Experiment Preparation and Performance for the Electromagnetic Levitator (EML) Onboard the International Space Station

The electromagnetic levitation (EML) facility on board the ISS is a powerful tool for investigation of solidification phenomena of metallic melts and precise measurement of thermophysical properties of the liquid. Containerless processing enables deep undercoolings prior to solidification and the analysis of crystal nucleation and growth phenomena. The microgravity environment allows studying these processes under reduced fluid flow and moreover under different levels of melt convection by systematic variation of electromagnetic stirring. Material properties like density, specific heat, surface tension, viscosity, thermal and electrical conductivity of liquid metals and semiconductors are determined in the absence of disturbances caused by container walls and gravity forces. Scientists are supported by facility and mission specialists for preparation and performance, which is decisive for successful operation on orbit. User support comprises the determination of material data, development of experiment procedure, parameter sets and their validation in the ground model as well as the conduction of space experiments by real-time monitoring and control. The comprehensive support program for the entire life cycle of science project from experiment definition to its operation ensures high-quality data and an optimum of scientific results

A Multi-dimensional Analysis of Managers' Power - Functional, Socio-political, Interpretive-discursive, and Socio-cultural Approaches

Managers' power within organisations has been analysed by several approaches: Orthodox management and organisation studies ('functional approach'), Critical Management Studies ('socio-political approaches'), interpretive, discourse-oriented and constructivist concepts ('interpretive-discursive approaches'), and anthropological, socio-psychological and sociological approaches ('socio-cultural approaches'). In organisational reality functional, socio-political, interpretive-discursive, and socio-cultural aspects are closely related and intertwined. However, because of division of intellectual labour, probably more because of different worldviews, researchers often make use of these approaches quite selectively. Such focussing has its advantages but also weaknesses. This paper therefore argues that it often helps to investigate complex phenomena such as managers' power in multi-dimensional ways.div_BaMAbercrombie, N./Hill, S./Turner, B. S. (1980): The Dominant Ideology Thesis. 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Myosin 1c and myosin IIB serve opposing roles in lamellipodial dynamics of the neuronal growth cone

The myosin family of motor proteins is implicated in mediating actin-based growth cone motility, but the roles of many myosins remain unclear. We previously implicated myosin 1c (M1c; formerly myosin Iβ) in the retention of lamellipodia (Wang et al., 1996). Here we address the role of myosin II (MII) in chick dorsal root ganglion neuronal growth cone motility and the contribution of M1c and MII to retrograde F-actin flow using chromophore-assisted laser inactivation (CALI). CALI of MII reduced neurite outgrowth and growth cone area by 25%, suggesting a role for MII in lamellipodial expansion. Micro-CALI of MII caused a rapid reduction in local lamellipodial protrusion in growth cones with no effects on filopodial dynamics. This is opposite to micro-CALI of M1c, which caused an increase in lamellipodial protrusion. We used fiduciary beads (Forscher et al., 1992) to observe retrograde F-actin flow during the acute loss of M1c or MII. Micro-CALI of M1c reduced retrograde bead flow by 76%, whereas micro-CALI of MII or the MIIB isoform did not. Thus, M1c and MIIB serve opposite and nonredundant roles in regulating lamellipodial dynamics, and M1c activity is specifically required for retrograde F-actin flow

First evidence of overlaps between HIV-Associated Dementia (HAD) and non-viral neurodegenerative diseases: proteomic analysis of the frontal cortex from HIV+ patients with and without dementia

<p>Abstract</p> <p>Background</p> <p>The pathogenesis of HIV-associated dementia (HAD) is poorly understood. To date, detailed proteomic fingerprinting directly from autopsied brain tissues of HAD and HIV non-dementia patients has not been performed.</p> <p>Result</p> <p>Here, we have analyzed total proteins from the frontal cortex of 9 HAD and 5 HIV non-dementia patients. Using 2-Dimensional differential in-gel electrophoresis (2-DIGE) to analyze the brain tissue proteome, 76 differentially expressed proteins (p < 0.05; fold change>1.25) were identified between HAD and HIV non-dementia patients, of which 36 protein spots (based on 3D appearance of spots on the images) were chosen for the mass spectrometry analysis. The large majority of identified proteins were represented in the energy metabolic (mitochondria) and signal transduction pathways. Furthermore, over 90% of the protein candidates are common to both HAD and other non-viral neurodegenerative disease, such as Alzheimer's disease. The data was further validated using specific antibodies to 4 proteins (CA2, GS, CKMT and CRMP2) by western blot (WB) in the same samples used for 2D-DIGE, with additional confirmation by immunohistochemitsry (IHC) using frontal lobe tissue from different HAD and HIV+ non-dementia patients. The validation for all 4 antibodies by WB and IHC was in concordance with the DIGE results, lending further credence to the current findings.</p> <p>Conclusion</p> <p>These results suggest not only convergent pathogenetic pathways for the two diseases but also the possibility of increased Alzheimer's disease (AD) susceptibility in HAD patients whose life expectancy has been significantly increased by highly active antiretroviral therapy.</p

Synthetic and mechanistic studies into the reductive functionalization of nitro compounds catalyzed by an Iion(salen) complex

We report on the use of a simple, bench-stable [Fe(salen)2]-μ-oxo precatalyst in the reduction of nitro compounds. The reaction proceeds at room temperature across a range of substrates, including nitro aromatics and aliphatics. By changing the reducing agent from pinacol borane (HBpin) to phenyl silane (H3SiPh), we can chemoselectively reduce nitro compounds while retaining carbonyl functionality. Our mechanistic studies, which include kinetics, electron paramagnetic resonance (EPR), mass spectrometry, and quantum chemistry, indicate the presence of a nitroso intermediate and the generation of an on-cycle iron hydride as a key catalytic intermediate. Based on this mechanistic insight, we were able to extend the chemistry to hydroamination and identified a simple substrate feature (alkene lowest unoccupied molecular orbital (LUMO) energy) that could be used to predict which alkenes would result in productive catalysis

Altered distribution of mucosal NK cells during HIV infection

The human gut mucosa is a major site of HIV infection and infection-associated pathogenesis. Increasing evidence shows that natural killer (NK) cells play an important role in control of HIV infection but the mechanism(s) by which they mediate antiviral activity in the gut is unclear. Here we show two distinct subsets of NK cells exist in the gut, one localized to intraepithelial spaces (IEL) and the other to the lamina propria (LP). The frequency of both subsets of NK cells was reduced in chronic infection, whereas IEL NK cells remained stable in spontaneous controllers with protective KIR/HLA genotypes. Both IEL and LP NK cells were significantly expanded in immunologic non-responsive (INR) patients, who incompletely recovered CD4+ T cells on HAART. These data suggest that both IEL and LP NK cells may expand in the gut in an effort to compensate for compromised CD4+ T cell recovery, but that only IEL NK cells may be involved in providing durable control of HIV in the gut

New twist on the regulation of NKG2D ligand expression

The NK cell–activating receptor NKG2D plays a prominent role in antitumor immune responses. Expression of the multiple NKG2D ligands must be tightly controlled to guarantee that NK cells attack tumors but not healthy cells. New data reveal a novel mechanism of posttranslational regulation of the mouse NKG2D ligand MULT1, in which MULT1 is ubiquitinated and degraded in healthy cells. In response to UV stress or heat shock, ubiquitination of MULT1 decreases and cell surface expression increases. Thus, targeting the ubiquitination machinery in cancer cells might increase the susceptibility of tumors to NK cell–mediated killing

Mouse nuclear myosin I knock-out shows interchangeability and redundancy of myosin isoforms in the cell nucleus.

Nuclear myosin I (NM1) is a nuclear isoform of the well-known "cytoplasmic" Myosin 1c protein (Myo1c). Located on the 11(th) chromosome in mice, NM1 results from an alternative start of transcription of the Myo1c gene adding an extra 16 amino acids at the N-terminus. Previous studies revealed its roles in RNA Polymerase I and RNA Polymerase II transcription, chromatin remodeling, and chromosomal movements. Its nuclear localization signal is localized in the middle of the molecule and therefore directs both Myosin 1c isoforms to the nucleus. In order to trace specific functions of the NM1 isoform, we generated mice lacking the NM1 start codon without affecting the cytoplasmic Myo1c protein. Mutant mice were analyzed in a comprehensive phenotypic screen in cooperation with the German Mouse Clinic. Strikingly, no obvious phenotype related to previously described functions has been observed. However, we found minor changes in bone mineral density and the number and size of red blood cells in knock-out mice, which are most probably not related to previously described functions of NM1 in the nucleus. In Myo1c/NM1 depleted U2OS cells, the level of Pol I transcription was restored by overexpression of shRNA-resistant mouse Myo1c. Moreover, we found Myo1c interacting with Pol II. The ratio between Myo1c and NM1 proteins were similar in the nucleus and deletion of NM1 did not cause any compensatory overexpression of Myo1c protein. We observed that Myo1c can replace NM1 in its nuclear functions. Amount of both proteins is nearly equal and NM1 knock-out does not cause any compensatory overexpression of Myo1c. We therefore suggest that both isoforms can substitute each other in nuclear processes