Energy-Efficient Cooperative Spectrum Sensing Using Machine Learning Algorithm.

Cognitive Radio (CR) is a practical technique for overcoming spectrum inefficiencies by sensing and utilizing spectrum holes over a wide spectrum. In particular, cooperative spectrum sensing (CSS) determines the state of primary users (PUs) by cooperating with multiple secondary users (SUs) distributed around a Cognitive Radio Network (CRN), further overcoming various noise and fading issues in the radio environment. But it's still challenging to balance energy efficiency and good sensing performances in the existing CSS system, especially when the CRN consists of battery-limited sensors.

Assessing the role of the cadherin/catenin complex at the Schwann cell-axon interface and in the initiation of myelination.

Myelination is dependent on complex reciprocal interactions between the Schwann cell (SC) and axon. Recent evidence suggests that the SC-axon interface represents a membrane specialization essential for myelination; however, the manner in which this polarized-apical domain is generated remains a mystery. The cell adhesion molecule N-cadherin is enriched at the SC-axon interface and colocalizes with the polarity protein Par-3.

Anterograde transport and secretion of brain-derived neurotrophic factor along sensory axons promote Schwann cell myelination.

The neurotrophin brain-derived neurotrophic factor (BDNF) inhibits Schwann cell (SC) migration and promotes myelination via the p75 neurotrophin receptor (NTR). Despite these recent findings, the expression, localization, and mechanism of BDNF action has yet to be determined. Here we demonstrate that the sensory neurons of the dorsal root ganglion (DRG) are a major source of BDNF during postnatal development.

The quest for remyelination: a new role for neurotrophins and their receptors.

The formation of myelin is dependent on a reciprocal and intimate relationship between neurons and the myelin-forming glia. Recently, the neurotrophin family of growth factors has been shown to regulate the complex cell-cell interactions that control myelination. Neurotrophins and their receptors influence myelin formation via two distinct mechanisms, either by acting on the neurons, changing the axonal signals that control myelination, or by acting directly on the myelin-forming glia.

The polarity protein Par-3 directly interacts with p75NTR to regulate myelination.

Cell polarity is critical in various cellular processes ranging from cell migration to asymmetric cell division and axon and dendrite specification. Similarly, myelination by Schwann cells is polarized, but the mechanisms involved remain unclear. Here, we show that the polarity protein Par-3 localizes asymmetrically in Schwann cells at the axon-glial junction and that disruption of Par-3 localization, by overexpression and knockdown, inhibits myelination.

Steroid hormone signaling between Schwann cells and neurons regulates the rate of myelin synthesis.

Fluorescence digital imaging microscopy was used to develop a method that allows the continuous monitoring and quantitative measurement of a single myelin internode throughout its development. Using this technique, steroid hormones such as progesterone and dexamethasone were shown to reduce the time required for the initiation and to regulate the rate of myelin synthesis. Progesterone was capable of increasing the rate of myelin synthesis in Schwann cell/neuronal co-cultures in a dose-dependent manner.

Caveolin scaffolding region and the membrane binding region of SRC form lateral membrane domains.

Formation of domains by the membrane binding motifs of caveolin and src were studied in large unilamellar vesicles using fluorescence digital imaging microscopy. Caveolin, a major structural protein of caveolae, contains a scaffolding region (residues 82-101) that contributes to the binding of the protein to the plasma membrane. A caveolin peptide (82-101) corresponding to this scaffolding region induced the formation of membrane domains enriched in the acidic lipids phosphatidylserine and phosphatidylinositol-4,5-bisphosphate.