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RISS 인기검색어
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- 저자 : Leib, Ryan D. (검색결과 5 건)
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Lei, B.,Shin, K.H.,Noh, D.Y.,Jo, I.H.,Koh, Y.H.,Kim, H.E.,Kim, S.E. Elsevier 2013 Materials science & engineering. C, Materials for Vol.33 No.3
This study investigated the effect of the addition of sol-gel derived nanoscale bioactive glass (NBG) particles on the mechanical properties and biological performances of PCL polymer, in order to evaluate the potential applications of PCL/NBG composites for bone tissue regeneration. Regardless of the NBG contents (10, 20, and 30wt.%), the NBG particles, which were synthesized through the sol-gel process using polyethylene glycol (PEG) polymer as a template, could be uniformly dispersed in the PCL matrix, while generating pores in the PCL/NBG composites. The elastic modulus of the PCL/NBG composites increased remarkably from 89+/-11MPa to 383+/-50MPa with increasing NBG content from 0 to 30wt.%, while still showing good ultimate tensile strength in the range of 15-19MPa. The hydrophilicity, water absorption and degradation behavior of the PCL/NBG composites were also enhanced by the addition of the NBG particles. Furthermore, the PCL/NBG composite with a NBG content of 30wt.% showed significantly enhanced in vitro bioactivity and cellular response compared to those of the pure PCL.
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Chun, B.S.,Kim, K.H.,Leibing, N.,Serrano-Guisan, S.,Schumacher, H.W.,Abid, M.,Chu, I.C.,Mryasov, O.N.,Kim, D.K.,Wu, H.C.,Hwang, C.,Kim, Y.K. Elsevier Science 2012 ACTA MATERIALIA Vol.60 No.19
We report the correlation between the crystalline structure, electronic structure and magnetic properties of Co<SUB>2</SUB>FeAl films as a function of growing temperature both experimentally and theoretically. The Co<SUB>2</SUB>FeAl film grown at room temperature is initially in the partially disordered B2 state, but then it gains a much higher ordered structure with increasing growing temperature due to its transition from short-range to long-range crystallographic order by surface diffusion. Electron energy loss spectroscopy measurements reveals that the increase in the I(L3)/I(L2) ratio of Co can be attributed to the enhanced ferromagnetic exchange interaction between neighboring Co atoms and the fact that the Co contribution is more dominant than the Fe contribution. As the growing temperature increases, many more unoccupied 3d states in Co are observed, hence the Gilbert damping constant increases due to a strong spin-orbit interaction. We also present the results of highly accurate quasiparticle self-consistent GW calculations and confirm that Co<SUB>2</SUB>FeAl in an ideal L2<SUB>1</SUB> structure is indeed a half-metal with a well-defined band gap in the minority spin channel.
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Structural and Functional Analysis of a β<sub>2</sub>-Adrenergic Receptor Complex with GRK5
Komolov, Konstantin E.,Du, Yang,Duc, Nguyen Minh,Betz, Robin M.,Rodrigues, Joã,o P.G.L.M.,Leib, Ryan D.,Patra, Dhabaleswar,Skiniotis, Georgios,Adams, Christopher M.,Dror, Ron O.,Chung, Ka Young Cell Press 2017 Cell Vol. No.
<P><B>Summary</B></P> <P>The phosphorylation of agonist-occupied G-protein-coupled receptors (GPCRs) by GPCR kinases (GRKs) functions to turn off G-protein signaling and turn on arrestin-mediated signaling. While a structural understanding of GPCR/G-protein and GPCR/arrestin complexes has emerged in recent years, the molecular architecture of a GPCR/GRK complex remains poorly defined. We used a comprehensive integrated approach of cross-linking, hydrogen-deuterium exchange mass spectrometry (MS), electron microscopy, mutagenesis, molecular dynamics simulations, and computational docking to analyze GRK5 interaction with the β<SUB>2</SUB>-adrenergic receptor (β<SUB>2</SUB>AR). These studies revealed a dynamic mechanism of complex formation that involves large conformational changes in the GRK5 RH/catalytic domain interface upon receptor binding. These changes facilitate contacts between intracellular loops 2 and 3 and the C terminus of the β<SUB>2</SUB>AR with the GRK5 RH bundle subdomain, membrane-binding surface, and kinase catalytic cleft, respectively. These studies significantly contribute to our understanding of the mechanism by which GRKs regulate the function of activated GPCRs.</P> <P><B>PaperClip</B></P> <P>Display Omitted</P> <P><B>Highlights</B></P> <P> <UL> <LI> GRK5-β<SUB>2</SUB>AR binding is enhanced by receptor and kinase ligands and acidic lipids </LI> <LI> GRK5 binding to the β<SUB>2</SUB>AR involves a multi-site interaction </LI> <LI> Receptor binding triggers substantial conformational changes in GRK5 </LI> <LI> RH/catalytic domain separation in GRK5 is essential for receptor phosphorylation </LI> </UL> </P> <P><B>Graphical Abstract</B></P> <P>[DISPLAY OMISSION]</P>
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