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5,854 result(s) for "Hansen, G"
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The Sustainability Balanced Scorecard: A Systematic Review of Architectures
The increasing strategic importance of environmental, social and ethical issues as well as related performance measures has spurred interest in corporate sustainability performance measurement and management systems. This paper focuses on the balanced scorecard (BSC), a performance measurement and management system aiming at balancing financial and non-financial as well as short and long-term measures. Modifications to the original BSC which explicitly consider environmental, social or ethical issues are often referred to as sustainability balanced scorecards (SBSCs). There is much scholarly discussion about SB SC architecture and how it can be designed to relate performance dimensions, strategic objectives and the logical links among these elements. To synthesise the widely scattered research findings and publications on the SBSC, we conducted a thematic analysis based on a systematic literature review containing 69 relevant articles spanning a period of two decades. We found that sustainability-oriented modifications of the BSC architecture are motivated by instrumental, social/political or normative theoretical perspectives. Moreover, these modifications can be mapped with a typology of generic SBSC architectures. The first dimension of the typology describes the hierarchy between performance perspectives and strategic objectives and how it is related to the organisational value system. The second dimension describes how sustainability-related strategic objectives are integrated into SBSC performance perspectives and how this is related to corporate sustainability strategy. This study contributes to the development of the emerging SBSC literature and practice and, more generally, to research on corporate sustainability performance measurement and management. We conclude with a research agenda and implications for management.
Controlled multi-photon subtraction with cascaded Rydberg superatoms as single-photon absorbers
The preparation of light pulses with well-defined quantum properties requires precise control at the individual photon level. Here, we demonstrate exact and controlled multi-photon subtraction from incoming light pulses. We employ a cascaded system of tightly confined cold atom ensembles with strong, collectively enhanced coupling of photons to Rydberg states. The excitation blockade resulting from interactions between Rydberg atoms limits photon absorption to one per ensemble and rapid dephasing of the collective excitation suppresses stimulated re-emission of the photon. We experimentally demonstrate subtraction with up to three absorbers. Furthermore, we present a thorough theoretical analysis of our scheme where we identify weak Raman decay of the long-lived Rydberg state as the main source of infidelity in the subtracted photon number and investigate the performance of the multi-photon subtractor for increasing absorber numbers in the presence of Raman decay. Interaction of photons with Rydberg atoms can be used to modify quantum states of light. Here the authors demonstrate a controlled nonlinear quantum behavior of multi-photon subtraction in a cascaded system based on Rydberg superatoms.
Tuning the activity of Pt alloy electrocatalysts by means of the lanthanide contraction
The high platinum loadings required to compensate for the slow kinetics of the oxygen reduction reaction (ORR) impede the widespread uptake of low-temperature fuel cells in automotive vehicles. We have studied the ORR on eight platinum (Pt)–lanthanide and Pt-alkaline earth electrodes, Pt₅M, where M is lanthanum, cerium, samarium, gadolinium, terbium, dysprosium, thulium, or calcium. The materials are among the most active polycrystalline Pt-based catalysts reported, presenting activity enhancement by a factor of 3 to 6 over Pt. The active phase consists of a Pt overlayer formed by acid leaching. The ORR activity versus the bulk lattice parameter follows a high peaked \"volcano\" relation. We demonstrate how the lanthanide contraction can be used to control strain effects and tune the activity, stability, and reactivity of these materials.
Proton–electron mass ratio by high-resolution optical spectroscopy of ion ensembles in the resolved-carrier regime
Optical spectroscopy in the gas phase is a key tool for elucidating the structure of atoms and molecules and their interaction with external fields. The line resolution is usually limited by a combination of first-order Doppler broadening due to particle thermal motion and a short transit time through the excitation beam. For trapped particles, suitable laser cooling techniques can lead to strong confinement (the Lamb–Dicke regime) and thus to optical spectroscopy free of these effects. For non-laser-coolable spectroscopy ions, this has so far only been achieved when trapping one or two atomic ions, together with a single laser-coolable atomic ion1,2. Here we show that one-photon optical spectroscopy free of Doppler and transit broadening can also be obtained with more easily prepared ensembles of ions, if performed with mid-infrared radiation. We demonstrate the method on molecular ions. We trap ~100 molecular hydrogen ions (HD+) within a Coulomb cluster of a few thousand laser-cooled atomic ions and perform laser spectroscopy of the fundamental vibrational transition. Transition frequencies were determined with a lowest uncertainty of 3.3 × 10−12 fractionally. As an application, we determine the proton–electron mass ratio by matching a precise ab initio calculation with the measured vibrational frequency.Laser spectroscopy can resolve vibrational transitions of molecular hydrogen ions without Doppler broadening when these are trapped within a cluster of laser-cooled atomic ions.
Rapid and efficient induction of functional astrocytes from human pluripotent stem cells
The derivation of astrocytes from human pluripotent stem cells is currently slow and inefficient. We demonstrate that overexpression of the transcription factors SOX9 and NFIB in human pluripotent stem cells rapidly and efficiently yields homogeneous populations of induced astrocytes. In our study these cells exhibited molecular and functional properties resembling those of adult human astrocytes and were deemed suitable for disease modeling. Our method provides new possibilities for the study of human astrocytes in health and disease.
Balanced mitochondrial and cytosolic translatomes underlie the biogenesis of human respiratory complexes
Background Oxidative phosphorylation (OXPHOS) complexes consist of nuclear and mitochondrial DNA-encoded subunits. Their biogenesis requires cross-compartment gene regulation to mitigate the accumulation of disproportionate subunits. To determine how human cells coordinate mitochondrial and nuclear gene expression processes, we tailored ribosome profiling for the unique features of the human mitoribosome. Results We resolve features of mitochondrial translation initiation and identify a small ORF in the 3′ UTR of MT-ND5 . Analysis of ribosome footprints in five cell types reveals that average mitochondrial synthesis levels correspond precisely to cytosolic levels across OXPHOS complexes, and these average rates reflect the relative abundances of the complexes. Balanced mitochondrial and cytosolic synthesis does not rely on rapid feedback between the two translation systems, and imbalance caused by mitochondrial translation deficiency is associated with the induction of proteotoxicity pathways. Conclusions Based on our findings, we propose that human OXPHOS complexes are synthesized proportionally to each other, with mitonuclear balance relying on the regulation of OXPHOS subunit translation across cellular compartments, which may represent a proteostasis vulnerability.
An ER surface retrieval pathway safeguards the import of mitochondrial membrane proteins in yeast
Eukaryotic cells contain membrane-bound organelles, defined by distinct protein compositions. Almost all cellular proteins are synthesized in the cytosol, and thus, organelle-resident proteins must be directed to their appropriate location after synthesis. Working in yeast, Hansen et al. identified a protein-targeting paradigm termed ER-SURF, in which the membrane expanse of the endoplasmic reticulum (ER) serves as a “capture net” for mitochondrial proteins. This process productively redirected mitochondrial precursor proteins for efficient mitochondrial import. Thus, two distinct organelles, once thought to be mutually exclusive protein destinations, can cooperate during protein targeting. Science , this issue p. 1118 The endoplasmic reticulum surface plays a part in the productive targeting of membrane proteins to mitochondria. The majority of organellar proteins are translated on cytosolic ribosomes and must be sorted correctly to function. Targeting routes have been identified for organelles such as peroxisomes and the endoplasmic reticulum (ER). However, little is known about the initial steps of targeting of mitochondrial proteins. In this study, we used a genome-wide screen in yeast and identified factors critical for the intracellular sorting of the mitochondrial inner membrane protein Oxa1. The screen uncovered an unexpected path, termed ER-SURF, for targeting of mitochondrial membrane proteins. This pathway retrieves mitochondrial proteins from the ER surface and reroutes them to mitochondria with the aid of the ER-localized chaperone Djp1. Hence, cells use the expanse of the ER surfaces as a fail-safe to maximize productive mitochondrial protein targeting.
Rotational spectroscopy of cold and trapped molecular ions in the Lamb–Dicke regime
Sympathetic cooling of trapped ions has been established as a powerful technique for the manipulation of non-laser-coolable ions1–4. For molecular ions, it promises vastly enhanced spectroscopic resolution and accuracy. However, this potential remains untapped so far, with the best resolution achieved being not better than 5 × 10−8 fractionally, due to residual Doppler broadening being present in ion clusters even at the lowest achievable translational temperatures5. Here we introduce a general and accessible approach that enables Doppler-free rotational spectroscopy. It makes use of the strong radial spatial confinement of molecular ions when trapped and crystallized in a linear quadrupole trap, providing the Lamb–Dicke regime for rotational transitions. We achieve a linewidth of 1 × 10−9 fractionally and 1.3 kHz absolute, an improvement of ≃50-fold over the previous highest resolution in rotational spectroscopy. As an application, we demonstrate the most precise test of ab initio molecular theory and the most accurate (1.3 × 10−9) determination of the proton mass using molecular spectroscopy. The results represent the long overdue extension of Doppler-free microwave spectroscopy of laser-cooled atomic ion clusters6 to higher spectroscopy frequencies and to molecules. This approach enables a wide range of high-accuracy measurements on molecules, both on rotational and, as we project, vibrational transitions.