MVibCode: Multi-Channel Vibrotactile Codec Using Hierarchical Perceptual Clustering.

To achieve convincing remote vibrotactile experiences, it is necessary to transmit a large number of signal channels corresponding to dense interaction points on the human skin. This leads to a dramatic increase in the amount of data to be transmitted. In order to cope with these data efficiently, vibrotactile codecs have to be used to reduce the data rate demands.

Quality Enhancement of Compressed Vibrotactile Signals Using Recurrent Neural Networks and Residual Learning.

We present a neural network-based compression artifact removal technique for vibrotactile signals. The proposed decoder-side quality enhancement approach is based on recurrent neural networks (RNNs) and the principle of residual learning. We use a total of 8 nonlinear RNN layers trained to first estimate the difference between the original and the compressed signal.

Perceptual Quality Assessment of Compressed Vibrotactile Signals Through Comparative Judgment.

In this article, we present a comprehensive scheme for the quality assessment of compressed vibrotactile signals with human assessors. Inspired by the multiple stimulus test with hidden reference and anchors (MUSHRA) from the audio domain, we designed a method in which each compressed signal is compared to its original signal and rated on a numerical scale. For each signal tested, the hidden reference and two anchor signals are used to validate the results and provide assessor screening criteria.

Adaptive Equalization of Vibrotactile Actuators.

In order to provide convincing artifical touch sensations, humans should be presented with high quality haptic stimuli. In the vibrotactile domain, signals are usually displayed through mechanical actuators. Current high quality actuators exhibit a high dynamic range and have the ability to display a wide range of frequencies.

A Tactile Computer Mouse for the Display of Surface Material Properties.

We present a novel input/output device to display the tactile properties of surface materials. The proposed Tactile Computer Mouse (TCM) is equipped with a series of actuators that can create perceptually relevant tactile cues to a user. The display capabilities of our TCM match the major tactile dimensions in human surface material perception, namely, hardness, friction, warmth, microscopic roughness, and macroscopic roughness.

Interference between p53 and cdc25C in cell cycle regulation.

The eukaryotic cell cycle is regulated by a network of different protein kinases and phosphatases which are by various mechanisms linked to the growth suppressor p53. Cell cycle regulation is quite similar from yeast to man. Although there is no endogenous p53 in yeast expression of human p53 led to growth arrest of yeast cells which can be suppressed by simultaneous overexpression of cdc25C, a phosphatase regulating entry into mitosis.

The G2/M checkpoint phosphatase cdc25C is located within centrosomes.

cdc25C is a phosphatase which regulates the activity of the mitosis promoting factor cyclin B/cdk1 by dephosphorylation, thus triggering G(2)/M transition. The activity and the sub-cellular localisation of cdc25C are regulated by phosphorylation. It is well accepted that cdc25C has to enter the nucleus to activate the cyclin B/cdk1 complex at G(2)/M transition.

The mitotic phosphatase cdc25C at the Golgi apparatus.

cdc25C is a phosphatase which regulates the activity of the mitosis promoting factor cyclin B/cdk1 by dephosphorylation, thus triggering G(2)/M transition. The activity of cdc25C is regulated by phosphorylation which by itself is implicated in regulating the subcellular localization. It is well accepted that cdc25C has to enter the nucleus to activate the cyclin B/cdk1 complex at G(2)/M transition.

Mutation of a CK2 phosphorylation site in cdc25C impairs importin alpha/beta binding and results in cytoplasmic retention.

cdc25C is a phosphatase, which activates the mitosis-promoting factor cyclin B1/cdc2 by dephosphorylation, and thus triggers G(2)/M transition. The activity of cdc25C itself is controlled by phosphorylation of certain amino-acid residues, which among other things determines the subcellular localization of the enzyme. Here, we describe a new phosphorylation site at threonine 236 of cdc25C, which is phosphorylated by protein kinase CK2.