Long-term results after lateral and osteotome technique sinus floor elevation: a retrospective analysis of 2190 implants over a time period of 15 years.

Background: During a time period of 15 years (1992-2007), 2190 implants were inserted in 983 patients after sinus floor elevation.

Materials And Methods: One thousand two hundred and seven implants (461 patients) were placed into sites, in which the sinus was augmented using the lateral approach (LSFE), and 983 implants (522 patients) in sites augmented with the osteotome technique. Bovine bone mineral (n=1217), beta-tricalcium phosphate (n=126), and in some cases, only autogenous bone were used for augmentation in the LSFE.

Mesenchymal stem cells and inorganic bovine bone mineral in sinus augmentation: comparison with augmentation by autologous bone in adult sheep.

Our aim was to compare the osteogenic potential of mononuclear cells harvested from the iliac crest combined with bovine bone mineral (BBM) (experimental group) with that of autogenous cancellous bone alone (control group). We studied bilateral augmentations of the sinus floor in 6 adult sheep. BBM and mononuclear cells (MNC) were mixed and placed into one side and autogenous bone in the other side.

Prion protein NMR structures of cats, dogs, pigs, and sheep.

The NMR structures of the recombinant cellular form of the prion proteins (PrPC) of the cat (Felis catus), dog (Canis familiaris), and pig (Sus scrofa), and of two polymorphic forms of the prion protein from sheep (Ovis aries) are presented. In all of these species, PrPC consists of an N-terminal flexibly extended tail with approximately 100 amino acid residues and a C-terminal globular domain of approximately 100 residues with three alpha-helices and a short antiparallel beta-sheet. Although this global architecture coincides with the previously reported murine, Syrian hamster, bovine, and human PrPC structures, there are local differences between the globular domains of the different species.

Prion protein NMR structures of chickens, turtles, and frogs.

The NMR structures of the recombinant prion proteins from chicken (Gallus gallus; chPrP), the red-eared slider turtle (Trachemys scripta; tPrP), and the African clawed frog (Xenopus laevis; xlPrP) are presented. The amino acid sequences of these prion proteins show approximately 30% identity with mammalian prion proteins. All three species form the same molecular architecture as mammalian PrPC, with a long, flexibly disordered tail attached to the N-terminal end of a globular domain.

Prion protein NMR structures of elk and of mouse/elk hybrids.

The NMR structure of the recombinant elk prion protein (ePrP), which represents the cellular isoform (ePrPC) in the healthy organism, is described here. As anticipated from the highly conserved amino acid sequence, ePrPC has the same global fold as other mammalian prion proteins (PrPs), with a flexibly disordered "tail" of residues 23-124 and a globular domain 125-226 with three alpha-helices and a short antiparallel beta-sheet. However, ePrPC shows a striking local structure variation when compared with most other mammalian PrPs, in particular human, bovine, and mouse PrPC.

Amino acid sequence of the Felis catus prion protein.

A new determination of the house cat (Felis catus) prion protein gene sequence (fPrnp), which has so far been subject of controversy, is reported. The newly determined fPrnp sequence is similar to dog (Canis familiaris) and mink (Mustela putorius) Prnp, but differs significantly from both fPrnp sequences that were previously deposited in the GenBank. Comparison of the canine and feline prion protein sequences suggests a set of amino acid replacements relative to bovine PrP that might relate to the observed different susceptibilities of the two species to TSE infection by ingestion of BSE-infected beef.

Prion protein interaction with the C-terminal SH3 domain of Grb2 studied using NMR and optical spectroscopy.

Transmissible spongiform encephalopathies have been observed exclusively in organisms expressing the host-encoded prion protein (PrP). The function of the cellular isoform of PrP found in healthy organisms has so far not been identified, although there are indications of a role in signal transduction in neurons. To gain further insight into the functional properties of cellular PrP, this paper investigated the binding of the C-terminal SH3 domain of the murine growth factor receptor-bound protein 2 (Grb2) to the murine PrP, using NMR, fluorescence, and circular dichroism spectroscopy.

P450 BM3: the very model of a modern flavocytochrome.

Flavocytochrome P450 BM3 is a bacterial P450 system in which a fatty acid hydroxylase P450 is fused to a mammalian-like diflavin NADPH-P450 reductase in a single polypeptide. The enzyme is soluble (unlike mammalian P450 redox systems) and its fusion arrangement affords it the highest catalytic activity of any P450 mono-oxygenase. This article discusses the fundamental properties of P450 BM3 and how progress with this model P450 has affected our comprehension of P450 systems in general.