Assessment of disease in low-input cereal cropping systems and variety trials

Disease assessment is the basis for describing disease resistance characteristics of commercial varieties in national variety lists for all crops where disease is considered a problem. It is well known that ‘disease’ in a specific situation depends on a whole range of interacting hosts, pathogens and environmental conditions. However, the biological complexity conflicts with the wish to express disease resistance characteristics of a variety as a single score per disease. This problem will be illustrated by basic dynamics of growth and senescence of both host and pathogen over time. Disease expressed in terms of absolute diseased leaf area, disease relative to total leaf area or green leaf area will be discussed in general. Two particular problems in low-input systems will be discussed, i.e. increased variability in nutritional status in field plots, which may influence the balance between abiotic and biotic stresses (diseases) and interact with disease on individual varieties, as well as the influence of weeds and diverse crops (variety mixtures and composite cross populations). The presence of disease in organic and low-input cropping systems may be underestimated because abiotic stresses, which enhance a general senescence of leaves, may obscure disease assessment, in particular disease on leaves. Weeds may interact by harbouring disease showing similar symptoms as on the target crop, or by ‘diluting’ disease by additional healthy green leaf area of the ‘crop’ like in a variety mixture. Other general topics such as differences between host/pathogen systems, timing of assessment, assessment scale, and interpretation and analysis of data are also discussed

Sortsblandingers udbyttestabilitet og udbyttepotentiale

Højere udbytte og bedre udbyttestabilitet er ofte fundet i sortsblandinger i vårbyg sammenlignet med målestandarder og komponentsorter, bl.a. i FØJO II projektet BAROF

Anvendelse af ufuldstændige blokforsøg

I forsøg med mange forsøgsled, forsøg på uensartede arealer og forsøg, som af praktiske grunde skal opdeles på mindre enheder, vil det ofte være fordelagtigt at anvende blokke, som ikke indeholder alle forsøgsled. Sådanne ufuldstændige blokke kan konstrueres efter flere forskellige principper. I enfaktorielle forsøg anvendes oftest metoder, som sikrer, at alle par af forsøgsled kan sammenlignes med den samme (og bedst mulige) sikkerhed, mens man i flerfaktorielle forsøg oftest anvender metoder, som sikrer, at de mest interessante effekter (hoved- og/eller vekselvirkninger) kan estimeres bedst muligt. Artiklen viser tre eksempler på anvendelse af ufuldstændige blokforsøg: 1) Sortsforsøg i ærter (enfaktoriel), 2) Frøavlsforsøg med strandsvingel (trefaktoriel) og 3) Forsøg med svampemidler i byg (tofaktorielt split-plot). For hver af disse vises den benyttede plan samt effekten af at benytte planen i stedet et randomiseret blokforsøg med fuldstændige blokke

Role of Hydrophobicity at the N-Terminal Region of Aβ42 in Secondary Nucleation.

The self-assembly of the amyloid β 42 (Aβ42) peptide is linked to Alzheimer's disease, and oligomeric intermediates are linked to neuronal cell death during the pathology of the disease. These oligomers are produced prolifically during secondary nucleation, by which the aggregation of monomers is catalyzed on fibril surfaces. Significant progress has been made in understanding the aggregation mechanism of Aβ42; still, a detailed molecular-level understanding of secondary nucleation is lacking. Here, we explore the role of four hydrophobic residues on the unstructured N-terminal region of Aβ42 in secondary nucleation. We create eight mutants with single substitutions at one of the four positions─Ala2, Phe4, Tyr10, and Val12─to decrease the hydrophobicity at respective positions (A2T, A2S, F4A, F4S, Y10A, Y10S, V12A, and V12S) and one mutant (Y10F) to remove the polar nature of Tyr10. Kinetic analyses of aggregation data reveal that the hydrophobicity at the N-terminal region of Aβ42, especially at positions 10 and 12, affects the rate of fibril mass generated via secondary nucleation. Cryo-electron micrographs reveal that most of the mutants with lower hydrophobicity form fibrils that are markedly longer than WT Aβ42, in line with the reduced secondary nucleation rates for these peptides. The dominance of secondary nucleation, however, is still retained in the aggregation mechanism of these mutants because the rate of primary nucleation is even more reduced. This highlights that secondary nucleation is a general phenomenon that is not dependent on any one particular feature of the peptide and is rather robust to sequence perturbations