University of Southern Denmark

About: University of Southern Denmark is a education organization based out in Odense, Syddanmark, Denmark. It is known for research contribution in the topics: Population & Randomized controlled trial. The organization has 11928 authors who have published 37918 publications receiving 1258559 citations. The organization is also known as: SDU.

Radiation guiding with surface plasmon polaritons

Abstract: Surface plasmon polaritons (SPPs) are electromagnetic (EM) modes propagating along metal‐dielectric interfaces, in which surface collective excitations of free electrons in the metal are coupled to evanescent EM fields in the dielectric. Various SPP modes can be supported by flat and curved, single and multiple surfaces, exhibiting remarkable properties, including the possibility of concentrating EM fields beyond the diffraction limit, i.e. on the nanoscale, while enhancing local field strengths by several orders of magnitude. This unique feature of SPP modes, along with the ever-increasing demands for miniaturization of photonic components and circuits, generates an exponentially growing interest in SPP-mediated radiation guiding and SPP-based waveguide components. Here we review the current status of this rapidly developing field, starting with a brief presentation of the main planar SPP modes along with the techniques employed for their excitation and manipulation by sets of nanoparticles. We then describe in detail various SPP-based waveguide configurations that ensure two-dimensional mode confinement in the plane perpendicular to the propagation direction and compare their characteristics. Excitation of SPP waveguide modes and recent progress in the development of SPP-based waveguide components are also discussed, concluding with our outlook on challenges and possible future developments in this field. (Some figures may appear in colour only in the online journal) This article was invited by Horst-Guenter Rubahn.

Face masks considerably reduce COVID-19 cases in Germany.

Abstract: We use the synthetic control method to analyze the effect of face masks on the spread of COVID-19 in Germany. Our identification approach exploits regional variation in the point in time when wearing of face masks became mandatory in public transport and shops. Depending on the region we consider, we find that face masks reduced the number of newly registered severe acute respiratory syndrome coronavirus 2 infections between 15% and 75% over a period of 20 days after their mandatory introduction. Assessing the credibility of the various estimates, we conclude that face masks reduce the daily growth rate of reported infections by around 47%.

Adverse effects of methylmercury: environmental health research implications.

Abstract: BackgroundThe scientific discoveries of health risks resulting from methylmercury exposure began in 1865 describing ataxia, dysarthria, constriction of visual fields, impaired hearing, and sensory ...

Gemin3 A Novel Dead Box Protein That Interacts with Smn, the Spinal Muscular Atrophy Gene Product, and Is a Component of Gems

Abstract: The survival of motor neurons (SMN) gene is the disease gene of spinal muscular atrophy (SMA), a common motor neuron degenerative disease. The SMN protein is part of a complex containing several proteins, of which one, SIP1 (SMN interacting protein 1), has been characterized so far. The SMN complex is found in both the cytoplasm and in the nucleus, where it is concentrated in bodies called gems. In the cytoplasm, SMN and SIP1 interact with the Sm core proteins of spliceosomal small nuclear ribonucleoproteins (snRNPs), and they play a critical role in snRNP assembly. In the nucleus, SMN is required for pre-mRNA splicing, likely by serving in the regeneration of snRNPs. Here, we report the identification of another component of the SMN complex, a novel DEAD box putative RNA helicase, named Gemin3. Gemin3 interacts directly with SMN, as well as with SmB, SmD2, and SmD3. Immunolocalization studies using mAbs to Gemin3 show that it colocalizes with SMN in gems. Gemin3 binds SMN via its unique COOH-terminal domain, and SMN mutations found in some SMA patients strongly reduce this interaction. The presence of a DEAD box motif in Gemin3 suggests that it may provide the catalytic activity that plays a critical role in the function of the SMN complex on RNPs.