A brain-computer interface (BCI) is a communication system that translates brain-activity into commands for a computer or other devices. In other words, a BCI allows users to act on their environment by using only brain-activity, without using peripheral nerves and muscles. In this paper, we present a BCI that achieves high classification accuracy and high bitrates for both disabled and able-bodied subjects. The system is based on the P300 evoked potential and is tested with five severely disabled and four able-bodied subjects. For four of the disabled subjects classification accuracies of 100% are obtained. The bitrates obtained for the disabled subjects range between 10 and 25bits/min. The effect of different electrode configurations and machine learning algorithms on classification accuracy is tested. Further factors that are possibly important for obtaining good classification accuracy in P300-based BCI systems for disabled subjects are discussed.
Presence of IPH on MRI strongly predicts cerebrovascular events. Homogenization of future studies is warranted to allow for sufficient assessment of level of evidence for intervention trials.
Individual rate constants for the interaction of H-, K-, and N-Ras with GAP-334 and NF1-333 were determined using fluorescent derivatives of guanine nucleotides at the active site of the Ras proteins. Stopped-flow experiments with NF1-333 show a fast concentration-dependent initial phase corresponding to the binding reaction followed by a slower phase, which corresponds to the hydrolysis reaction. With Ras bound to the nonhydrolyzable analogue mant-GppNHp, only the concentration-dependent first phase was observed. The Ras x mant-GppNHp x NF1-333 complexes were also used to measure dissociation rate constants of the Ras-GAP complexes. Using GAP-334 as the catalyst, the concentration-dependent first phase was too fast to be measured by the stopped-flow method, but the subsequent chemical cleavage reaction occurred at a similar rate (5-10 s(-1)) to that seen with NF1-333. With both GAP-334 and NF1-333, after rapidly reaching the initial equilibrium, there was no further time-dependent change on mixing GAPs with Ras x mant-GppNHp. The results obtained provide new insights into the individual steps of the GAP-catalyzed GTPase reaction on Ras. They do not require the postulation of a rate-limiting step occurring before GTP hydrolysis.
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