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Molecular programs initiating cell fate divergence (CFD) are difficult to identify. Current approaches usually compare cells long after CFD initiation, therefore missing molecular changes at its start. Ideally, single cells that differ in their CFD molecular program but are otherwise identical are compared early in CFD. This is possible in diverging sister cells, which were identical until their mother’s division and thus differ mainly in CFD properties. In asymmetrically dividing cells, divergent daughter fates are prospectively committed during division, and diverging sisters can thus be identified at the start of CFD. Using asymmetrically dividing blood stem cells, we developed a pipeline (ie, trackSeq) for imaging, tracking, isolating, and transcriptome sequencing of single cells. Their identities, kinship, and histories are maintained throughout, massively improving molecular noise filtering and candidate identification. In addition to many identified blood stem CFD regulators, we offer here this pipeline for use in CFDs other than asymmetric division.

Estonian rural tourism partnership sustainability is analysed according to the tourism partnership life cycle model, which employs qualitative methodology. Leadership, confusing aims, decreasing communication, time availability, uncertain funding, institutional changes and lack of collaboration with urban centre – trigger deceleration of partnership and therefore influence partnership sustainability.

Die molekulare Bildgebung mit FDG-PET/CT stellt ein wertvolles Instrument zur Tumorlokalisation, Ausbreitungsdiagnostik und Therapiekontrolle dar. International ist ein breites Indikationsspektrum etabliert, während das deutsche Gesundheitssystem eine deutlich restriktivere Position vertritt. Die Translation innovativer Bildgebungsansätze in die klinische Medizin ist ohne geeignete Förder und Evaluationsinstrumente problematisch.

The adsorption of β-casein at hydrophobic and hydrophilic silica surfaces has been studied by time-resolved ellipsometry. Marked differences in, e.g., adsorption kinetics and plateau adsorption coverage, were observed on the two types of surfaces. The miscellaneous adsorption mechanisms at the two surfaces resulted in different structures of the adsorbed layers as evident from the thicknesses and protein densities measured on the two substrates as well as the effect on the adsorbed layer properties of a subsequently added specific proteolytic enzyme, endoproteinase Asp-N. At the hydrophobic surface, the adsorption is fast and the surface is saturated within a relatively short period. The addition of endoproteinase Asp-N reduces the surface excess and the thickness by 24 and 45%, respectively. This corresponds to cleavage at amino acid residues 43 and/or 47 in the hydrophilic portion of the protein. Adsorption from solutions containing added electrolyte leads to significant increase of the surface excess. However, no significant change was observed in the ellipsometric layer thickness. At constant ionic strength, the surface excess increased in the order NaCl < MgCl2 < CaCl2. From the experimental evidence, it was concluded that the adsorbed layer structure at the hydrophobic surface can be described as a monolayer with an inner dense region comprising the relatively large hydrophobic portions of the protein molecules and an outer region of the highly charged N-terminal portions protruding into the aqueous phase. The adsorption kinetics at the hydrophilic silica surface, although initially the same as on the hydrophobic surface, was found to be much slower and plateau surface excess values were not reached even after 2 h of adsorption. This suggests that substantial rearrangements of the protein molecules take place within the adsorbed layer during the adsorption process. Although the maximum surface excess at the hydrophilic surface of 4.3 mg m^-2 is higher than the value of 2.8 mg m^-2 measured at the hydrophobic surface, the thickness is slightly smaller, i.e., 60 Å and 66 Å, respectively. Hence, the protein adopt a more compact structure at the hydrophilic surface, at least in the inner part of the adsorbed layer. The different structure at the hydrophilic surface was confirmed by the larger reduction of the surface excess and layer thickness associated with the addition of endoproteinase Asp-N, leaving a very thin compact layer at the surface.