (mAb) D11.15, which cross-reacts with several avian lysozymes, in some cases with a higher affinity (heteroclitic binding) than for HEL. We have determined the(More)
Tryptophan 54 of the alpha 7 neuronal nicotinic homooligomeric receptor is homologous to gamma-Trp-55 and delta-Trp-57 of non-alpha subunits of Torpedo receptor labeled by d-tubocurarine. This residue was mutated on the alpha 7-V201-5-hydroxytryptamine (5HT)3 homooligomeric chimera, which displays alpha 7 nicotinic pharmacology, and for which both(More)
The neuronal nicotinic alpha 7 (nAChR) and 5-hydroxytryptamine (5HT3) receptors are ligand-gated ion channels with a homologous topological organization and have activation and desensitization reactions in common. Yet these homo-oligomeric receptors differ in the pharmacology of their binding sites for agonists and competitive antagonists, and in their(More)
The three-dimensional structures of the free and antigen-complexed Fabs from the mouse monoclonal anti-hen egg white lysozyme antibody D44.1 have been solved and refined by X-ray crystallographic techniques. The crystals of the free and lysozyme-bound Fabs were grown under identical conditions and their X-ray diffraction data were collected to 2.1 and 2.5(More)
Recent studies have suggested that alcohols can affect the function of neurotransmitter-gated ion channels by a direct interaction with the receptor protein. However, the molecular region of the receptor protein that mediates the alcohol action is not known. To address this question, we studied the effect of ethanol on the function of recombinant nicotinic(More)
Porin, a channel-forming protein spanning bacterial outer membranes, was denatured in 6 M guanidinium hydrochloride or, alternatively, in sodium dodecyl sulfate at 95 degrees C. Circular dichroism spectra revealed that this protein, which in its native state consist of beta-pleated sheets as the sole detectable secondary structure, is transformed into(More)
A protein from outer membranes of Escherichia coli K-12, porin OmpF was crystallized either with short acyl chain phospolipids or with various detergents as amphiphiles. In dihexanoyl phosphatidylcholine, crystals greater than 0.3 mm in all dimensions were obtained that diffract X-rays beyond 3.5 A. Crystal morphology and unit cell dimensions were(More)