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Koo, Bon-Chul,McKee, Christopher F.,Suh, Kyung-Won,Moon, Dae-Sik,Onaka, Takashi,Burton, Michael G.,Hiramatsu, Masaaki,Bessell, Michael S.,Gaensler, B. M.,Kim, Hyun-Jeong,Lee, Jae-Joon,Jeong, Woong-Seo IOP Publishing 2011 The Astrophysical journal Vol.732 No.1
<P>We report new mid-infrared (MIR) observations of the remarkable object IRAS 15099-5856 using the space telescopes AKARI and Spitzer, which demonstrate the presence of prominent crystalline silicate emission in this bright source. IRAS 15099-5856 has a complex morphology with a bright central compact source (IRS1) surrounded by knots, spurs, and several extended (similar to 4') arc-like filaments. The source is seen only at >= 10 mu m. The Spitzer mid-infrared spectrum of IRS1 shows prominent emission features from Mg-rich crystalline silicates, strong [Ne II] 12.81 mu m, and several other faint ionic lines. We model the MIR spectrum as thermal emission from dust and compare with the Herbig Be star HD 100546 and the luminous blue variable R71, which show very similar MIR spectra. Molecular line observations reveal two molecular clouds around the source, but no associated dense molecular cores. We suggest that IRS1 is heated by UV radiation from the adjacent O star Muzzio 10 and that its crystalline silicates most likely originated in a mass outflow from the progenitor of the supernova remnant (SNR) MSH 15-52. IRS1, which is embedded in the SNR, could have been shielded from the SN blast wave if the progenitor was in a close binary system with Muzzio 10. If MSH 15-52 is a remnant of Type Ib/c supernova (SN Ib/c), as has been previously proposed, this would confirm the binary model for SN Ib/c. IRS1 and the associated structures may be the relics of massive star death, as shaped by the supernova explosion, the pulsar wind, and the intense ionizing radiation of the embedded O star.</P>
황순욱(S. W. Hwang),최경호(G. H. Choi),박용헌(Sam. Park),R. Michael Ench,Alex M. Bate,이상철(S. C. Lee),권오성(O. S. Kwon),이동하(D. H. Lee) 한국태양에너지학회 2012 한국태양에너지학회 학술대회논문집 Vol.2012 No.3
Proton Exchange Membrane Fuel Cells (PEMFC) are the most appropriate for energy source of small robot applications. PEMFC has superior in power density and thermodynamic efficiency as compared with the Direct Methaol Fuel Cell (DMFC). Furthermore, PEMFC has lighter weight and smaller size than DMFC which are very important factors as small robot power system. The most significant factor of mobile robots is weight which relates closely with energy consumption and robot operation. This research tried to find optimum specifications in terms of type, number of cell, active area, cooling method, weight, and size. In order to find optimum 500W PEMFC, six options are designed in this paper and studied to reduce total stack weight by applying new materials and design innovations. However, still remaining problems are thermal management, robot space for energy sources, and so on. For a thermal management, design options need to analysis of Computational Fluid Dynamics (CFD) for determining which option has the improved performance and durability.
Van Nguyen, T.,Lee, J.,Sweredoski, Michael J.,Yang, S.J.,Jeon, S.J.,Harrison, Joseph S.,Yim, J.H.,Lee, S.,Handa, H.,Kuhlman, B.,Jeong, J.S.,Reitsma, Justin M.,Park, C.S.,Hess, S.,Deshaies, Raymond J. Cell Press 2016 Molecular cell Vol.61 No.6
<P>Cereblon (CRBN), a substrate receptor for the cullin-RING ubiquitin ligase 4 (CRL4) complex, is a direct protein target for thalidomide teratogenicity and antitumor activity of immunomodulatory drugs (IMiDs). Here we report that glutamine synthetase (GS) is an endogenous substrate of CRL4(CRBN). Upon exposing cells to high glutamine concentration, GS is acetylated at lysines 11 and 14, yielding a degron that is necessary and sufficient for binding and ubiquitylation by CRL4 CRBN and degradation by the proteasome. Binding of acetylated degron peptides to CRBN depends on an intact thalidomide-binding pocket but is not competitive with IMiDs. These findings reveal a feedback loop involving CRL4 CRBN that adjusts GS protein levels in response to glutamine and uncover a new function for lysine acetylation.</P>
Fabricating genetically engineered high-power lithium-ion batteries using multiple virus genes.
Lee, Yun Jung,Yi, Hyunjung,Kim, Woo-Jae,Kang, Kisuk,Yun, Dong Soo,Strano, Michael S,Ceder, Gerbrand,Belcher, Angela M American Association for the Advancement of Scienc 2009 Science Vol.324 No.5930
<P>Development of materials that deliver more energy at high rates is important for high-power applications, including portable electronic devices and hybrid electric vehicles. For lithium-ion (Li+) batteries, reducing material dimensions can boost Li+ ion and electron transfer in nanostructured electrodes. By manipulating two genes, we equipped viruses with peptide groups having affinity for single-walled carbon nanotubes (SWNTs) on one end and peptides capable of nucleating amorphous iron phosphate(a-FePO4) fused to the viral major coat protein. The virus clone with the greatest affinity toward SWNTs enabled power performance of a-FePO4 comparable to that of crystalline lithium iron phosphate (c-LiFePO4) and showed excellent capacity retention upon cycling at 1C. This environmentally benign low-temperature biological scaffold could facilitate fabrication of electrodes from materials previously excluded because of extremely low electronic conductivity.</P>
Nelson, Michael T,Joksovic, Pavle M,Su, Peihan,Kang, Ho-Won,Van Deusen, Amy,Baumgart, Joel P,David, Laurence S,Snutch, Terrance P,Barrett, Paula Q,Lee, Jung-Ha,Zorumski, Charles F,Perez-Reyes, Edward Society for Neuroscience 2007 The Journal of neuroscience Vol.27 No.46
<P>T-type Ca2+ channels (T-channels) are involved in the control of neuronal excitability and their gating can be modulated by a variety of redox agents. Ascorbate is an endogenous redox agent that can function as both an anti- and pro-oxidant. Here, we show that ascorbate selectively inhibits native Ca(v)3.2 T-channels in peripheral and central neurons, as well as recombinant Ca(v)3.2 channels heterologously expressed in human embryonic kidney 293 cells, by initiating the metal-catalyzed oxidation of a specific, metal-binding histidine residue in domain 1 of the channel. Our biophysical experiments indicate that ascorbate reduces the availability of Ca(v)3.2 channels over a wide range of membrane potentials, and inhibits Ca(v)3.2-dependent low-threshold-Ca2+ spikes as well as burst-firing in reticular thalamic neurons at physiologically relevant concentrations. This study represents the first mechanistic demonstration of ion channel modulation by ascorbate, and suggests that ascorbate may function as an endogenous modulator of neuronal excitability.</P>
Cand1 Promotes Assembly of New SCF Complexes through Dynamic Exchange of F Box Proteins
Pierce, Nathan W.,Lee, J.,Liu, X.,Sweredoski, Michael J.,Graham, Robert L.J.,Larimore, Elizabeth A.,Rome, M.,Zheng, N.,Clurman, Bruce E.,Hess, S.,Shan, S.o.,Deshaies, Raymond J. Cell Press ; MIT Press 2013 Cell Vol.153 No.1
The modular SCF (Skp1, cullin, and F box) ubiquitin ligases feature a large family of F box protein substrate receptors that enable recognition of diverse targets. However, how the repertoire of SCF complexes is sustained remains unclear. Real-time measurements of formation and disassembly indicate that SCF<SUP>Fbxw7</SUP> is extraordinarily stable, but, in the Nedd8-deconjugated state, the cullin-binding protein Cand1 augments its dissociation by one-million-fold. Binding and ubiquitylation assays show that Cand1 is a protein exchange factor that accelerates the rate at which Cul1-Rbx1 equilibrates with multiple F box protein-Skp1 modules. Depletion of Cand1 from cells impedes recruitment of new F box proteins to pre-existing Cul1 and profoundly alters the cellular landscape of SCF complexes. We suggest that catalyzed protein exchange may be a general feature of dynamic macromolecular machines and propose a hypothesis for how substrates, Nedd8, and Cand1 collaborate to regulate the cellular repertoire of SCF complexes.
황순욱,최경호,박용헌,이상철,권오성,이동하,Hwang, S.W.,Choi, G.H.,Park, Sam.,Ench, R. Michael,Bates, Alex M.,Lee, S.C.,Kwon, O.S.,Lee, D.H. 한국태양에너지학회 2012 한국태양에너지학회 논문집 Vol.32 No.suppl3
Proton Exchange Membrane Fuel Cells (PEMFC) are the most appropriate for energy source of small robot applications. PEMFC has superior in power density and thermodynamic efficiency as compared with the Direct Methaol Fuel Cell (DMFC). Furthermore, PEMFC has lighter weight and smaller size than DMFC which are very important factors as small robot power system. The most significant factor of mobile robots is weight which relates closely with energy consumption and robot operation. This research tried to find optimum specifications in terms of type, number of cell, active area, cooling method, weight, and size. In order to find optimum 500W PEMFC, six options are designed in this paper and studied to reduce total stack weight by applying new materials and design innovations. However, still remaining problems are thermal management, robot space for energy sources, and soon. For a thermal management, design options need to analysis of Computational Fluid Dynamics (CFD) for determining which option has the improved performance and durability.
Ghalali Aram,Wang Liangzhe,Stopsack Konrad H.,Rice James M.,Wu Shulin,Wu Chin-Lee,Zetter Bruce R.,Rogers Michael S. 생화학분자생물학회 2022 Experimental and molecular medicine Vol.54 No.-
The transcript encoding Antizyme Inhibitor 1 (AZIN1) is frequently edited in various cancers, and this editing is associated with enhanced tumor aggressiveness. After comparison of wild-type AZIN1 (wtAZIN1) and edited AZIN1 (edAZIN1, which contains a Ser367Gly substitution), we report differential binding of edAZIN1 to a small set of proteins; specifically, edAZIN1 binds to alpha-smooth muscle actin (ACTA2), gamma actin 1 (ACTG1), and myosin9, whereas wtAZIN1 does not. This binding enables nuclear translocation of edAZIN1. In contrast to overexpression of edAZIN1 and, to a lesser extent, (editable) wtAZIN1, overexpression of an uneditable AZIN1 allele does not promote a cellular phenotype associated with increased tumorigenicity. In patients, both editing and nuclear localization of AZIN1 are common and are associated with tumor aggressiveness, i.e., a higher Gleason score, higher genomic instability, and a shorter progression-free survival time. In conclusion, the data indicate that binding of edAZIN1 to the actin/myosin9 complex supports its nuclear translocation, leading to enhanced cellular aggressiveness, and is associated with worse prostate cancer outcomes.