http://chineseinput.net/에서 pinyin(병음)방식으로 중국어를 변환할 수 있습니다.
변환된 중국어를 복사하여 사용하시면 됩니다.
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.
Overexpression of the AtSTK Gene Increases Salt, PEG and ABA Tolerance in Arabidopsis
Lei Bing,Cui-Cui Feng,Jing-Lan Li,Xiao-Xu Li,Baocun Zhao,Yin-Zhu Shen,Zhan-Jing Huang,Rong-Chao Ge 한국식물학회 2013 Journal of Plant Biology Vol.56 No.6
AtSTK (At5g02800), which is a serine-threonineprotein kinase gene of Arabidopsis thaliana, was cloned, andits function was studied. The study found that the overexpressionof AtSTK could significantly improve the ability of A. thaliana to tolerate salt, PEG, and ABA stresses. RT-PCRanalysis revealed that the expression of the AtSTK genecould be obviously induced by salt, PEG, and ABA. Theexamination of the physiological characteristics showed thatthe overexpression of AtSTK in Arabidopsis significantlyreduced the plasma membrane permeability, significantlyincreased the proline content, and decreased the MDA content. These changes may reflect the physiological mechanismsthrough which AtSTK overexpression improves stress resistancein Arabidopsis. In addition, the overexpression of the AtSTKgene significantly antagonised the inhibitory effect of highconcentrations of exogenous ABA on Arabidopsis seedgermination. The subcellular localisation results showed thatAtSTK is located in both the cytosol and the nucleus. Theexamination of its tissue-specific expression showed thatAtSTK is expressed in various Arabidopsis tissues and isparticularly strongly expressed in the vessels. The signallingpathway analysis indicated that AtSTK might transfer thesalt stress signal in Arabidopsis through the MAPK pathway.
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>