Laminar signal extraction over extended cortical areas by means of a spatial GLM.

There is converging evidence that distinct neuronal processes leave distinguishable footprints in the laminar BOLD response. However, even though the achievable spatial resolution in functional MRI has much improved over the years, it is still challenging to separate signals arising from different cortical layers. In this work, we propose a new method to extract laminar signals.

A biologically plausible mechanism for neuronal coding organized by the phase of alpha oscillations.

The visual system receives a wealth of sensory information of which only little is relevant for behaviour. We present a mechanism in which alpha oscillations serve to prioritize different components of visual information. By way of simulated neuronal networks, we show that inhibitory modulation in the alpha range (~ 10 Hz) can serve to temporally segment the visual information to prevent information overload.

Adhesion forces in the self-recognition of oligosaccharide epitopes of the proteoglycan aggregation factor of the marine sponge Microciona prolifera.

Cell aggregation in the marine sponge Microciona prolifera is mediated by a multimillion molecular-mass aggregation factor, termed MAF. Earlier investigations revealed that the cell aggregation activity of MAF depends on two functional domains: (i) a Ca(2+)-independent cell-binding domain and (ii) a Ca(2+)-dependent proteoglycan self-interaction domain. Structural analysis of involved carbohydrate fragments of the proteoglycan in the self-association established a sulfated disaccharide beta-D: -GlcpNAc3S-(1-->3)-alpha-L: -Fucp and a pyruvated trisaccharide beta-D: -Galp4,6(R)Pyr-(1-->4)-beta-D: -GlcpNAc-(1-->3)-alpha-L: -Fucp.

Domain formation in phosphatidylcholine bilayers containing transmembrane peptides: specific effects of flanking residues.

Lateral segregation in biological membranes leads to the formation of domains. We have studied the lateral segregation in gel-state model membranes consisting of supported dipalmitoylphosphatidylcholine (DPPC) bilayers with various model peptides, using atomic force microscopy (AFM). The model peptides are derivatives of the Ac-GWWL(AL)(n)WWA-Etn peptides (the so-called WALP peptides) and have instead of tryptophans, other flanking residues.