PubMed · 4505984
The source did not provide an abstract. Follow the original record for more information.
Explore connections, maps & timelines
C H Schwalbe, H G Gassen, W Saenger. 1972-08-09. 3-Deazauridine: crystal structure and conformation.. https://doi.org/10.1038/newbio238171a0
Cite the original work for its findings. Save a collection to share your selection of sources.
KEEP EXPLORING
Explore the source record for details and available documents.
This paper presents an architectural model of wheat (Triticum aestivum), designed to explain effects of light conditions at the individual leaf level on tillering kinetics. Various model variables, including blade length and curvature, were parameterized for spring wheat, and compared with winter wheat and other Gramineae species. The architectural model enables simulation of plant properties at the level of individual organs. Parameterization was based on data derived from an outdoor experiment with spring wheat cv. Minaret. Final organ dimensions of tillers could be modelled using the concept of relative phytomer numbers. Various variables in spring wheat showed marked similarities to winter wheat and other species, suggesting possibilities for a general Gramineae architectural model. Our descriptive model is suitable for our objective: investigating light effects on tiller behaviour. However, we plan to replace the descriptive modelling solutions by physiological, mechanistic solutions, starting with the localized production and partitioning of assimilates as affected by abiotic growth factors.
Silent information regulator 2 (Sir2) proteins, or sirtuins, are protein deacetylases dependent on nicotine adenine dinucleotide (NAD) and are found in organisms ranging from bacteria to humans. In eukaryotes, sirtuins regulate transcriptional repression, recombination, the cell-division cycle, microtubule organization, and cellular responses to DNA-damaging agents. Sirtuins have also been implicated in regulating the molecular mechanisms of aging. The Sir2 catalytic domain, which is shared among all sirtuins, consists of two distinct domains that bind NAD and the acetyl-lysine substrate, respectively. In addition to the catalytic domain, eukaryotic sirtuins contain variable amino- and carboxy-terminal extensions that regulate their subcellular localizations and catalytic activity.