Nutritional Assessment of Ready-to-Eat Salads in German Supermarkets: Comparison of the nutriRECIPE-Index and the Nutri-Score.

Globally, an unbalanced diet causes more deaths than any other factor. Due to a lack of knowledge, it is difficult for consumers to select healthy foods at the point of sale. Although different front-of-pack labeling schemes exist, their informative value is limited due to small sets of considered parameters and lacking information on ingredient composition.

The nutriRECIPE-Index - development and validation of a nutrient-weighted index for the evaluation of recipes.

Background: Our objective was to develop a nutrient-based index for evaluating and improving menus in public catering. The nutriRECIPE-Index comprises 24 nutrients and nutrient groups. In developing the index, the following steps were included: setting the goals of the index, nutrient selection, target metrics and scaling, weighting, proof of concept and validation of the index.

Evolutionary constraints of phosphorylation in eukaryotes, prokaryotes, and mitochondria.

High accuracy mass spectrometry has proven to be a powerful technology for the large scale identification of serine/threonine/tyrosine phosphorylation in the living cell. However, despite many described phosphoproteomes, there has been no comparative study of the extent of phosphorylation and its evolutionary conservation in all domains of life. Here we analyze the results of phosphoproteomics studies performed with the same technology in a diverse set of organisms.

Mass spectrometry analysis of complexes formed by myotonic dystrophy protein kinase (DMPK).

Myotonic dystrophy type 1 (DM1) is caused by an expansion of CTG repeats at the 3'-UTR of the serine/threonine protein kinase DMPK. Expanded CTG repeats are toxic since they are transcribed into an RNA molecule which is then sequestered within the nucleus in the form of foci. RNA cytotoxicity is linked to the aberrant splicing of several developmentally regulated genes.

Differential substrate specificity of group I and group II chaperonins in the archaeon Methanosarcina mazei.

Chaperonins are macromolecular machines that assist in protein folding. The archaeon Methanosarcina mazei has acquired numerous bacterial genes by horizontal gene transfer. As a result, both the bacterial group I chaperonin, GroEL, and the archaeal group II chaperonin, thermosome, coexist.