3,455 research outputs found
Observation of Topologically Stable 2D Skyrmions in an Antiferromagnetic Spinor Bose-Einstein Condensate
We present the creation and time evolution of two-dimensional Skyrmion
excitations in an antiferromagnetic spinor Bose-Einstein condensate. Using a
spin rotation method, the Skyrmion spin textures were imprinted on a sodium
condensate in a polar phase, where the two-dimensional Skyrmion is
topologically protected. The Skyrmion was observed to be stable on a short time
scale of a few tens of ms but to have dynamical instability to deform its shape
and eventually decay to a uniform spin texture. The deformed spin textures
reveal that the decay dynamics involves breaking the polar phase inside the
condensate without having topological charge density flow through the boundary
of the finite-sized sample. We discuss the possible formation of half-quantum
vortices in the deformation process.Comment: 5 pages, 5 figure
Protein kinase CK2 phosphorylates and activates p21-activated kinase 1
Activation of the p21-activated kinase 1 (PAK1) is achieved through a conformational change that converts an inactive PAK1 dimer to an active monomer. In this paper, we show that this change is necessary but not sufficient to activate PAK1 and that it is, rather, required for CK2-dependent PAK1S223 phosphorylation that converts a monomeric PAK1 into a catalytically active form. This phosphorylation appears to be essential for autophosphorylation at specific residues and overall activity of PAK1. A phosphomimetic mutation (S223E) bypasses the requirement for GTPases in PAK1 activation, whereas the constitutive activity of the PAK1 mutant (PAK1H83,86L), postulated to mimic GTPase-induced structural changes, is abolished by inhibition of S223 phosphorylation. Thus, S223 is likely accessible to CK2 upon conformational changes of PAK1 induced by GTPase-dependent and GTPase-independent stimuli, suggesting that S223 phosphorylation may play a key role in the final step of the PAK1 activation process. The physiological significance of this phosphorylation is reinforced by the observations that CK2 is responsible for epidermal growth factor–induced PAK1 activation and that inhibition of S223 phosphorylation abrogates PAK1-mediated malignant transformation of prostate epithelial cells. Taken together, these findings identify CK2 as an upstream activating kinase of PAK1, providing a novel mechanism for PAK1 activation
Evidence for a preformed Cooper pair model in the pseudogap spectra of a Ca10(Pt4As8)(Fe2As2)5 single crystal with a nodal superconducting gap
For high-Tc superconductors, clarifying the role and origin of the pseudogap
is essential for understanding the pairing mechanism. Among the various models
describing the pseudogap, the preformed Cooper pair model is a potential
candidate. Therefore, we present experimental evidence for the preformed Cooper
pair model by studying the pseudogap spectrum observed in the optical
conductivity of a Ca10(Pt4As8)(Fe2As2)5 (Tc = 34.6 K) single crystal. We
observed a clear pseudogap structure in the optical conductivity and observed
its temperature dependence. In the superconducting (SC) state, one SC gap with
a gap size of {\Delta} = 26 cm-1, a scattering rate of 1/{\tau} = 360 cm-1 and
a low-frequency extra Drude component were observed. Spectral weight analysis
revealed that the SC gap and pseudogap are formed from the same Drude band.
This means that the pseudogap is a gap structure observed as a result of a
continuous temperature evolution of the SC gap observed below Tc. This provides
clear experimental evidence for the preformed Cooper pair model.Comment: 15 pages, 4 figure
Institutional Investment Horizons and CEO Compensation
I investigate the relation between the structure of CEO compensation and
the investment horizons of a firms institutional investors and find results
consistent with the assertion that short-sighted institutions focus on shortterm
earnings leads firms to grant more options with higher sensitivity to
stock price. In contrast, the percentage holdings of long-term investors are
negatively correlated with the use of options and the sensitivity of total CEO
equity incentives to changes in stock price. Further results suggest that
firms with higher short-term institutional ownership are more concerned
about a negative earnings surprise and that when determining annual
bonuses, they punish their CEOs more severely. In total, the analyses
provide evidence that the investment horizon of institutional investors is
associated with firms CEO compensation policies.This work
was also supported by Research Settlement Fund for the new faculty of SNU
Relaxation of superfluid turbulence in highly oblate Bose-Einstein condensates
We investigate thermal relaxation of superfluid turbulence in a highly oblate
Bose-Einstein condensate. We generate turbulent flow in the condensate by
sweeping the center region of the condensate with a repulsive optical
potential. The turbulent condensate shows a spatially disordered distribution
of quantized vortices and the vortex number of the condensate exhibits
nonexponential decay behavior which we attribute to the vortex pair
annihilation. The vortex-antivortex collisions in the condensate are identified
with crescent-shaped, coalesced vortex cores. We observe that the
nonexponential decay of the vortex number is quantitatively well described by a
rate equation consisting of one-body and two-body decay terms. In our
measurement, we find that the local two-body decay rate is closely proportional
to , where is the temperature and is the chemical potential.Comment: 7 pages, 9 figure
The Role of the Pleckstrin Homology Domain-Containing Protein CKIP-1 in Activation of p21-activated Kinase 1 (PAK1)
Upon growth factor stimulation, PAK1 is recruited to the plasma membrane and activated by a mechanism that requires its phosphorylation at S223 by the protein kinase CK2. However, the upstream signaling molecules that regulate this phosphorylation event are not clearly defined. Here, we demonstrate a major role of the CK2α-interacting protein CKIP-1 in activation of PAK1. CK2α, CKIP-1 and PAK1 are translocated to membrane ruffles in response to the epidermal growth factor (EGF), where CKIP-1 mediates the interaction between CK2α, and PAK1 in a PI3K-dependent manner. Consistently, we observe that PAK1 mediates phosphorylation and modulation of the activity of p41-Arc, one of its plasma membrane substrate, in a fashion that requires PI3K and CKIP-1. Moreover, CKIP-1 knockdown or PI3K inhibition suppresses PAK1-mediated cell migration and invasion, demonstrating the physiological significance of the PI3K-CKIP-1-CK2α-PAK1 signaling pathway. Taken together, these findings identify a novel mechanism for the activation of PAK1 at the plasma membrane, which is critical for cell migration and invasion
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